eF-site ID 1s26-ABCDEF PDB Code 1s26 Chain A, B, C, D, E, F click to enlarge Title Structure of Anthrax Edema Factor-Calmodulin-alpha,beta-methyleneadenosine 5'-triphosphate Complex Reveals an Alternative Mode of ATP Binding to the Catalytic Site Classification TOXIN,LYASE/METAL BINDING PROTEIN Compound Calmodulin-sensitive adenylate cyclase Source (CALM_HUMAN) Sequence A:  RIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPV NKLATNLIKSGVATKGLNVHGKSSDWGPVAGYIPFDQDLS KKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIE ELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENN EVQYKTKEGKITVLGEKFNWRNIEVMAKNVEGVLKPLTAD YDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTN LLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTG GDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMT GRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITK AKINTIPTSAEFIKNLSSIRRSSSVKKIAGYLSDYYNSAN HIFSQEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYF QYLKERITNQVQLLLTHQKFKLLYKQLNFTENETDNFEVF QKIID B:  DVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNK LATNLIKSGVATKGLNVHGKSSDWGPVAGYIPFDQDLSKK HGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEEL KENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEV QYKTKEGKITVLGEKFNWRNIEVMAKNVEGVLKPLTADYD LFALAPSLTEIKKQIPQKEWDKVVNTPNEKQKGVTNLLIK YGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVV NHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMTGRFI EKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAKIN TIPSVKKIAGYLSDYYNSANHIFSQEKKRKISIFRGIQAY NEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKF KLLYKQLNFTENETDNFEVFQKIID C:  RIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPV NKLATNLIKSGVATKGLNVHGKSSDWGPVAGYIPFDQDLS KKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIE ELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENN EVQYKTKEGKITVLGEKFNWRNIEVMAKNVEGVLKPLTAD YDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTN LLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTG GDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMT GRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITK AKINTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKK ESVKKIAGYLSDYYNSANHIFSQEKKRKISIFRGIQAYNE IENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKFKL LYKQLNFTENETDNFEVFQKIID D:  TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPT EAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEE IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM IREADIDGDGQVNYEEFVQMMTA E:  TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPT EAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEE IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM IREADIDGDGQVNYEEFVQMMTA F:  TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPT EAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEE IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM IREADIDGDGQVNYEEFVQMMTA Description Functional site 1) chain D residue 129 type sequence D description BINDING SITE FOR RESIDUE CA D 800 source : AC1 2) chain D residue 131 type sequence D description BINDING SITE FOR RESIDUE CA D 800 source : AC1 3) chain D residue 133 type sequence D description BINDING SITE FOR RESIDUE CA D 800 source : AC1 4) chain D residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA D 800 source : AC1 5) chain D residue 140 type sequence E description BINDING SITE FOR RESIDUE CA D 800 source : AC1 6) chain D residue 93 type sequence D description BINDING SITE FOR RESIDUE CA D 801 source : AC2 7) chain D residue 95 type sequence D description BINDING SITE FOR RESIDUE CA D 801 source : AC2 8) chain D residue 97 type sequence N description BINDING SITE FOR RESIDUE CA D 801 source : AC2 9) chain D residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA D 801 source : AC2 10) chain D residue 104 type sequence E description BINDING SITE FOR RESIDUE CA D 801 source : AC2 11) chain E residue 129 type sequence D description BINDING SITE FOR RESIDUE CA E 802 source : AC3 12) chain E residue 131 type sequence D description BINDING SITE FOR RESIDUE CA E 802 source : AC3 13) chain E residue 133 type sequence D description BINDING SITE FOR RESIDUE CA E 802 source : AC3 14) chain E residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA E 802 source : AC3 15) chain E residue 140 type sequence E description BINDING SITE FOR RESIDUE CA E 802 source : AC3 16) chain E residue 93 type sequence D description BINDING SITE FOR RESIDUE CA E 803 source : AC4 17) chain E residue 95 type sequence D description BINDING SITE FOR RESIDUE CA E 803 source : AC4 18) chain E residue 97 type sequence N description BINDING SITE FOR RESIDUE CA E 803 source : AC4 19) chain E residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA E 803 source : AC4 20) chain E residue 104 type sequence E description BINDING SITE FOR RESIDUE CA E 803 source : AC4 21) chain F residue 131 type sequence D description BINDING SITE FOR RESIDUE CA F 804 source : AC5 22) chain F residue 133 type sequence D description BINDING SITE FOR RESIDUE CA F 804 source : AC5 23) chain F residue 135 type sequence Q description BINDING SITE FOR RESIDUE CA F 804 source : AC5 24) chain F residue 140 type sequence E description BINDING SITE FOR RESIDUE CA F 804 source : AC5 25) chain F residue 93 type sequence D description BINDING SITE FOR RESIDUE CA F 805 source : AC6 26) chain F residue 95 type sequence D description BINDING SITE FOR RESIDUE CA F 805 source : AC6 27) chain F residue 97 type sequence N description BINDING SITE FOR RESIDUE CA F 805 source : AC6 28) chain F residue 99 type sequence Y description BINDING SITE FOR RESIDUE CA F 805 source : AC6 29) chain F residue 104 type sequence E description BINDING SITE FOR RESIDUE CA F 805 source : AC6 30) chain A residue 491 type sequence D description BINDING SITE FOR RESIDUE YB A 901 source : AC7 31) chain A residue 493 type sequence D description BINDING SITE FOR RESIDUE YB A 901 source : AC7 32) chain A residue 577 type sequence H description BINDING SITE FOR RESIDUE YB A 901 source : AC7 33) chain B residue 491 type sequence D description BINDING SITE FOR RESIDUE YB B 902 source : AC8 34) chain B residue 493 type sequence D description BINDING SITE FOR RESIDUE YB B 902 source : AC8 35) chain B residue 577 type sequence H description BINDING SITE FOR RESIDUE YB B 902 source : AC8 36) chain C residue 491 type sequence D description BINDING SITE FOR RESIDUE YB C 903 source : AC9 37) chain C residue 493 type sequence D description BINDING SITE FOR RESIDUE YB C 903 source : AC9 38) chain C residue 577 type sequence H description BINDING SITE FOR RESIDUE YB C 903 source : AC9 39) chain A residue 329 type sequence R description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 40) chain A residue 346 type sequence K description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 41) chain A residue 351 type sequence H description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 42) chain A residue 353 type sequence K description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 43) chain A residue 354 type sequence S description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 44) chain A residue 372 type sequence K description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 45) chain A residue 382 type sequence K description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 46) chain A residue 386 type sequence E description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 47) chain A residue 493 type sequence D description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 48) chain A residue 583 type sequence N description BINDING SITE FOR RESIDUE APC A 1139 source : BC1 49) chain B residue 329 type sequence R description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 50) chain B residue 346 type sequence K description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 51) chain B residue 351 type sequence H description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 52) chain B residue 352 type sequence G description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 53) chain B residue 354 type sequence S description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 54) chain B residue 372 type sequence K description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 55) chain B residue 382 type sequence K description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 56) chain B residue 490 type sequence A description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 57) chain B residue 491 type sequence D description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 58) chain B residue 493 type sequence D description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 59) chain B residue 583 type sequence N description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 60) chain B residue 586 type sequence F description BINDING SITE FOR RESIDUE APC B 2139 source : BC2 61) chain C residue 329 type sequence R description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 62) chain C residue 346 type sequence K description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 63) chain C residue 351 type sequence H description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 64) chain C residue 353 type sequence K description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 65) chain C residue 354 type sequence S description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 66) chain C residue 372 type sequence K description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 67) chain C residue 583 type sequence N description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 68) chain C residue 586 type sequence F description BINDING SITE FOR RESIDUE APC C 3139 source : BC3 69) chain D residue 111 type MOD_RES sequence N description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 70) chain E residue 111 type MOD_RES sequence N description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 71) chain F residue 111 type MOD_RES sequence N description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 72) chain D residue 116 type MOD_RES sequence L description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 73) chain E residue 116 type MOD_RES sequence L description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 74) chain F residue 116 type MOD_RES sequence L description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI11 75) chain D residue 21 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 76) chain D residue 68 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 77) chain E residue 21 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 78) chain E residue 23 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 79) chain E residue 25 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 80) chain E residue 27 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 81) chain E residue 32 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 82) chain E residue 57 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 83) chain E residue 59 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 84) chain E residue 61 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 85) chain E residue 63 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 86) chain D residue 23 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 87) chain E residue 68 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 88) chain F residue 21 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 89) chain F residue 23 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 90) chain F residue 25 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 91) chain F residue 27 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 92) chain F residue 32 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 93) chain F residue 57 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 94) chain F residue 59 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 95) chain F residue 61 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 96) chain F residue 63 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 97) chain D residue 25 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 98) chain F residue 68 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 99) chain D residue 27 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 100) chain D residue 32 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 101) chain D residue 57 type BINDING sequence A description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 102) chain D residue 59 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 103) chain D residue 61 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 104) chain D residue 63 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI1 105) chain D residue 139 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 106) chain E residue 139 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 107) chain F residue 139 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI12 108) chain D residue 22 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 source Swiss-Prot : SWS_FT_FI13 109) chain E residue 22 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 source Swiss-Prot : SWS_FT_FI13 110) chain F residue 22 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 source Swiss-Prot : SWS_FT_FI13 111) chain D residue 82 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 112) chain E residue 82 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 113) chain F residue 82 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 114) chain D residue 95 type MOD_RES sequence D description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 115) chain E residue 95 type MOD_RES sequence D description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 116) chain F residue 95 type MOD_RES sequence D description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 117) chain D residue 100 type MOD_RES sequence I description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 118) chain E residue 100 type MOD_RES sequence I description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 119) chain F residue 100 type MOD_RES sequence I description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI8 120) chain D residue 102 type MOD_RES sequence A description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 121) chain E residue 102 type MOD_RES sequence A description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 122) chain F residue 102 type MOD_RES sequence A description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 123) chain D residue 94 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 124) chain D residue 141 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 125) chain E residue 94 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 126) chain E residue 96 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 127) chain E residue 98 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 128) chain E residue 100 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 129) chain E residue 105 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 130) chain E residue 130 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 131) chain E residue 132 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 132) chain E residue 134 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 133) chain E residue 136 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 134) chain D residue 96 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 135) chain E residue 141 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 136) chain F residue 94 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 137) chain F residue 96 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 138) chain F residue 98 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 139) chain F residue 100 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 140) chain F residue 105 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 141) chain F residue 130 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 142) chain F residue 132 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 143) chain F residue 134 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 144) chain F residue 136 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 145) chain D residue 98 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 146) chain F residue 141 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 147) chain D residue 100 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 148) chain D residue 105 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 149) chain D residue 130 type BINDING sequence I description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 150) chain D residue 132 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 151) chain D residue 134 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 152) chain D residue 136 type BINDING sequence V description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03 source Swiss-Prot : SWS_FT_FI2 153) chain D residue 22 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 154) chain E residue 22 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 155) chain F residue 22 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 156) chain D residue 45 type MOD_RES sequence E description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 157) chain E residue 45 type MOD_RES sequence E description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 158) chain F residue 45 type MOD_RES sequence E description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29 source Swiss-Prot : SWS_FT_FI5 159) chain D residue 20-32 type prosite sequence DKDGDGTITTKEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 160) chain D residue 56-68 type prosite sequence DADGNGTIDFPEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 161) chain D residue 93-105 type prosite sequence DKDGNGYISAAEL description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018 162) chain D residue 129-141 type prosite sequence DIDGDGQVNYEEF description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL source prosite : PS00018

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