ID G3ANH5_SPAPN Unreviewed; 448 AA.
AC G3ANH5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=G1 cyclin {ECO:0000313|EMBL:EGW31964.1};
GN ORFNames=SPAPADRAFT_152230 {ECO:0000313|EMBL:EGW31964.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31964.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|ARBA:ARBA00008742, ECO:0000256|RuleBase:RU000383}.
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DR EMBL; GL996502; EGW31964.1; -; Genomic_DNA.
DR RefSeq; XP_007375240.1; XM_007375178.1.
DR AlphaFoldDB; G3ANH5; -.
DR STRING; 619300.G3ANH5; -.
DR GeneID; 18870921; -.
DR KEGG; spaa:SPAPADRAFT_152230; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_033561_0_0_1; -.
DR InParanoid; G3ANH5; -.
DR OMA; QFYPNIY; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:UniProt.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:InterPro.
DR CDD; cd20559; CYCLIN_ScCLN_like; 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; IPR014399; Cyclin_CLN.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF553; G1_S-SPECIFIC CYCLIN CLN3; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001770; Cyclin_CLN; 2.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 1.
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|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT DOMAIN 79..165
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 366..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 51238 MW; FF6E72640E05B305 CRC64;
MISNSPDPFL QVRLFNSQVK STNFNLQSME FKCHSTTICD YQMEMLHHLL TVESKTLPSM
TLIEQQPEIK LGMRPLLLDF LMEVITILNL SRSTFPLTVN LIDRYCSTRI VKKQHYQLLG
LTSLWISCKN LDSKFKIPTL NDLRKICVDS YYKELFIEME KHILKSLEWM VNSPTFDAFI
DLYLNLLISN NNNPSVCDII RKSIHNIKLL SNYIGELFQF YPNIYFDYTS SQIALIAILA
SIMTLKIPVN LISLLNFYND LLKTDEYKSN ACGDEADNFD EILSINSFQS LFTKGFLKNL
IKIIDNPPKS LEIKYFSEKG KYTQLMKSLV QCAIDSLMTL LDPPVTPKVE IPEIKQPTTF
ALPLTPVSNS TSPRRFKSEK PDDEGTTADA TAVNASGTIT PVSLSSPNKK RGYDSIDELE
IATSTIEQYQ KVEHDEFKKS KGIFFIPR
//
