GENTAUR Molecular Products.

 A0A0D0YW08_9TREE        Unreviewed;       299 AA.
 A0A0D0YW08;
 29-APR-2015, integrated into UniProtKB/TrEMBL.
 29-APR-2015, sequence version 1.
 23-MAY-2018, entry version 19.
 SubName: Full=Unplaced genomic scaffold supercont2.6, whole genome shotgun sequence {ECO:0000313|EMBL:KIR87014.1};
 ORFNames=I308_02706 {ECO:0000313|EMBL:KIR87014.1};
 Cryptococcus gattii VGIV IND107.
 Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
 Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
 Cryptococcus gattii species complex.
 NCBI_TaxID=1296105 {ECO:0000313|EMBL:KIR87014.1, ECO:0000313|Proteomes:UP000054399};
 [1] {ECO:0000313|EMBL:KIR87014.1, ECO:0000313|Proteomes:UP000054399}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=IND107 {ECO:0000313|EMBL:KIR87014.1,
 ECO:0000313|Proteomes:UP000054399};
 The Broad Institute Genomics Platform;
 Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
 Dromer F., Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L.,
 Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S.,
 Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C., Naylor J.,
 Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
 Wortman J., Nusbaum C., Birren B.;
 "The Genome Sequence of Cryptococcus gattii IND107.";
 Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
 -!- SIMILARITY: Belongs to the protein kinase superfamily.
     {ECO:0000256|RuleBase:RU000304}.
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 EMBL; KN848860; KIR87014.1; -; Genomic_DNA.
 EnsemblFungi; KIR87014; KIR87014; I308_02706.
 Proteomes; UP000054399; Unassembled WGS sequence.
 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:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
 GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
 GO; GO:0005816; C:spindle pole body; IEA:EnsemblFungi.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; IEA:EnsemblFungi.
 GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:EnsemblFungi.
 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:0098783; P:correction of merotelic kinetochore attachment, mitotic; 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:1905785; P:negative regulation of anaphase-promoting complex-dependent catabolic process; IEA:EnsemblFungi.
 GO; GO:1902424; P:negative regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:EnsemblFungi.
 GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; 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:1903500; P:negative regulation of mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
 GO; GO:1903467; P:negative regulation of mitotic DNA replication initiation; IEA:EnsemblFungi.
 GO; GO:1902845; P:negative regulation of mitotic spindle elongation; IEA:EnsemblFungi.
 GO; GO:1904537; P:negative regulation of mitotic telomere tethering at nuclear periphery; IEA:EnsemblFungi.
 GO; GO:0032091; P:negative regulation of protein binding; IEA:EnsemblFungi.
 GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; 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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:EnsemblFungi.
 GO; GO:0031536; P:positive regulation of exit from mitosis; IEA:EnsemblFungi.
 GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
 GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; 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:1903380; P:positive regulation of mitotic chromosome condensation; IEA:EnsemblFungi.
 GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; 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:0042307; P:positive regulation of protein import into nucleus; IEA:EnsemblFungi.
 GO; GO:0031031; P:positive regulation of septation initiation signaling; 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: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:0072429; P:response to intra-S DNA damage checkpoint signaling; IEA:EnsemblFungi.
 GO; GO:1990820; P:response to mitotic DNA integrity checkpoint signaling; IEA:EnsemblFungi.
 GO; GO:0072435; P:response to mitotic G2 DNA damage checkpoint signaling; 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:UP000054399};
 Kinase {ECO:0000256|RuleBase:RU000304};
 Nucleotide-binding {ECO:0000256|RuleBase:RU000304};
 Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
 Transferase {ECO:0000256|RuleBase:RU000304}.
 DOMAIN        7    291       Protein kinase.
                              {ECO:0000259|PROSITE:PS50011}.
 SEQUENCE   299 AA;  33893 MW;  240FBA3E288B0005 CRC64;
 MCLDNKYKKI EKVGEGTYGV VFKAKDLETG NIVALKRIRL EAEDEGVPST SIREISLLKE
 LNQDDNIVKL LDIVHSEAKL YLVFEFLDMD LKKYMDTIGE NEGLGLDMVK KFSYQLVKGL
 YFCHGRRILH RDLKPQNLLI NKAGDLKIGD FGLARAFGIP LRTYTHEVVT LWYRAPEILL
 GSRHYSTAID MWSVGCIIAE MATRQPLFPG DSEIDEIFRI FRVLGTPDED VWPGVGGLPD
 YKPTFPQWHP VDLADVIHGF EPDGIDLIAQ TLVYNPSHRI SAKRALQHPY FDTVNLSAA

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