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Database: UniProt
Entry: S3BVK2_OPHP1
LinkDB: S3BVK2_OPHP1
Original site: S3BVK2_OPHP1 
ID   S3BVK2_OPHP1            Unreviewed;       435 AA.
AC   S3BVK2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=G2 mitotic-specific cyclin-b1 {ECO:0000313|EMBL:EPE03451.1};
GN   ORFNames=F503_06624 {ECO:0000313|EMBL:EPE03451.1};
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:EPE03451.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE03451.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE03451.1,
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.
CC       {ECO:0000256|ARBA:ARBA00008742, ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; KE148167; EPE03451.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3BVK2; -.
DR   STRING; 1262450.S3BVK2; -.
DR   VEuPathDB; FungiDB:F503_06624; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_020695_4_0_1; -.
DR   OMA; QHMRQME; -.
DR   OrthoDB; 5474295at2759; -.
DR   Proteomes; UP000016923; Unassembled WGS sequence.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF523; G1_S-SPECIFIC CYCLIN CLN1-RELATED; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 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          90..176
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          185..291
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          188..268
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
SQ   SEQUENCE   435 AA;  48952 MW;  DB876AE5EF432DB1 CRC64;
     MAYHQIKDET FFVESDECTM PRMSARDAAK MLARNRQEMI ANELSRLASE EYLEDIMRHM
     RNMEDETLPD VALIDMQREI QWFMRPYLID FIVEAHAAFS LLPETLFLTI NLLDRYCSKR
     VVYKQHYQLV GCAALLIAAK YGDKKDRVPQ INELNNMCCG LYDAGMFTQM EMHVLNTLEW
     NIGHPSVDFF AQLIVAEERD DREVENMASY ISEIALYHRD FVSTKPSTMA RASLALARAI
     LSRPEVNDGE WDHADNVTLL TLSQNLHQPS ATLSRKYASA HLSCVSAKLT DFLARHAASI
     NNSRLNANGA NANRATSPCE ESGAAVADVY STPHKGMGAV PGVADGYMTP PITPDGTNFV
     NGQQAAAAKD MYPQPPRCPV TPTPQPAQNA AAANSYVPHQ QHLHVQHPQQ HQYQQQQQQT
     QHHAAQYYYD AQIAH
//
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