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   27-MAR-2024, entry version 191.
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; 591.
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; 4932-YGR098C; -.
DR   PeptideAtlas; Q03018; -.
DR   EnsemblFungi; YGR098C_mRNA; YGR098C; YGR098C.
DR   GeneID; 852990; -.
DR   KEGG; sce:YGR098C; -.
DR   AGR; SGD:S000003330; -.
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; VISIDVC; -.
DR   OrthoDB; 5479815at2759; -.
DR   BioCyc; YEAST:G3O-30808-MONOMER; -.
DR   BRENDA; 3.4.22.49; 984.
DR   Reactome; R-SCE-2467813; Separation of Sister Chromatids.
DR   BioGRID-ORCS; 852990; 2 hits in 10 CRISPR screens.
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:0035308; P:negative regulation of protein dephosphorylation; 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; EXTRA SPINDLE POLES 1-RELATED; 1.
DR   PANTHER; PTHR12792:SF0; SEPARIN; 1.
DR   Pfam; PF03568; Peptidase_C50; 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
//