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Database: UniProt
Entry: S9W2R5_SCHCR
LinkDB: S9W2R5_SCHCR
Original site: S9W2R5_SCHCR 
ID   S9W2R5_SCHCR            Unreviewed;      1338 AA.
AC   S9W2R5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=SPOG_04214 {ECO:0000313|EMBL:EPY54323.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY54323.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY54323.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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DR   EMBL; KE546988; EPY54323.1; -; Genomic_DNA.
DR   RefSeq; XP_013021929.1; XM_013166475.1.
DR   STRING; 653667.S9W2R5; -.
DR   EnsemblFungi; EPY54323; EPY54323; SPOG_04214.
DR   GeneID; 25038527; -.
DR   eggNOG; KOG0996; Eukaryota.
DR   HOGENOM; CLU_001042_4_1_1; -.
DR   OMA; CPALDNM; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0000796; C:condensin complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR   GO; GO:1990814; F:DNA/DNA annealing activity; IEA:EnsemblFungi.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT   DOMAIN          652..765
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          380..505
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          549..614
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          812..912
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1012..1060
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1338 AA;  151848 MW;  BB0C5C4C2E2E4554 CRC64;
     MSDKRPARTS SVPSIVDATP DRAERPRKQV RQVVTTPSRS EDPSRIVKLE QTPSQGFHSE
     FLKKRITDSL RERPNLLNKF ISANQETPSK ASVPNPFNSS NAEDSSLIED AITGQDNLDV
     LAPRLIVYQL TLKNFKSYAG TQIIGPFHPS FSSIVGPNGS GKSNVIDALL FVFGFRASKL
     RQTKASALIH KSAAHPSLDS CDVEIVFKEV DPDSNYIDGS ELSIRRSAYK NNVSKYFLNN
     VESSFSTVSN VLKERGIDLN HKRFLILQGE VESIAQMKPK AMTENDDGLL EYLEDIIGTS
     KYKPIIEEKI NELSTLNDVC NEKENRFNLV VAERNKLESS KNEVLDILRD ENNLYRKLHT
     LYQLNLFELN SKKVLITNML QKLEDSYKSK NANFEENEKV VFEMTEELTQ LKSKVQDLKN
     SNRAEKRERQ RYEQQAVKIE EKLKHLSSKQ KKTQKQLETL SANKSELQYS LDTHDDVHQR
     LTQEIEEISS KLSSEEDQLN KIRESLRGKT EGISNAIEEK QKLMAPSEKK VNELNSVKQV
     TKAELDMLFE QEKSLNEEQQ NAKSSLENLI AEQKEKTLLL NSKKNHHNTI KKDSQSLERN
     ISDLRRKKSE LHRVIAQSRV KLEEMKATLS SSRSRGNVLG GLQTLHDSGQ LEGFHGRLGD
     LGTIDSKYDV AISTACPALN HIVVDSLEVG QKCIAFLRSN NLGRSSFIVL RALQERNLKP
     IQTPENVPRL FDLLHFKNEI FAPAFFSVLQ NTLVADNLEQ ANRIAFGKTR WRVVTLSGQL
     IDKSGTMTGG GTRVKQGGMA SQLPSDISPV SLSNAEDQTT DAENRHRQVS EELVALLEKS
     DELKNEAPCL ELEISKLHLD LSAFNNLVEG AKNQVSNSRK ALKEERSLQE RKQKLTGDLT
     KLDQQIDNIK ASNGGLVAEV RELQDKIMQI GGIKYRIQKS KVDDLHEQHK YIKEKLTNVS
     FEKRKNEQRV HSIIGELESL QSDFSTTQKE LETNETDFNL LRGKIKDYTT KIDELSNSIH
     DINDSINELN NRIDFESKEI NSMKAERLDL ENKLTEQKTA HSDVLHNEKK LQKLLSELIL
     HDLREYDQSE ARAPEFQEFS EDELASMNKQ SLYEGISEFK KKTEEKEVDV GVLQSYLRCT
     KEVEKRASDF EADTRKRNNV KQTVTDLQTQ RLDEFMEGFG NISQKLKAMY QIITMGGNAE
     LELVDSLDPF SEGVLFSIMP PKKSWKNISN LSGGEKTLSS LALVFALHSY KPTPLYVMDE
     IDAALDFKNV SIVANYIKER TKNAQFIVIS LRSNMFELSS RLVGIYKTAN MTKSVTINNR
     DLQVNAEKDS DHSPSQVN
//
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