ID G0W3H0_NAUDC Unreviewed; 413 AA.
AC G0W3H0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCD22358.1};
GN Name=NDAI0A02000 {ECO:0000313|EMBL:CCD22358.1};
GN OrderedLocusNames=NDAI_0A02000 {ECO:0000313|EMBL:CCD22358.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22358.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22358.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; HE580267; CCD22358.1; -; Genomic_DNA.
DR RefSeq; XP_003667601.1; XM_003667553.1.
DR AlphaFoldDB; G0W3H0; -.
DR STRING; 1071378.G0W3H0; -.
DR GeneID; 11493416; -.
DR KEGG; ndi:NDAI_0A02000; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_12_1_1; -.
DR OMA; PRYMDFQ; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000000689; Chromosome 1.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:UniProt.
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:SF615; G2_MITOTIC-SPECIFIC CYCLIN-B; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 194..278
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 287..402
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 291..372
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 24..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 47379 MW; A59BB3D15A499E62 CRC64;
MHQFSRSLSS IAYNNPVDIE NIPPESKNYI KSNVNQNNAN NGPTTRSSNG HRVALSDVTS
QVNNKGLSNT SSLTKISSTG DTKDSHLQTI KTSSEDSEKQ ETTSRVKSNG KLIDPLQIPY
DVHIQKILDL AHSKFYRNLP DPCDEDTYDV VMVAELTNDI FPYLNTLENK FKPDSNYMAY
QPEIEWEHRR TIIGWLVQFH SKCRLLPETL YLTINIMDRF LSKQTISISK FQLIAAASLF
IAAKYEEINW PSLKDIVYML NNAYTKQEVL AAERIILGEL GFEIGWPGPM SFLRRISKAD
NYEYEIRTLS KYFLESTLME PTLVSALPSW LAAGAYLLSQ IILGYEDWSL AHIYYSGYTQ
DQILPLARLI LENCRDPGTH HREIWEKYSS RQQHCSAQLV SKWISEAERR VDE
//
