ESP1_YEAST
ID ESP1_YEAST Reviewed; 1630 AA.
AC Q03018; D6VUN0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Separin;
DE EC=3.4.22.49;
DE AltName: Full=Separase;
GN Name=ESP1; OrderedLocusNames=YGR098C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-1630.
RX PubMed=1493337; DOI=10.1091/mbc.3.12.1443;
RA McGrew J.T., Goetsch L., Byers B.E., Baum P.;
RT "Requirement for ESP1 in the nuclear division of Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 3:1443-1454(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND INTERACTION WITH PDS1.
RX PubMed=9635435; DOI=10.1016/s0092-8674(00)81211-8;
RA Ciosk R., Zachariae W., Michaelis C., Shevchenko A., Mann M., Nasmyth K.;
RT "An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the
RT metaphase to anaphase transition in yeast.";
RL Cell 93:1067-1076(1998).
RN [5]
RP CLEAVAGE OF MCD1, AND FUNCTION.
RX PubMed=10403247; DOI=10.1038/21831;
RA Uhlmann F., Lottspeich F., Nasmyth K.;
RT "Sister-chromatid separation at anaphase onset is promoted by cleavage of
RT the cohesin subunit Scc1.";
RL Nature 400:37-42(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1568-ASP--ASP-1570.
RX PubMed=11149918; DOI=10.1083/jcb.152.1.27;
RA Jensen S., Segal M., Clarke D.J., Reed S.I.;
RT "A novel role of the budding yeast separin Esp1 in anaphase spindle
RT elongation: evidence that proper spindle association of Esp1 is regulated
RT by Pds1.";
RL J. Cell Biol. 152:27-40(2001).
RN [7]
RP FUNCTION AS A COMPONENT OF THE FEAR NETWORK.
RX PubMed=11832211; DOI=10.1016/s0092-8674(02)00618-9;
RA Stegmeier F., Visintin R., Amon A.;
RT "Separase, polo kinase, the kinetochore protein Slk19, and Spo12 function
RT in a network that controls Cdc14 localization during early anaphase.";
RL Cell 108:207-220(2002).
CC -!- FUNCTION: Caspase-like protease, which plays a central role in the
CC chromosome segregation by cleaving the MCD1/SCC1 subunit of the cohesin
CC complex at the onset of anaphase. During most of the cell cycle, it is
CC inactivated by securin/PDS1 protein. It also promotes anaphase spindle
CC elongation. A component of the FEAR (CDC14 early anaphase release)
CC network which promotes CDC14 release from the nucleolus during early
CC anaphase. Cleaves SLK19. {ECO:0000269|PubMed:10403247,
CC ECO:0000269|PubMed:11149918, ECO:0000269|PubMed:11832211,
CC ECO:0000269|PubMed:9635435}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=All bonds known to be hydrolyzed by this endopeptidase have
CC arginine in P1 and an acidic residue in P4. P6 is often occupied by
CC an acidic residue or by a hydroxy-amino-acid residue, the
CC phosphorylation of which enhances cleavage.; EC=3.4.22.49;
CC -!- ACTIVITY REGULATION: It is inactivated via its interaction with PDS1,
CC which probably covers its active site. PDS1 degradation at anaphase,
CC liberates it and triggers MCD1 cleavage.
CC -!- SUBUNIT: May bind calcium. Interacts with PDS1. Interacts with MCD1.
CC {ECO:0000269|PubMed:9635435}.
CC -!- INTERACTION:
CC Q03018; Q00362: CDC55; NbExp=2; IntAct=EBI-6657, EBI-1942;
CC Q03018; P40316: PDS1; NbExp=2; IntAct=EBI-6657, EBI-16908;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11149918}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, spindle pole body
CC {ECO:0000269|PubMed:11149918}. Cytoplasm {ECO:0000269|PubMed:11149918}.
CC Note=Accumulates in the nucleus in G2 and is mobilized onto the spindle
CC pole bodies and spindle midzone at anaphase onset, where it persists
CC into midanaphase. The association with MCD1 may be important for its
CC nuclear targeting.
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DR EMBL; L07289; AAB03897.1; -; Genomic_DNA.
DR EMBL; Z72883; CAA97101.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08191.1; -; Genomic_DNA.
DR PIR; S64403; S64403.
DR RefSeq; NP_011612.3; NM_001181227.3.
DR PDB; 5U1S; X-ray; 3.00 A; A=51-1630.
DR PDB; 5U1T; X-ray; 2.60 A; A=51-1630.
DR PDBsum; 5U1S; -.
DR PDBsum; 5U1T; -.
DR AlphaFoldDB; Q03018; -.
DR SMR; Q03018; -.
DR BioGRID; 33341; 590.
DR ComplexPortal; CPX-1340; Separase-Securin complex.
DR DIP; DIP-2933N; -.
DR ELM; Q03018; -.
DR IntAct; Q03018; 7.
DR MINT; Q03018; -.
DR STRING; 4932.YGR098C; -.
DR MEROPS; C50.001; -.
DR iPTMnet; Q03018; -.
DR MaxQB; Q03018; -.
DR PaxDb; Q03018; -.
DR PRIDE; Q03018; -.
DR EnsemblFungi; YGR098C_mRNA; YGR098C; YGR098C.
DR GeneID; 852990; -.
DR KEGG; sce:YGR098C; -.
DR SGD; S000003330; ESP1.
DR VEuPathDB; FungiDB:YGR098C; -.
DR eggNOG; KOG1849; Eukaryota.
DR GeneTree; ENSGT00390000004990; -.
DR HOGENOM; CLU_243454_0_0_1; -.
DR InParanoid; Q03018; -.
DR OMA; SMTPRGK; -.
DR BioCyc; YEAST:G3O-30808-MON; -.
DR BRENDA; 3.4.22.49; 984.
DR Reactome; R-SCE-2467813; Separation of Sister Chromatids.
DR PRO; PR:Q03018; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; Q03018; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990520; C:separase-securin complex; IPI:ComplexPortal.
DR GO; GO:0005819; C:spindle; IDA:SGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0051307; P:meiotic chromosome separation; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IMP:SGD.
DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IMP:SGD.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:SGD.
DR GO; GO:1902104; P:positive regulation of metaphase/anaphase transition of meiotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:SGD.
DR InterPro; IPR005314; Peptidase_C50.
DR InterPro; IPR030397; SEPARIN_core_dom.
DR PANTHER; PTHR12792; PTHR12792; 1.
DR PROSITE; PS51700; SEPARIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Chromosome partition; Cytoplasm; Cytoskeleton;
KW Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..1630
FT /note="Separin"
FT /id="PRO_0000205904"
FT DOMAIN 1443..1542
FT /note="Peptidase C50"
FT REGION 1016..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1531
FT /evidence="ECO:0000250"
FT MUTAGEN 1568..1570
FT /note="DKD->AKA: Reduces function. Loss of function."
FT /evidence="ECO:0000269|PubMed:11149918"
FT CONFLICT 136
FT /note="F -> S (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 250..253
FT /note="TVEC -> IRRV (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="V -> L (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="S -> Y (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="K -> E (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="A -> E (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1146
FT /note="I -> T (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1295
FT /note="K -> R (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1333..1336
FT /note="QEID -> ARKSI (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT CONFLICT 1443
FT /note="E -> Q (in Ref. 1; AAB03897)"
FT /evidence="ECO:0000305"
FT HELIX 54..73
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 157..162
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 332..347
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 376..391
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 399..418
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 442..459
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 535..543
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 557..567
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 586..590
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 591..606
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 612..622
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 627..630
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 636..651
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 655..667
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 676..689
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 693..706
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 709..712
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 714..723
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 734..742
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 744..748
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 750..753
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 763..786
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 790..809
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 810..812
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 816..839
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 843..859
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 863..879
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 883..897
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 902..904
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 906..915
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 919..925
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 927..930
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 939..946
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 953..955
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 958..960
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 961..980
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 984..989
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 994..997
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1046..1062
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1065..1067
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1070..1088
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1096..1106
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1109..1122
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1126..1130
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1145..1161
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1165..1173
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1175..1177
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1180..1186
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1187..1190
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1191..1197
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1214..1232
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1234..1237
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1243..1271
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1272..1275
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1276..1279
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1286..1303
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1305..1309
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1313..1315
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 1321..1328
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1337..1354
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1361..1363
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1366..1381
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1390..1396
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1398..1400
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1405..1407
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1409..1413
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1416..1420
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1422..1431
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1432..1434
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1436..1441
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1446..1450
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1457..1470
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1478..1483
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1487..1495
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1498..1505
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1509..1511
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1514..1517
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1526..1528
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1531..1534
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1537..1539
FT /evidence="ECO:0007829|PDB:5U1S"
FT STRAND 1542..1545
FT /evidence="ECO:0007829|PDB:5U1S"
FT HELIX 1547..1553
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1557..1564
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1568..1582
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1598..1605
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 1606..1608
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1609..1611
FT /evidence="ECO:0007829|PDB:5U1T"
FT TURN 1612..1617
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1619..1623
FT /evidence="ECO:0007829|PDB:5U1T"
FT STRAND 1626..1629
FT /evidence="ECO:0007829|PDB:5U1T"
SQ SEQUENCE 1630 AA; 187447 MW; FBAFD33FF706C6BA CRC64;
MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS SNSIGILAMH
NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH MWGHINSTVK QHLMIIVKLI
NNNALGLASS EIIFLFNETN LFQAHSLKNI LLADFSTWND YYLSNLKILA LQIILKRKLV
DEYLPHILEL FSHDKRYLLK DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL
PFKKFISNIT VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG KHISATLKCL
VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES AAALLSELLG VLSEICIDYK
EPKRLSNIIS VLFNASVLFK SHSFLLKTAN LEISNVLISN DSKTSHRTIL KFEKFISSAQ
SAQKKIEIFS CLFNVYCMLR NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV
LYGNSSIENI PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN FNNFDKLSIE
LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK NQLQKTMNLS TAKIEQALLH
ASSLINVHLW DSDLTAFQIY FGKTLPAMKP ELFDINNDHN LPMSLYIKVI LLNIKIFNES
AKLNIKAGNV ISAVIDCRKA QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI
GSARDCEFYS KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD IDDSICLSEY
MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL PVIPSTMPNN ILKTPSKHST
GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI SKLKQMKELL ESLKLDTLDN HELSKISSLS
SLTLTILSNI TSIHNAESSL ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP
NNISTITESI RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW TTRYDLDKRM
QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL HQNLPSRKLY GNPAMFIKVE
DWVIELFLKL NPQEIDFLSK MEDLIYFVLD ILLFHGEENA YDEIDFSMLH VQLEEQIKKY
RATMTTNSIF HTFLVVSSSC HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV
TIEDNISMIL NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT YLLGGCPMVL
GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY AVSKSRGVCH LRYLNGAAPV
IYGLPIKFVS
