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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//