ID I2H6W3_TETBL Unreviewed; 564 AA.
AC I2H6W3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=G1/S-specific cyclin {ECO:0000256|PIRNR:PIRNR001770};
GN Name=TBLA0G01710 {ECO:0000313|EMBL:CCH62115.1};
GN ORFNames=TBLA_0G01710 {ECO:0000313|EMBL:CCH62115.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62115.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH62115.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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 -!- FUNCTION: G1/S-specific cyclin essential for the control of the cell
CC cycle at the G1/S (start) transition. {ECO:0000256|PIRNR:PIRNR001770}.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|ARBA:ARBA00008742, ECO:0000256|PIRNR:PIRNR001770,
CC ECO:0000256|RuleBase:RU000383}.
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DR EMBL; HE806322; CCH62115.1; -; Genomic_DNA.
DR RefSeq; XP_004181634.1; XM_004181586.1.
DR AlphaFoldDB; I2H6W3; -.
DR STRING; 1071380.I2H6W3; -.
DR GeneID; 14497247; -.
DR KEGG; tbl:TBLA_0G01710; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_536434_0_0_1; -.
DR InParanoid; I2H6W3; -.
DR OMA; CLMQYEL; -.
DR OrthoDB; 1966232at2759; -.
DR Proteomes; UP000002866; Chromosome 7.
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 GO; GO:0001932; P:regulation of protein phosphorylation; IEA:UniProt.
DR CDD; cd20559; CYCLIN_ScCLN_like; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
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; PTHR21615:SF2; CYCLIN N-TERMINAL DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR21615; UNCHARACTERIZED; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001770; Cyclin_CLN; 1.
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, ECO:0000256|PIRNR:PIRNR001770};
KW Cell division {ECO:0000256|ARBA:ARBA00022618,
KW ECO:0000256|PIRNR:PIRNR001770};
KW Cyclin {ECO:0000256|PIRNR:PIRNR001770, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 87..196
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
SQ SEQUENCE 564 AA; 63636 MW; 6BCD3DDEF8E1CCC2 CRC64;
MSCTTNTTRS KSNIPQKLGL IVNAKQTHYP IELSNSELLN HFNVINEYNN DISTNSVQLS
NKLNPSINLI NQQPEMIPHL TRYDILSFLF ELSVVTRVIP GVYYHAVRLY DRYSSKRIVL
KNQAKLVVAT CLWISAKTQG GCNHIINNVC IPTGGRFYGP NPRARIPRLS ELIHYSGGES
VFDKSMFIQM ESHILSTLGW EVSEPLINDY LLNVDENCLI QYKVYQKQLE LFNKKKIEQQ
LNSNSSSSPQ INEEEQEEDL DLQLKIQLIN IKRFLIDLST WELEFLSFNI YEIALIILKL
INKYINPSNF IEFEQSSILN LPEISIDKQN YLISIFESLL IKTNKIPVSL YEIYKDQAGI
CDFITLIKKY NDYNLSTTNS NTATISSSSN TASINVIDGS PCGYNTPEKN SHYPTHTLSY
TNSSMDFNLS STSDISIFSH FEQPSPITPY PSNTTTNVNS TMNTNSSLNN ALANLPLKSK
QINKSNSSSI YSNDSLITST TSIANKENIQ PISNTNKITN NSKIPNIIKI NNSNIFLSNS
EDKFTLNNNS TTSLLSIPTP NLSS
//
