eF-site ID 3j94-ABCDEF PDB Code 3j94 Chain A, B, C, D, E, F Title Structure of ATP-bound N-ethylmaleimide sensitive factor determined by single particle cryoelectron microscopy Classification HYDROLASE Compound Vesicle-fusing ATPase Source (NSF_CRIGR) Sequence A:  FEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVK GILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKY VGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAIC HDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRP GRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDI KELAVETKNFSGAELEGLVRAAQSTAMNRHIDFLASLEND IKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQ TKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKI CSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIER LLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTS RKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFK DKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVR KFLALLREEG B:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIHDTVVN QLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVK MEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVE TKNFSGAELEGLVRAAQSTAMNRHIDFLASLENDIKPAFG TNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDR TPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKM IGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVP IGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQ EMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTT IAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALL REEG C:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICHD TVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGR LEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKE LAVETKNFSGAELEGLVRAAQSTAMNRHIDFLASLENDIK PAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTK NSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICS PDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLL DYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRK DVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDK ERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKF LALLREEG D:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAIDTV VNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLE VKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELA VETKNFSGAELEGLVRAAQSTAMNRHIFLASLENDIKPAF GTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSD RTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDK MIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYV PIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVL QEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERT TIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLAL LREEG E:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIHDTVVN QLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVK MEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVE TKNFSGAELEGLVRAAQSTAMNRHIDFLASLENDIKPAFG TEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTP LVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIG FSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIG PRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEM EMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIA QQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLRE EG F:  KMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGI LLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVG ESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIHDTVVN QLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVK MEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVE TKNFSGAELEGLVRAAQSTAMNRHIEDYASYIMNGIIKWG DPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTA LAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDD AYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLK KAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIA TGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLL MLIEMSLQMDPEYRVRKFLALLREEG Description Functional site 1) chain A residue 502 type sequence Y description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 2) chain A residue 503 type sequence I description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 3) chain A residue 504 type sequence M description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 4) chain A residue 505 type sequence N description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 5) chain A residue 506 type sequence G description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 6) chain A residue 507 type sequence I description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 7) chain A residue 546 type sequence H description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 8) chain A residue 548 type sequence G description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 9) chain A residue 549 type sequence K description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 10) chain A residue 550 type sequence T description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 11) chain A residue 551 type sequence A description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 12) chain A residue 708 type sequence K description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 13) chain A residue 711 type sequence L description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 14) chain F residue 631 type sequence K description BINDING SITE FOR RESIDUE ATP A 801 source : AC1 15) chain A residue 221 type sequence G description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 16) chain A residue 264 type sequence C description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 17) chain A residue 265 type sequence G description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 18) chain A residue 267 type sequence T description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 19) chain A residue 268 type sequence L description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 20) chain A residue 328 type sequence D description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 21) chain A residue 406 type sequence I description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 22) chain A residue 438 type sequence G description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 23) chain A residue 439 type sequence A description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 24) chain A residue 442 type sequence E description BINDING SITE FOR RESIDUE ATP A 802 source : AC2 25) chain A residue 631 type sequence K description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 26) chain B residue 502 type sequence Y description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 27) chain B residue 503 type sequence I description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 28) chain B residue 504 type sequence M description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 29) chain B residue 505 type sequence N description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 30) chain B residue 506 type sequence G description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 31) chain B residue 508 type sequence I description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 32) chain B residue 510 type sequence W description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 33) chain B residue 546 type sequence H description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 34) chain B residue 547 type sequence S description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 35) chain B residue 548 type sequence G description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 36) chain B residue 549 type sequence K description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 37) chain B residue 550 type sequence T description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 38) chain B residue 551 type sequence A description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 39) chain B residue 708 type sequence K description BINDING SITE FOR RESIDUE ATP B 801 source : AC3 40) chain B residue 221 type sequence G description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 41) chain B residue 263 type sequence G description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 42) chain B residue 264 type sequence C description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 43) chain B residue 265 type sequence G description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 44) chain B residue 266 type sequence K description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 45) chain B residue 268 type sequence L description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 46) chain B residue 406 type sequence I description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 47) chain B residue 437 type sequence S description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 48) chain B residue 438 type sequence G description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 49) chain B residue 439 type sequence A description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 50) chain B residue 442 type sequence E description BINDING SITE FOR RESIDUE ATP B 802 source : AC4 51) chain C residue 505 type sequence N description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 52) chain C residue 506 type sequence G description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 53) chain C residue 507 type sequence I description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 54) chain C residue 508 type sequence I description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 55) chain C residue 510 type sequence W description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 56) chain C residue 514 type sequence V description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 57) chain C residue 546 type sequence H description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 58) chain C residue 548 type sequence G description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 59) chain C residue 549 type sequence K description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 60) chain C residue 550 type sequence T description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 61) chain C residue 551 type sequence A description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 62) chain C residue 552 type sequence L description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 63) chain C residue 708 type sequence K description BINDING SITE FOR RESIDUE ATP C 801 source : AC5 64) chain B residue 382 type sequence A description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 65) chain B residue 385 type sequence R description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 66) chain B residue 388 type sequence R description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 67) chain C residue 221 type sequence G description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 68) chain C residue 262 type sequence P description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 69) chain C residue 263 type sequence G description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 70) chain C residue 264 type sequence C description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 71) chain C residue 265 type sequence G description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 72) chain C residue 266 type sequence K description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 73) chain C residue 267 type sequence T description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 74) chain C residue 268 type sequence L description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 75) chain C residue 406 type sequence I description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 76) chain C residue 438 type sequence G description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 77) chain C residue 439 type sequence A description BINDING SITE FOR RESIDUE ATP C 802 source : AC6 78) chain C residue 631 type sequence K description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 79) chain D residue 502 type sequence Y description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 80) chain D residue 503 type sequence I description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 81) chain D residue 504 type sequence M description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 82) chain D residue 505 type sequence N description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 83) chain D residue 506 type sequence G description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 84) chain D residue 507 type sequence I description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 85) chain D residue 508 type sequence I description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 86) chain D residue 544 type sequence P description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 87) chain D residue 545 type sequence P description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 88) chain D residue 546 type sequence H description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 89) chain D residue 547 type sequence S description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 90) chain D residue 548 type sequence G description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 91) chain D residue 549 type sequence K description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 92) chain D residue 550 type sequence T description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 93) chain D residue 551 type sequence A description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 94) chain D residue 707 type sequence I description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 95) chain D residue 708 type sequence K description BINDING SITE FOR RESIDUE ATP D 801 source : AC7 96) chain C residue 385 type sequence R description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 97) chain D residue 221 type sequence G description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 98) chain D residue 222 type sequence G description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 99) chain D residue 263 type sequence G description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 100) chain D residue 264 type sequence C description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 101) chain D residue 265 type sequence G description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 102) chain D residue 266 type sequence K description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 103) chain D residue 267 type sequence T description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 104) chain D residue 268 type sequence L description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 105) chain D residue 374 type sequence N description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 106) chain D residue 406 type sequence I description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 107) chain D residue 438 type sequence G description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 108) chain D residue 439 type sequence A description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 109) chain D residue 442 type sequence E description BINDING SITE FOR RESIDUE ATP D 802 source : AC8 110) chain D residue 631 type sequence K description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 111) chain E residue 504 type sequence M description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 112) chain E residue 505 type sequence N description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 113) chain E residue 506 type sequence G description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 114) chain E residue 507 type sequence I description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 115) chain E residue 508 type sequence I description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 116) chain E residue 545 type sequence P description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 117) chain E residue 546 type sequence H description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 118) chain E residue 548 type sequence G description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 119) chain E residue 549 type sequence K description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 120) chain E residue 550 type sequence T description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 121) chain E residue 551 type sequence A description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 122) chain E residue 552 type sequence L description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 123) chain E residue 707 type sequence I description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 124) chain E residue 708 type sequence K description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 125) chain E residue 711 type sequence L description BINDING SITE FOR RESIDUE ATP E 801 source : AC9 126) chain D residue 382 type sequence A description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 127) chain D residue 388 type sequence R description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 128) chain E residue 262 type sequence P description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 129) chain E residue 263 type sequence G description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 130) chain E residue 264 type sequence C description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 131) chain E residue 265 type sequence G description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 132) chain E residue 266 type sequence K description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 133) chain E residue 267 type sequence T description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 134) chain E residue 268 type sequence L description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 135) chain E residue 374 type sequence N description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 136) chain E residue 406 type sequence I description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 137) chain E residue 437 type sequence S description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 138) chain E residue 438 type sequence G description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 139) chain E residue 439 type sequence A description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 140) chain E residue 442 type sequence E description BINDING SITE FOR RESIDUE ATP E 802 source : BC1 141) chain E residue 631 type sequence K description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 142) chain F residue 503 type sequence I description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 143) chain F residue 505 type sequence N description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 144) chain F residue 506 type sequence G description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 145) chain F residue 508 type sequence I description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 146) chain F residue 545 type sequence P description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 147) chain F residue 546 type sequence H description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 148) chain F residue 547 type sequence S description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 149) chain F residue 548 type sequence G description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 150) chain F residue 549 type sequence K description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 151) chain F residue 550 type sequence T description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 152) chain F residue 551 type sequence A description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 153) chain F residue 552 type sequence L description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 154) chain F residue 707 type sequence I description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 155) chain F residue 708 type sequence K description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 156) chain F residue 711 type sequence L description BINDING SITE FOR RESIDUE ATP F 801 source : BC2 157) chain A residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 158) chain A residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 159) chain B residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 160) chain B residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 161) chain C residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 162) chain C residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 163) chain D residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 164) chain D residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 165) chain E residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 166) chain E residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 167) chain F residue 505 type BINDING sequence N description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 168) chain F residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:9731775, ECO:0000305|PubMed:9727495 source Swiss-Prot : SWS_FT_FI1 169) chain A residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 170) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 171) chain C residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 172) chain D residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 173) chain E residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 174) chain F residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:9731775 source Swiss-Prot : SWS_FT_FI2 175) chain A residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 176) chain B residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 177) chain C residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 178) chain D residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 179) chain E residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 180) chain F residue 259 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI5 181) chain A residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 182) chain B residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 183) chain C residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 184) chain D residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 185) chain E residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 186) chain F residue 569 type MOD_RES sequence S description Phosphoserine; by CDK16 => ECO:0000250|UniProtKB:P46460 source Swiss-Prot : SWS_FT_FI6 187) chain A residue 367-385 type prosite sequence ILVIGMTNRPDLIDEALLR description AAA AAA-protein family signature. IlVIgMTNrpdlIDeALl.R source prosite : PS00674 188) chain A residue 549 type catalytic sequence K description 642 source MCSA : MCSA1 189) chain A residue 550 type catalytic sequence T description 642 source MCSA : MCSA1 190) chain A residue 603 type catalytic sequence D description 642 source MCSA : MCSA1 191) chain A residue 604 type catalytic sequence D description 642 source MCSA : MCSA1 192) chain A residue 631 type catalytic sequence K description 642 source MCSA : MCSA1 193) chain A residue 708 type catalytic sequence K description 642 source MCSA : MCSA1 194) chain B residue 549 type catalytic sequence K description 642 source MCSA : MCSA2 195) chain B residue 550 type catalytic sequence T description 642 source MCSA : MCSA2 196) chain B residue 603 type catalytic sequence D description 642 source MCSA : MCSA2 197) chain B residue 604 type catalytic sequence D description 642 source MCSA : MCSA2 198) chain B residue 631 type catalytic sequence K description 642 source MCSA : MCSA2 199) chain B residue 708 type catalytic sequence K description 642 source MCSA : MCSA2 200) chain C residue 549 type catalytic sequence K description 642 source MCSA : MCSA3 201) chain C residue 550 type catalytic sequence T description 642 source MCSA : MCSA3 202) chain C residue 603 type catalytic sequence D description 642 source MCSA : MCSA3 203) chain C residue 604 type catalytic sequence D description 642 source MCSA : MCSA3 204) chain C residue 631 type catalytic sequence K description 642 source MCSA : MCSA3 205) chain C residue 708 type catalytic sequence K description 642 source MCSA : MCSA3 206) chain D residue 631 type catalytic sequence K description 642 source MCSA : MCSA4 207) chain D residue 549 type catalytic sequence K description 642 source MCSA : MCSA4 208) chain D residue 550 type catalytic sequence T description 642 source MCSA : MCSA4 209) chain D residue 603 type catalytic sequence D description 642 source MCSA : MCSA4 210) chain D residue 604 type catalytic sequence D description 642 source MCSA : MCSA4 211) chain D residue 708 type catalytic sequence K description 642 source MCSA : MCSA4 212) chain E residue 549 type catalytic sequence K description 642 source MCSA : MCSA5 213) chain E residue 550 type catalytic sequence T description 642 source MCSA : MCSA5 214) chain E residue 603 type catalytic sequence D description 642 source MCSA : MCSA5 215) chain E residue 604 type catalytic sequence D description 642 source MCSA : MCSA5 216) chain E residue 631 type catalytic sequence K description 642 source MCSA : MCSA5 217) chain E residue 708 type catalytic sequence K description 642 source MCSA : MCSA5 218) chain F residue 549 type catalytic sequence K description 642 source MCSA : MCSA6 219) chain F residue 550 type catalytic sequence T description 642 source MCSA : MCSA6 220) chain F residue 603 type catalytic sequence D description 642 source MCSA : MCSA6 221) chain F residue 604 type catalytic sequence D description 642 source MCSA : MCSA6 222) chain F residue 631 type catalytic sequence K description 642 source MCSA : MCSA6 223) chain F residue 708 type catalytic sequence K description 642 source MCSA : MCSA6

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