eF-site ID 3zry-ABCDEFGHIJKLMNOPQRS PDB Code 3zry Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S click to enlarge Title Rotor architecture in the F(1)-c(10)-ring complex of the yeast F-ATP synthase Classification HYDROLASE Compound ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; Sequence A:  NLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMA LNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGL LGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVH EPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTI LNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQH DAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKH ALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHS RLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVI SITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAL KQVAGSLKLFLAQYREVAAFAQSDLDASTKQTLVRGERLT QLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFE SSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFV ATF B:  ANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGM ALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPG LLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSV HEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDT ILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQ HDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGK HALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLH SRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNV ISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKA LKQVAGSLKLFLAQYREVAAFAQSDLDASTKQTLVRGERL TQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEF ESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESF VATF C:  NLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMA LNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGL LGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVH EPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTI LNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQH DAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKH ALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHS RLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVI SITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAL KQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGER LTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGE FESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATES FVATF D:  STPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGK LVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISV PVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFA EQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTV FIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETG VINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTL ATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATT FAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQ EHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVE RARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVL EGKYDNIPEHAFYMVGGIEDVVAKAEKLAAE E:  PITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLV LEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPV GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQ STSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFI QELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVI NLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEE GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT DMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFA HLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEH YDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERA RKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEG KYDNIPEHAFYMVGGIEDVVAKAEKLAAE F:  TPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKL VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVP VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAE QSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVF IQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGV INLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDE EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLA TDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTF AHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQE HYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVER ARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLE GKYDNIPEHAFYMVGGIEDVVAKAEKLAAE G:  ATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKIS AKKMDEAEQLFYKNAETKNKELIVAITSDKGLCGSIHSQL AKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSIN GIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVS SLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFE YTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRY SILYNRTRQAVITNELVDIITGASSL H:  LQFALPHETLYSEVTQVNLPAKSGRIGVLANHVPTVEQLL PGVVEVMEGSNSKKFFISGGFATVQPDSQLCVTAIEAPLE SFSENIKNLLAEAKKNVSSSREAAEAAIQVEVLENLQSV I:  MSYAAYLNVAAQAIRSSTELQTASVTNRSQTDAFYTQYKN ASEPTPMTK J:  QLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRNP SIKDTVFPMAILGFALSEATGLFCLMVSFLLLF K:  LVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRNPS IKDTVFPMAILGFALSEATGLFCLMVSFLLLFG L:  QLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRNP SIKDTVFPMAILGFALSEATGLFCLMVSFLLL M:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLL N:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLL O:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLF P:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFG Q:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFG R:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLF S:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLF Description Functional site 1) chain A residue 174 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 2) chain A residue 176 type sequence G description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 3) chain A residue 177 type sequence K description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 4) chain A residue 178 type sequence T description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 5) chain A residue 179 type sequence A description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 6) chain A residue 359 type sequence F description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 7) chain A residue 364 type sequence R description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 8) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 9) chain A residue 433 type sequence N description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 10) chain A residue 434 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 11) chain D residue 368 type sequence Y description BINDING SITE FOR RESIDUE ANP A 600 source : AC1 12) chain A residue 178 type sequence T description BINDING SITE FOR RESIDUE MG A 700 source : AC2 13) chain B residue 173 type sequence R description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 14) chain B residue 174 type sequence Q description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 15) chain B residue 175 type sequence T description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 16) chain B residue 176 type sequence G description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 17) chain B residue 177 type sequence K description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 18) chain B residue 178 type sequence T description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 19) chain B residue 179 type sequence A description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 20) chain B residue 359 type sequence F description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 21) chain B residue 364 type sequence R description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 22) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP B 600 source : AC3 23) chain B residue 178 type sequence T description BINDING SITE FOR RESIDUE MG B 700 source : AC4 24) chain B residue 271 type sequence D description BINDING SITE FOR RESIDUE MG B 700 source : AC4 25) chain C residue 173 type sequence R description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 26) chain C residue 174 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 27) chain C residue 175 type sequence T description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 28) chain C residue 176 type sequence G description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 29) chain C residue 177 type sequence K description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 30) chain C residue 178 type sequence T description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 31) chain C residue 179 type sequence A description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 32) chain C residue 330 type sequence E description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 33) chain C residue 364 type sequence R description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 34) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 35) chain C residue 434 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC5 36) chain C residue 178 type sequence T description BINDING SITE FOR RESIDUE MG C 700 source : AC6 37) chain C residue 271 type sequence D description BINDING SITE FOR RESIDUE MG C 700 source : AC6 38) chain C residue 346 type sequence S description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 39) chain C residue 375 type sequence R description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 40) chain D residue 160 type sequence G description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 41) chain D residue 161 type sequence V description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 42) chain D residue 162 type sequence G description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 43) chain D residue 163 type sequence K description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 44) chain D residue 164 type sequence T description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 45) chain D residue 165 type sequence V description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 46) chain D residue 189 type sequence E description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 47) chain D residue 190 type sequence R description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 48) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 49) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 50) chain D residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP D 600 source : AC7 51) chain D residue 164 type sequence T description BINDING SITE FOR RESIDUE MG D 700 source : AC8 52) chain D residue 189 type sequence E description BINDING SITE FOR RESIDUE MG D 700 source : AC8 53) chain D residue 190 type sequence R description BINDING SITE FOR RESIDUE MG D 700 source : AC8 54) chain D residue 193 type sequence E description BINDING SITE FOR RESIDUE MG D 700 source : AC8 55) chain B residue 375 type sequence R description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 56) chain F residue 158 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 57) chain F residue 159 type sequence A description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 58) chain F residue 160 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 59) chain F residue 161 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 60) chain F residue 162 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 61) chain F residue 163 type sequence K description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 62) chain F residue 164 type sequence T description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 63) chain F residue 165 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 64) chain F residue 189 type sequence E description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 65) chain F residue 190 type sequence R description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 66) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 67) chain F residue 346 type sequence P description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 68) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 69) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 70) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP F 600 source : AC9 71) chain F residue 163 type sequence K description BINDING SITE FOR RESIDUE MG F 700 source : BC1 72) chain F residue 164 type sequence T description BINDING SITE FOR RESIDUE MG F 700 source : BC1 73) chain F residue 189 type sequence E description BINDING SITE FOR RESIDUE MG F 700 source : BC1 74) chain F residue 256 type sequence D description BINDING SITE FOR RESIDUE MG F 700 source : BC1 75) chain J residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 76) chain J residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 77) chain K residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 78) chain K residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 79) chain L residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 80) chain L residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 81) chain M residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 82) chain M residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 83) chain N residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 84) chain N residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 85) chain O residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 86) chain O residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 87) chain P residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 88) chain P residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 89) chain Q residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 90) chain Q residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 91) chain R residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 92) chain R residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 93) chain S residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 94) chain S residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 95) chain J residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 96) chain K residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 97) chain L residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 98) chain M residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 99) chain N residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 100) chain O residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 101) chain P residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 102) chain Q residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 103) chain R residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 104) chain S residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 105) chain M residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 106) chain N residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 107) chain O residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 108) chain P residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 109) chain Q residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 110) chain R residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 111) chain S residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 112) chain G residue 263-276 type prosite sequence ITNELVDIITGASS description ATPASE_GAMMA ATP synthase gamma subunit signature. ITnElvDiitGAsS source prosite : PS00153 113) chain J residue 38-59 type prosite sequence SRNPSIKDTVFPMAILGFALSE description ATPASE_C ATP synthase c subunit signature. SRNPsikdtVfPmaILgfaLsE source prosite : PS00605 114) chain A residue 365-374 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSKS source prosite : PS00152 115) chain D residue 346-355 type prosite sequence PAVDPLDSKS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSKS source prosite : PS00152

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