ID S3CVA3_OPHP1 Unreviewed; 488 AA.
AC S3CVA3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=G2 mitotic-specific cyclin-b {ECO:0000313|EMBL:EPE04685.1};
GN ORFNames=F503_06234 {ECO:0000313|EMBL:EPE04685.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE04685.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE04685.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE04685.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000256|ARBA:ARBA00006955}.
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DR EMBL; KE148159; EPE04685.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CVA3; -.
DR STRING; 1262450.S3CVA3; -.
DR VEuPathDB; FungiDB:F503_06234; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_10_2_1; -.
DR OMA; FMAYRPS; -.
DR OrthoDB; 5474295at2759; -.
DR Proteomes; UP000016923; 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; cd20568; CYCLIN_CLBs_yeast_rpt1; 1.
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:SF587; S-PHASE ENTRY CYCLIN-5-RELATED; 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:UP000016923}.
FT DOMAIN 265..349
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT DOMAIN 358..466
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 362..443
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 150..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 54114 MW; 273FFB86F08968CF CRC64;
MPPARTARQR VATNENDENN VTAARMTRAK AASLHVDDLA VPAKPLQAKK TAGAAQPTGL
RKRAALGDVS NVAKVDVVEA KKAIGKAGLV SKAAQPTGVQ KNTARPAGRT ALSTKETVKK
TTEVKKSGPG SINAVQKRKV AASALATAVK EDTPVDDGEP ARKKAHVATS RAEEQPKPKA
EVKVSKLEQE LMEEPAEEYV PTEFVYPEGV KDLDAEDFDD PQMVAEYAAD IFEYLRDLEC
SSLPNPRYMS HQDELDWKTR GVLIDWLVEV HTRFHLLPET LFLAVNIVDR FLSAKVVQLD
RLQLVGVTAM FIAAKYEEVL SPSVGSFRHV ADDGFTEAEI LSAERFMLGT LNYDLSYPNP
MNFLRRVSKA DNYDIQTRTV AKYLTEISLL DHRFMSYRPS HVAAAAMFLA RLILDRGEWD
ATLSFYAGYT EEEIEPVAIL MVDYLARPST HEAFFKKYAT SLITRQWAKK NAIHFGITDV
ELSVDEIS
//
