ID S9PWI4_SCHOY Unreviewed; 477 AA.
AC S9PWI4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=G2/M B-type cyclin Cdc13 {ECO:0000313|EMBL:EPX73446.1};
GN ORFNames=SOCG_02670 {ECO:0000313|EMBL:EPX73446.1};
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:EPX73446.1};
RN [1] {ECO:0000313|EMBL:EPX73446.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX73446.1};
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:EPX73446.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YFS286 {ECO:0000313|EMBL:EPX73446.1};
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 -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000256|ARBA:ARBA00006955}.
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DR EMBL; KE503206; EPX73446.1; -; Genomic_DNA.
DR RefSeq; XP_013016615.1; XM_013161161.1.
DR AlphaFoldDB; S9PWI4; -.
DR EnsemblFungi; EPX73446; EPX73446; SOCG_02670.
DR GeneID; 25031645; -.
DR VEuPathDB; FungiDB:SOCG_02670; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_10_6_1; -.
DR OMA; AEDWADP; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000016088; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0072687; C:meiotic spindle; IEA:EnsemblFungi.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR GO; GO:0071958; C:new mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0140602; C:nucleolar peripheral inclusion body; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR GO; GO:0071957; C:old mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:EnsemblFungi.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0140013; P:meiotic nuclear division; IEA:EnsemblFungi.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR GO; GO:0075297; P:negative regulation of ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR CDD; cd20568; CYCLIN_CLBs_yeast_rpt1; 1.
DR CDD; cd20512; CYCLIN_CLBs_yeast_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF587; S-PHASE ENTRY CYCLIN-5-RELATED; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383}.
FT DOMAIN 236..320
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 329..443
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 333..414
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 85..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 55492 MW; 2B1662FD7752C789 CRC64;
MTTRRLTRQH ILANALSNHD ENNPSKHLMH SSENAIIPGK KTISTSTSNK KRHALDDVSN
FHSKEANAPL ASKSTNVRHT NAVYPIHRPQ ERQDTIKAVD DEPVSKKRRQ PSALNSLSSF
SAAHPVDMAT TKPVTELHAE TYAKENEALS KKLKKDTEER IPLQEIMRQN AAAEKTEVQD
WDDLDAEDWA DPLMVSEYVV DIFQYLNQLE IETMPSPTYM DRQRELAWKM RGILTDWIIE
VHSRFRLLPE TLFLAVNIID RFLSLRVCSL GKLQLVGIAA LFIASKYEEV MCPSVQNFVY
MADGSYDEED ILQAERYILR VLEFNLAFPN PMNFLRRISK ADYYDIQTRT VAKYLVEIAL
LDHRLLPYPP SQQCAAAMYL AREMLGRGVW NRNLVHYSGY EEHELISVVK KMINYLQKPV
RHEAFFKKYA SKKFMKASLF VRDWIKKNSM PLEDDIDEDY AYHQEQRIHH DMRDESW
//
