ID K1WMZ8_TRIAC Unreviewed; 435 AA.
AC K1WMZ8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKD02494.1};
GN ORFNames=A1Q2_03254 {ECO:0000313|EMBL:EKD02494.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD02494.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD02494.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD02494.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD02494.1}.
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DR EMBL; AMBO01000282; EKD02494.1; -; Genomic_DNA.
DR AlphaFoldDB; K1WMZ8; -.
DR STRING; 1220162.K1WMZ8; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_10_6_1; -.
DR InParanoid; K1WMZ8; -.
DR OMA; PRYMDFQ; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
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 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:SF198; CYCLIN B; 1.
DR PANTHER; PTHR10177; CYCLINS; 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:UP000006757}.
FT DOMAIN 217..301
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 311..425
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 315..395
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 49921 MW; DB1568A68E113D96 CRC64;
MSAATRAKAA AITSTKPSQP VKAGSKRNVL GAVTNIREDH GEVAKKPARS TAQRQPLSNR
SQTFDNNRGT TTTRATRAAA AQVFAQPEPV EVEVVSRETA RIDLQSNNVI VEDEYEDDEK
TVGARSDDMD EDEDDEFDDE DWLRMSPEEE LAARQELMAV KDTFQDDIDM FDTTMVAEYA
DEIFAHMEEM ELATMPNPRY MDFQSEVEWT MRTTLVDWLL QVHLRYHLLP ETLWIAVNIL
DRFLSVRVVS TQKLQLVGLT ALFIAAKYEE ILAPSVDEFV YMADNGYTKD EILKGERIIL
QTLDFNISAY CTPYSWVRRI SKADDYDIQT RTLSKFLMEV TLLDHRFLRC KPSMIAAVGM
YLSRKMLGSD WNDAFVFYSE FTESQLRTAA DMICERLVED GFERVFVYVK YSSKKFLRAS
AYACDWAMTN YRPAE
//
