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Database: UniProt
Entry: A7TRQ6_VANPO
LinkDB: A7TRQ6_VANPO
Original site: A7TRQ6_VANPO 
ID   A7TRQ6_VANPO            Unreviewed;       562 AA.
AC   A7TRQ6;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN   ORFNames=Kpol_367p5 {ECO:0000313|EMBL:EDO15050.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO15050.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; DS480485; EDO15050.1; -; Genomic_DNA.
DR   RefSeq; XP_001642908.1; XM_001642858.1.
DR   AlphaFoldDB; A7TRQ6; -.
DR   STRING; 436907.A7TRQ6; -.
DR   GeneID; 5543098; -.
DR   KEGG; vpo:Kpol_367p5; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_033561_1_0_1; -.
DR   InParanoid; A7TRQ6; -.
DR   OMA; FIMYCHT; -.
DR   OrthoDB; 5474295at2759; -.
DR   PhylomeDB; A7TRQ6; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:UniProt.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:UniProt.
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; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF553; G1_S-SPECIFIC CYCLIN CLN3; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 1.
PE   3: Inferred from homology;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT   DOMAIN          100..186
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          415..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  63838 MW;  08FBFBB596E85C16 CRC64;
     MNVSTTTIIN NDNVKVVDSL PNLHHLAHIR RNVARSKAAN PSLLKNQFNV HRISVLEYSK
     SLLNHLIRLE DSTNLEYPLI INNFKAQPQI NDKMRNLIID FIICCHTRLK LSSSTLFLTI
     DLLNRYSSKF IIKCNNYQLF ALTALWISSK YWDSKNKIPN FNILTSLCCN QFTPTQFKEI
     EWHLLTSLNW SILQNPTTDY FIDLLLVIDN NNSSQNLNPI YWKNSNLNLN EIKSGAILLA
     ELASFDLNLS FSYNSSAIAL ASITLITLAL NFHDLNNWEN YHVDSKDANL NKICDKLLFL
     ATDKDAFPSS FKFKYLNDQQ KNSTTAAVTN TNLNNGNKIL TALSNYYLQL QFEEFYNSQE
     FNNLANSIND NLINDQNIMH SNNEFMKTNQ DSSSNCMKGR MNIYSNHSNY NDKHYNNSNI
     NITNNSPHSV SSSTSSSAIS TFASPDSAMT AESDKEISSS TSSLLPNSLL LLPLTPTTPT
     LFQVDTKSSE KKRLMTLNSI NNNNNFSKQD NQASARSNPI VNIPASSGIR TFVKGHIKRS
     SSSMDIDFFD TDMDYKRNPN RY
//
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