eF-site ID 4wyb-ABCDEFGHIJKLMNOPQRSTUVXY PDB Code 4wyb Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, X, Y Title Structure of the Bud6 flank domain in complex with actin Classification CONTRACTILE PROTEIN/PROTEIN BINDING Compound Actin, alpha skeletal muscle Source ORGANISM_COMMON: Rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus; Sequence A:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVH B:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERKL C:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR D:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMER E:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR F:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME G:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRDSYVG DEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELR VAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVA IQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAI MRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEK LCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERF RCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYA NNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPER KYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVH H:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME I:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR J:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMERK K:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVH L:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME M:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR N:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME O:  ALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYVGD EAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRV APEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAI QAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIM RLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKL CYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFR CPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYAN NVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERK YSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVH P:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME Q:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVH R:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME S:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR T:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEMER U:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR V:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME X:  TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHDSYV GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNEL RVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYV AIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHA IMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLY ANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE RKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHR Y:  TFNQVREQVMVAVQSLNPDHDSRVEAIDKAEKMWEME Description Functional site 1) chain A residue 13 type sequence G description binding site for residue ATP A 401 source : AC1 2) chain A residue 14 type sequence S description binding site for residue ATP A 401 source : AC1 3) chain A residue 15 type sequence G description binding site for residue ATP A 401 source : AC1 4) chain A residue 16 type sequence L description binding site for residue ATP A 401 source : AC1 5) chain A residue 18 type sequence K description binding site for residue ATP A 401 source : AC1 6) chain A residue 156 type sequence G description binding site for residue ATP A 401 source : AC1 7) chain A residue 157 type sequence D description binding site for residue ATP A 401 source : AC1 8) chain A residue 158 type sequence G description binding site for residue ATP A 401 source : AC1 9) chain A residue 159 type sequence V description binding site for residue ATP A 401 source : AC1 10) chain A residue 182 type sequence G description binding site for residue ATP A 401 source : AC1 11) chain A residue 210 type sequence R description binding site for residue ATP A 401 source : AC1 12) chain A residue 213 type sequence K description binding site for residue ATP A 401 source : AC1 13) chain A residue 214 type sequence E description binding site for residue ATP A 401 source : AC1 14) chain A residue 301 type sequence G description binding site for residue ATP A 401 source : AC1 15) chain A residue 302 type sequence G description binding site for residue ATP A 401 source : AC1 16) chain A residue 303 type sequence T description binding site for residue ATP A 401 source : AC1 17) chain A residue 305 type sequence M description binding site for residue ATP A 401 source : AC1 18) chain A residue 306 type sequence Y description binding site for residue ATP A 401 source : AC1 19) chain A residue 336 type sequence K description binding site for residue ATP A 401 source : AC1 20) chain A residue 137 type sequence Q description binding site for residue CA A 402 source : AC2 21) chain C residue 13 type sequence G description binding site for residue ATP C 401 source : AC3 22) chain C residue 14 type sequence S description binding site for residue ATP C 401 source : AC3 23) chain C residue 15 type sequence G description binding site for residue ATP C 401 source : AC3 24) chain C residue 16 type sequence L description binding site for residue ATP C 401 source : AC3 25) chain C residue 18 type sequence K description binding site for residue ATP C 401 source : AC3 26) chain C residue 156 type sequence G description binding site for residue ATP C 401 source : AC3 27) chain C residue 157 type sequence D description binding site for residue ATP C 401 source : AC3 28) chain C residue 158 type sequence G description binding site for residue ATP C 401 source : AC3 29) chain C residue 159 type sequence V description binding site for residue ATP C 401 source : AC3 30) chain C residue 213 type sequence K description binding site for residue ATP C 401 source : AC3 31) chain C residue 214 type sequence E description binding site for residue ATP C 401 source : AC3 32) chain C residue 302 type sequence G description binding site for residue ATP C 401 source : AC3 33) chain C residue 306 type sequence Y description binding site for residue ATP C 401 source : AC3 34) chain C residue 137 type sequence Q description binding site for residue CA C 402 source : AC4 35) chain E residue 13 type sequence G description binding site for residue ATP E 401 source : AC5 36) chain E residue 14 type sequence S description binding site for residue ATP E 401 source : AC5 37) chain E residue 15 type sequence G description binding site for residue ATP E 401 source : AC5 38) chain E residue 16 type sequence L description binding site for residue ATP E 401 source : AC5 39) chain E residue 18 type sequence K description binding site for residue ATP E 401 source : AC5 40) chain E residue 156 type sequence G description binding site for residue ATP E 401 source : AC5 41) chain E residue 157 type sequence D description binding site for residue ATP E 401 source : AC5 42) chain E residue 158 type sequence G description binding site for residue ATP E 401 source : AC5 43) chain E residue 159 type sequence V description binding site for residue ATP E 401 source : AC5 44) chain E residue 210 type sequence R description binding site for residue ATP E 401 source : AC5 45) chain E residue 213 type sequence K description binding site for residue ATP E 401 source : AC5 46) chain E residue 214 type sequence E description binding site for residue ATP E 401 source : AC5 47) chain E residue 302 type sequence G description binding site for residue ATP E 401 source : AC5 48) chain E residue 306 type sequence Y description binding site for residue ATP E 401 source : AC5 49) chain E residue 336 type sequence K description binding site for residue ATP E 401 source : AC5 50) chain E residue 137 type sequence Q description binding site for residue CA E 402 source : AC6 51) chain G residue 13 type sequence G description binding site for residue ATP G 401 source : AC7 52) chain G residue 14 type sequence S description binding site for residue ATP G 401 source : AC7 53) chain G residue 15 type sequence G description binding site for residue ATP G 401 source : AC7 54) chain G residue 16 type sequence L description binding site for residue ATP G 401 source : AC7 55) chain G residue 18 type sequence K description binding site for residue ATP G 401 source : AC7 56) chain G residue 156 type sequence G description binding site for residue ATP G 401 source : AC7 57) chain G residue 157 type sequence D description binding site for residue ATP G 401 source : AC7 58) chain G residue 158 type sequence G description binding site for residue ATP G 401 source : AC7 59) chain G residue 159 type sequence V description binding site for residue ATP G 401 source : AC7 60) chain G residue 182 type sequence G description binding site for residue ATP G 401 source : AC7 61) chain G residue 213 type sequence K description binding site for residue ATP G 401 source : AC7 62) chain G residue 214 type sequence E description binding site for residue ATP G 401 source : AC7 63) chain G residue 301 type sequence G description binding site for residue ATP G 401 source : AC7 64) chain G residue 302 type sequence G description binding site for residue ATP G 401 source : AC7 65) chain G residue 303 type sequence T description binding site for residue ATP G 401 source : AC7 66) chain G residue 305 type sequence M description binding site for residue ATP G 401 source : AC7 67) chain G residue 306 type sequence Y description binding site for residue ATP G 401 source : AC7 68) chain G residue 336 type sequence K description binding site for residue ATP G 401 source : AC7 69) chain G residue 137 type sequence Q description binding site for residue CA G 402 source : AC8 70) chain I residue 13 type sequence G description binding site for residue ATP I 401 source : AC9 71) chain I residue 14 type sequence S description binding site for residue ATP I 401 source : AC9 72) chain I residue 15 type sequence G description binding site for residue ATP I 401 source : AC9 73) chain I residue 16 type sequence L description binding site for residue ATP I 401 source : AC9 74) chain I residue 18 type sequence K description binding site for residue ATP I 401 source : AC9 75) chain I residue 156 type sequence G description binding site for residue ATP I 401 source : AC9 76) chain I residue 157 type sequence D description binding site for residue ATP I 401 source : AC9 77) chain I residue 158 type sequence G description binding site for residue ATP I 401 source : AC9 78) chain I residue 159 type sequence V description binding site for residue ATP I 401 source : AC9 79) chain I residue 182 type sequence G description binding site for residue ATP I 401 source : AC9 80) chain I residue 213 type sequence K description binding site for residue ATP I 401 source : AC9 81) chain I residue 214 type sequence E description binding site for residue ATP I 401 source : AC9 82) chain I residue 302 type sequence G description binding site for residue ATP I 401 source : AC9 83) chain I residue 303 type sequence T description binding site for residue ATP I 401 source : AC9 84) chain I residue 305 type sequence M description binding site for residue ATP I 401 source : AC9 85) chain I residue 306 type sequence Y description binding site for residue ATP I 401 source : AC9 86) chain I residue 336 type sequence K description binding site for residue ATP I 401 source : AC9 87) chain I residue 137 type sequence Q description binding site for residue CA I 402 source : AD1 88) chain K residue 13 type sequence G description binding site for residue ATP K 401 source : AD2 89) chain K residue 14 type sequence S description binding site for residue ATP K 401 source : AD2 90) chain K residue 15 type sequence G description binding site for residue ATP K 401 source : AD2 91) chain K residue 16 type sequence L description binding site for residue ATP K 401 source : AD2 92) chain K residue 156 type sequence G description binding site for residue ATP K 401 source : AD2 93) chain K residue 157 type sequence D description binding site for residue ATP K 401 source : AD2 94) chain K residue 158 type sequence G description binding site for residue ATP K 401 source : AD2 95) chain K residue 159 type sequence V description binding site for residue ATP K 401 source : AD2 96) chain K residue 182 type sequence G description binding site for residue ATP K 401 source : AD2 97) chain K residue 213 type sequence K description binding site for residue ATP K 401 source : AD2 98) chain K residue 214 type sequence E description binding site for residue ATP K 401 source : AD2 99) chain K residue 302 type sequence G description binding site for residue ATP K 401 source : AD2 100) chain K residue 303 type sequence T description binding site for residue ATP K 401 source : AD2 101) chain K residue 305 type sequence M description binding site for residue ATP K 401 source : AD2 102) chain K residue 306 type sequence Y description binding site for residue ATP K 401 source : AD2 103) chain K residue 137 type sequence Q description binding site for residue CA K 402 source : AD3 104) chain M residue 13 type sequence G description binding site for residue ATP M 401 source : AD4 105) chain M residue 14 type sequence S description binding site for residue ATP M 401 source : AD4 106) chain M residue 15 type sequence G description binding site for residue ATP M 401 source : AD4 107) chain M residue 16 type sequence L description binding site for residue ATP M 401 source : AD4 108) chain M residue 18 type sequence K description binding site for residue ATP M 401 source : AD4 109) chain M residue 156 type sequence G description binding site for residue ATP M 401 source : AD4 110) chain M residue 157 type sequence D description binding site for residue ATP M 401 source : AD4 111) chain M residue 158 type sequence G description binding site for residue ATP M 401 source : AD4 112) chain M residue 159 type sequence V description binding site for residue ATP M 401 source : AD4 113) chain M residue 213 type sequence K description binding site for residue ATP M 401 source : AD4 114) chain M residue 214 type sequence E description binding site for residue ATP M 401 source : AD4 115) chain M residue 302 type sequence G description binding site for residue ATP M 401 source : AD4 116) chain M residue 305 type sequence M description binding site for residue ATP M 401 source : AD4 117) chain M residue 306 type sequence Y description binding site for residue ATP M 401 source : AD4 118) chain M residue 336 type sequence K description binding site for residue ATP M 401 source : AD4 119) chain M residue 137 type sequence Q description binding site for residue CA M 402 source : AD5 120) chain O residue 13 type sequence G description binding site for residue ATP O 401 source : AD6 121) chain O residue 14 type sequence S description binding site for residue ATP O 401 source : AD6 122) chain O residue 15 type sequence G description binding site for residue ATP O 401 source : AD6 123) chain O residue 16 type sequence L description binding site for residue ATP O 401 source : AD6 124) chain O residue 18 type sequence K description binding site for residue ATP O 401 source : AD6 125) chain O residue 156 type sequence G description binding site for residue ATP O 401 source : AD6 126) chain O residue 157 type sequence D description binding site for residue ATP O 401 source : AD6 127) chain O residue 158 type sequence G description binding site for residue ATP O 401 source : AD6 128) chain O residue 159 type sequence V description binding site for residue ATP O 401 source : AD6 129) chain O residue 213 type sequence K description binding site for residue ATP O 401 source : AD6 130) chain O residue 214 type sequence E description binding site for residue ATP O 401 source : AD6 131) chain O residue 302 type sequence G description binding site for residue ATP O 401 source : AD6 132) chain O residue 303 type sequence T description binding site for residue ATP O 401 source : AD6 133) chain O residue 305 type sequence M description binding site for residue ATP O 401 source : AD6 134) chain O residue 306 type sequence Y description binding site for residue ATP O 401 source : AD6 135) chain O residue 137 type sequence Q description binding site for residue CA O 402 source : AD7 136) chain Q residue 13 type sequence G description binding site for residue ATP Q 401 source : AD8 137) chain Q residue 14 type sequence S description binding site for residue ATP Q 401 source : AD8 138) chain Q residue 15 type sequence G description binding site for residue ATP Q 401 source : AD8 139) chain Q residue 16 type sequence L description binding site for residue ATP Q 401 source : AD8 140) chain Q residue 18 type sequence K description binding site for residue ATP Q 401 source : AD8 141) chain Q residue 156 type sequence G description binding site for residue ATP Q 401 source : AD8 142) chain Q residue 157 type sequence D description binding site for residue ATP Q 401 source : AD8 143) chain Q residue 158 type sequence G description binding site for residue ATP Q 401 source : AD8 144) chain Q residue 159 type sequence V description binding site for residue ATP Q 401 source : AD8 145) chain Q residue 182 type sequence G description binding site for residue ATP Q 401 source : AD8 146) chain Q residue 213 type sequence K description binding site for residue ATP Q 401 source : AD8 147) chain Q residue 214 type sequence E description binding site for residue ATP Q 401 source : AD8 148) chain Q residue 302 type sequence G description binding site for residue ATP Q 401 source : AD8 149) chain Q residue 303 type sequence T description binding site for residue ATP Q 401 source : AD8 150) chain Q residue 305 type sequence M description binding site for residue ATP Q 401 source : AD8 151) chain Q residue 306 type sequence Y description binding site for residue ATP Q 401 source : AD8 152) chain Q residue 137 type sequence Q description binding site for residue CA Q 402 source : AD9 153) chain S residue 13 type sequence G description binding site for residue ATP S 401 source : AE1 154) chain S residue 14 type sequence S description binding site for residue ATP S 401 source : AE1 155) chain S residue 15 type sequence G description binding site for residue ATP S 401 source : AE1 156) chain S residue 16 type sequence L description binding site for residue ATP S 401 source : AE1 157) chain S residue 18 type sequence K description binding site for residue ATP S 401 source : AE1 158) chain S residue 156 type sequence G description binding site for residue ATP S 401 source : AE1 159) chain S residue 157 type sequence D description binding site for residue ATP S 401 source : AE1 160) chain S residue 158 type sequence G description binding site for residue ATP S 401 source : AE1 161) chain S residue 159 type sequence V description binding site for residue ATP S 401 source : AE1 162) chain S residue 213 type sequence K description binding site for residue ATP S 401 source : AE1 163) chain S residue 214 type sequence E description binding site for residue ATP S 401 source : AE1 164) chain S residue 302 type sequence G description binding site for residue ATP S 401 source : AE1 165) chain S residue 303 type sequence T description binding site for residue ATP S 401 source : AE1 166) chain S residue 305 type sequence M description binding site for residue ATP S 401 source : AE1 167) chain S residue 306 type sequence Y description binding site for residue ATP S 401 source : AE1 168) chain S residue 336 type sequence K description binding site for residue ATP S 401 source : AE1 169) chain S residue 137 type sequence Q description binding site for residue CA S 402 source : AE2 170) chain U residue 13 type sequence G description binding site for residue ATP U 401 source : AE3 171) chain U residue 14 type sequence S description binding site for residue ATP U 401 source : AE3 172) chain U residue 15 type sequence G description binding site for residue ATP U 401 source : AE3 173) chain U residue 16 type sequence L description binding site for residue ATP U 401 source : AE3 174) chain U residue 18 type sequence K description binding site for residue ATP U 401 source : AE3 175) chain U residue 156 type sequence G description binding site for residue ATP U 401 source : AE3 176) chain U residue 157 type sequence D description binding site for residue ATP U 401 source : AE3 177) chain U residue 158 type sequence G description binding site for residue ATP U 401 source : AE3 178) chain U residue 159 type sequence V description binding site for residue ATP U 401 source : AE3 179) chain U residue 182 type sequence G description binding site for residue ATP U 401 source : AE3 180) chain U residue 213 type sequence K description binding site for residue ATP U 401 source : AE3 181) chain U residue 214 type sequence E description binding site for residue ATP U 401 source : AE3 182) chain U residue 302 type sequence G description binding site for residue ATP U 401 source : AE3 183) chain U residue 303 type sequence T description binding site for residue ATP U 401 source : AE3 184) chain U residue 306 type sequence Y description binding site for residue ATP U 401 source : AE3 185) chain U residue 336 type sequence K description binding site for residue ATP U 401 source : AE3 186) chain U residue 137 type sequence Q description binding site for residue CA U 402 source : AE4 187) chain X residue 13 type sequence G description binding site for residue ATP X 401 source : AE5 188) chain X residue 14 type sequence S description binding site for residue ATP X 401 source : AE5 189) chain X residue 15 type sequence G description binding site for residue ATP X 401 source : AE5 190) chain X residue 16 type sequence L description binding site for residue ATP X 401 source : AE5 191) chain X residue 18 type sequence K description binding site for residue ATP X 401 source : AE5 192) chain X residue 156 type sequence G description binding site for residue ATP X 401 source : AE5 193) chain X residue 157 type sequence D description binding site for residue ATP X 401 source : AE5 194) chain X residue 158 type sequence G description binding site for residue ATP X 401 source : AE5 195) chain X residue 159 type sequence V description binding site for residue ATP X 401 source : AE5 196) chain X residue 182 type sequence G description binding site for residue ATP X 401 source : AE5 197) chain X residue 213 type sequence K description binding site for residue ATP X 401 source : AE5 198) chain X residue 214 type sequence E description binding site for residue ATP X 401 source : AE5 199) chain X residue 302 type sequence G description binding site for residue ATP X 401 source : AE5 200) chain X residue 303 type sequence T description binding site for residue ATP X 401 source : AE5 201) chain X residue 305 type sequence M description binding site for residue ATP X 401 source : AE5 202) chain X residue 306 type sequence Y description binding site for residue ATP X 401 source : AE5 203) chain X residue 336 type sequence K description binding site for residue ATP X 401 source : AE5 204) chain X residue 137 type sequence Q description binding site for residue CA X 402 source : AE6 205) chain A residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 206) chain S residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 207) chain U residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 208) chain X residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 209) chain C residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 210) chain E residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 211) chain G residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 212) chain I residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 213) chain K residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 214) chain M residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 215) chain O residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 216) chain Q residue 61 type MOD_RES sequence K description N6-malonyllysine => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 217) chain A residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 218) chain S residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 219) chain U residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 220) chain X residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 221) chain C residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 222) chain E residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 223) chain G residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 224) chain I residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 225) chain K residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 226) chain M residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 227) chain O residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 228) chain Q residue 73 type MOD_RES sequence H description Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK source Swiss-Prot : SWS_FT_FI5 229) chain A residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 230) chain S residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 231) chain U residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 232) chain X residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 233) chain C residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 234) chain E residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 235) chain G residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 236) chain I residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 237) chain K residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 238) chain M residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 239) chain O residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 240) chain Q residue 84 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68133 source Swiss-Prot : SWS_FT_FI6 241) chain A residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 242) chain S residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 243) chain U residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 244) chain X residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 245) chain C residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 246) chain E residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 247) chain G residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 248) chain I residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 249) chain K residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 250) chain M residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 251) chain O residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 252) chain Q residue 177 type MOD_RES sequence R description ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 source Swiss-Prot : SWS_FT_FI7 253) chain A residue 53-63 type prosite sequence YVGDEAQSKRG description ACTINS_1 Actins signature 1. YVGDEAQs.KRG source prosite : PS00406 254) chain A residue 356-364 type prosite sequence WITKQEYDE description ACTINS_2 Actins signature 2. WITKqEYDE source prosite : PS00432 255) chain A residue 104-116 type prosite sequence LLTEAPLNPKANR description ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR source prosite : PS01132

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