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Entry: S9RK13_SCHOY
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Original site: S9RK13_SCHOY 
ID   S9RK13_SCHOY            Unreviewed;      1338 AA.
AC   S9RK13;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=SOCG_03524 {ECO:0000313|EMBL:EPX74314.1};
OS   Schizosaccharomyces octosporus (strain yFS286) (Fission yeast)
OS   (Octosporomyces octosporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=483514 {ECO:0000313|EMBL:EPX74314.1};
RN   [1] {ECO:0000313|EMBL:EPX74314.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YFS286 {ECO:0000313|EMBL:EPX74314.1};
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).
RN   [2] {ECO:0000313|EMBL:EPX74314.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YFS286 {ECO:0000313|EMBL:EPX74314.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Nusbaum C., Russ C., Rhind N., Niki H., Allshire R., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Birren B.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; KE503206; EPX74314.1; -; Genomic_DNA.
DR   RefSeq; XP_013017466.1; XM_013162012.1.
DR   EnsemblFungi; EPX74314; EPX74314; SOCG_03524.
DR   GeneID; 25032496; -.
DR   VEuPathDB; FungiDB:SOCG_03524; -.
DR   eggNOG; KOG0996; Eukaryota.
DR   HOGENOM; CLU_001042_4_1_1; -.
DR   OMA; HEGNESG; -.
DR   OrthoDB; 231904at2759; -.
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:0140097; F:catalytic activity, acting on DNA; IEA:UniProt.
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; 1.20.1060.20; -; 1.
DR   Gene3D; 1.20.5.340; -; 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; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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}.
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          81..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          394..442
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          478..505
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          531..614
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          812..853
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          885..919
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          963..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;  151857 MW;  DE6085E7E73D3247 CRC64;
     MSDKGPARTS SVPSIVDATP DRAERPRKQV RQVVTTPSRS EDPSRIVKLE QTPSQGFHSE
     FLKKRITDSL RERPNLLNKF ISANQETPSK PSAPNSLNSS NAEDSSLIED TITEQENPDI
     LAPRLVVYQL TLKNFKSYAG TQIIGPFHPS FSSIVGPNGS GKSNVIDALL FVFGFRASKL
     RQTKASALIH KSAAHPSLES CDVEILFKEV NPDSSYIEGS ELSIRRSAYK NNVSKYFLNN
     VESSFSTISN MLKERGVDLN HKRFLILQGE VESIAQMKPK ALTESDDGLL EYLEDIIGTS
     RYKPIIEEKI NELTALNDTC NEKENRFQLV VAEKNKLESS KNVVLDILRD ENNLNRKLHT
     LYQLNLFELN SKRNLITNML QKLEDSYKSK NDNFNENEKV VAQMVEELNQ LKSKAQEFKN
     SNRAEKRERQ RYEQQAVKIE EKWKHLSSKQ KKNQKQLETL SAKKSELEYS LDTHGDLHHR
     LTQEMEEIVS KLSAEEDELN KIRESLRGKT EGISNAIEEK QKLMAPSEKK INELNSVKQV
     TKAELDMLLE QEKNSDEEQQ KAKSSLEKLL AEQKEKTQLL NSKKTHHHSI KKESQNLARN
     VSDLKQKKNE LHRIIAQSRV KLEEIRSTLS SSRSRGNVLG GLQTLHDSGQ LTGFHGRLGD
     LATIDSKYDV AISTACPALN HIVVDNLEVG QKCIAFLRSN NLGRSSFIVL GALQEKNLKP
     IQTPENVPRL FDLLHYKDNI FAPAFFSVLQ NTLVADNLEQ ANRIAFGKTR WRVVTLNGQL
     IDKSGTMTGG GTRVKQGGMA SQLPAEISPV ALNNIETQTT DAENRHRQVS EQLQALLEKS
     DILKNEIPSL ELEISKLHLD LSAFNNLVEG ARNQVSNSRM ASKDERSLQD RKQKLTSDLK
     KLQQQIDSIN DSNAGVVAEV RELQDKIMQI GGIKYRIQKS KVDDLHEQHK FVKEKITNIN
     FEKRKNEQRV HSIAQELESL QSDISITEKD IKMNEDELSS LRQKTKEYTG KIDKLSNMIH
     DIDDSINELN SRVEFESKEI NSMKAERLDL ENKLTEQKSA HTDVLNSEKK IRKLLSELLL
     HDLREYDQSE TQAPEFQEFS EDELASLNKQ SLYDGISEFK KKTEEKEVDV GVLQSYLKCT
     KDAEKKAIDF EAETQKRNNV KQTVTDLQTQ RLDEFMEGFN IISQKLKAMY QIITMGGNAE
     LELVDSLDPF SEGVLFSIMP PKKSWKNISN LSGGEKTLSS LALVFALHSY KPTPLYVMDE
     IDAALDFKNV SIVANYIKER TKNAQFIVIS LRSNMFELSS RLVGIYKTAN MTKSVTINNR
     DLQMNAEKDV DHSALQVN
//
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