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Database: UniProt/TrEMBL
Entry: Q0UMA7_PHANO
LinkDB: Q0UMA7_PHANO
Original site: Q0UMA7_PHANO 
ID   Q0UMA7_PHANO            Unreviewed;       489 AA.
AC   Q0UMA7;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAT85758.1};
GN   ORFNames=SNOG_07107 {ECO:0000313|EMBL:EAT85758.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT85758.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006955}.
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DR   EMBL; CH445334; EAT85758.1; -; Genomic_DNA.
DR   RefSeq; XP_001797460.1; XM_001797408.1.
DR   AlphaFoldDB; Q0UMA7; -.
DR   STRING; 321614.Q0UMA7; -.
DR   EnsemblFungi; SNOT_07107; SNOT_07107; SNOG_07107.
DR   GeneID; 5974350; -.
DR   KEGG; pno:SNOG_07107; -.
DR   VEuPathDB; FungiDB:JI435_071070; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   HOGENOM; CLU_020695_10_2_1; -.
DR   InParanoid; Q0UMA7; -.
DR   OMA; FMAYRPS; -.
DR   OrthoDB; 5474295at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0072687; C:meiotic spindle; IEA:EnsemblFungi.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR   GO; GO:0071958; C:new mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0140602; C:nucleolar peripheral inclusion body; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0071957; C:old mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR   GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0140013; P:meiotic nuclear division; IEA:EnsemblFungi.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0075297; P:negative regulation of ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IEA:EnsemblFungi.
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:UP000001055}.
FT   DOMAIN          255..339
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          348..462
FT                   /note="Cyclin C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01332"
FT   DOMAIN          352..433
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
SQ   SEQUENCE   489 AA;  54639 MW;  C6739DD1BB47A9CB CRC64;
     MPPAARALRQ RTVTNENDEN AATTRMTRAK AALGSHESAA DVPKKGLQVK KSTATLNGAA
     GTRKRAALGE VTNVTKTETV GAGGKVGGKK PLTTKVGPVT QASRPTKIEK ASRPATQSIL
     SKEKRTMSSE LKRPLSGSGI AGQPAKKRAT TSNGSKKEDV EEAENVMPAQ NVTAKPEVTK
     PTTKVEVLEE ELEEPITEAF VDLDKEDVDD PLMVSEYVVE IFEYLKELEI ATMANPDYME
     NQNELEWKMR GILVDWLLEV HTRFRLLPET LFLAVNIIDR FLSAKVVQLD RLQLVGVTAM
     FIASKYEEVL SPHVQNFRHV ADDGFTEDEI LSAERFVLAA LNYDLSYPNP MNFLRRISKA
     DNYDIQTRTL GKYLLEIGCL DHRFLAHPPS QVAAASMYLA RLVLDRGPWD ATLVHYSGYT
     EEEIQPVLQL MIDYLSSPVI HEAFFKKYAS KKFLKASIVL RQWAKKYVAE YGNVLEQSEE
     EDSQPRTKH
//
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