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Cyclin-dependent kinase 1 (EC 2.7.11.22)

 W1Q7A7_OGAPD            Unreviewed;       317 AA.
W1Q7A7;
19-MAR-2014, integrated into UniProtKB/TrEMBL.
19-MAR-2014, sequence version 1.
23-MAY-2018, entry version 24.
SubName: Full=Cyclin-dependent kinase 1 {ECO:0000313|EMBL:ESW96234.1};
EC=2.7.11.22 {ECO:0000313|EMBL:ESW96234.1};
ORFNames=HPODL_02864 {ECO:0000313|EMBL:ESW96234.1};
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 /
NRRL Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Pichiaceae; Ogataea.
NCBI_TaxID=871575 {ECO:0000313|EMBL:ESW96234.1, ECO:0000313|Proteomes:UP000008673};
[1] {ECO:0000313|Proteomes:UP000008673}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
{ECO:0000313|Proteomes:UP000008673};
Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
"Genome sequence of the methylotrophic yeast Hansenula polymorpha
DL1.";
Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
-!- SIMILARITY: Belongs to the protein kinase superfamily.
{ECO:0000256|RuleBase:RU000304}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ESW96234.1}.
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EMBL; AEOI02000010; ESW96234.1; -; Genomic_DNA.
RefSeq; XP_013932664.1; XM_014077189.1.
EnsemblFungi; ESW96234; ESW96234; HPODL_02864.
GeneID; 25772312; -.
Proteomes; UP000008673; Chromosome VII.
GO; GO:0000235; C:astral microtubule; IEA:EnsemblFungi.
GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:EnsemblFungi.
GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
GO; GO:0005816; C:spindle pole body; IEA:EnsemblFungi.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
GO; GO:0000993; F:RNA polymerase II core binding; IEA:EnsemblFungi.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:EnsemblFungi.
GO; GO:0044257; P:cellular protein catabolic process; IEA:EnsemblFungi.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
GO; GO:0000706; P:meiotic DNA double-strand break processing; IEA:EnsemblFungi.
GO; GO:1990758; P:mitotic sister chromatid biorientation; IEA:EnsemblFungi.
GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:EnsemblFungi.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:EnsemblFungi.
GO; GO:0045875; P:negative regulation of sister chromatid cohesion; IEA:EnsemblFungi.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:EnsemblFungi.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:EnsemblFungi.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi.
GO; GO:0045819; P:positive regulation of glycogen catabolic process; IEA:EnsemblFungi.
GO; GO:0051446; P:positive regulation of meiotic cell cycle; IEA:EnsemblFungi.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:EnsemblFungi.
GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IEA:EnsemblFungi.
GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:EnsemblFungi.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
GO; GO:1901319; P:positive regulation of trehalose catabolic process; IEA:EnsemblFungi.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:EnsemblFungi.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IEA:EnsemblFungi.
GO; GO:1990139; P:protein localization to nuclear periphery; IEA:EnsemblFungi.
GO; GO:1902889; P:protein localization to spindle microtubule; IEA:EnsemblFungi.
GO; GO:0010568; P:regulation of budding cell apical bud growth; IEA:EnsemblFungi.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IEA:EnsemblFungi.
GO; GO:0010570; P:regulation of filamentous growth; IEA:EnsemblFungi.
GO; GO:0060303; P:regulation of nucleosome density; IEA:EnsemblFungi.
GO; GO:1905634; P:regulation of protein localization to chromatin; IEA:EnsemblFungi.
GO; GO:0090169; P:regulation of spindle assembly; IEA:EnsemblFungi.
GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IEA:EnsemblFungi.
GO; GO:0007130; P:synaptonemal complex assembly; IEA:EnsemblFungi.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|RuleBase:RU000304};
Complete proteome {ECO:0000313|Proteomes:UP000008673};
Kinase {ECO:0000256|RuleBase:RU000304};
Nucleotide-binding {ECO:0000256|RuleBase:RU000304};
Reference proteome {ECO:0000313|Proteomes:UP000008673};
Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
Transferase {ECO:0000256|RuleBase:RU000304}.
DOMAIN 7 292 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
SEQUENCE 317 AA; 36308 MW; 6C53531272381AD6 CRC64;
MAELNDFEKL EKIGEGTYGV VYKALDTKHN NRVVALKKIR LESEDEGVPS TTIREISLLK
ELRDDNIVAL YDIVHSNSNK IYLVFEFLDM DLKKYMESIP EGEGLGNDMV KKFMLQLVRG
LYHCHAHRVL HRDLKPQNLL IDKEGNLKVA DFGLARAFGV PLRAYTHEVV TLWYRSPEIL
LGGKQYSTGV DMWSIGCIFA EMSNRKPLFA GDSEIDQIFK IFRVLGTPTE EIWPDVTYLS
DFKPSFPKWS KQNLADIVPN LDPHGVDLLE QLLTYDPAGR ISAKRALMHP YFQEDYVQPS
EYPQQSAMQV DTSTIYV


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