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Unplaced genomic scaffold scaffold_201, whole genome shotgun sequence

 A0A0D0DRL6_9HOMO        Unreviewed;       294 AA.
A0A0D0DRL6;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
05-JUL-2017, entry version 13.
SubName: Full=Unplaced genomic scaffold scaffold_201, whole genome shotgun sequence {ECO:0000313|EMBL:KIK95748.1};
ORFNames=PAXRUDRAFT_826701 {ECO:0000313|EMBL:KIK95748.1};
Paxillus rubicundulus Ve08.2h10.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Agaricomycetidae; Boletales; Paxilineae; Paxillaceae;
Paxillus.
NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK95748.1, ECO:0000313|Proteomes:UP000054538};
[1] {ECO:0000313|EMBL:KIK95748.1, ECO:0000313|Proteomes:UP000054538}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK95748.1,
ECO:0000313|Proteomes:UP000054538};
DOE Joint Genome Institute;
Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
Nordberg H.P., Cantor M.N., Hua S.X.;
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000054538}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
DOE Joint Genome Institute;
Mycorrhizal Genomics Consortium;
Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
"Evolutionary Origins and Diversification of the Mycorrhizal
Mutualists.";
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; KN825023; KIK95748.1; -; Genomic_DNA.
EnsemblFungi; KIK95748; KIK95748; PAXRUDRAFT_826701.
Proteomes; UP000054538; 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:0005829; C:cytosol; 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: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:0098783; P:correction of merotelic kinetochore attachment, mitotic; 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: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: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:0045875; P:negative regulation of sister chromatid cohesion; IEA:EnsemblFungi.
GO; GO:0007070; P:negative regulation of transcription from RNA polymerase II promoter during mitotic cell cycle; 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: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:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:EnsemblFungi.
GO; GO:0031031; P:positive regulation of septation initiation signaling; IEA:EnsemblFungi.
GO; GO:0010696; P:positive regulation of spindle pole body separation; IEA:EnsemblFungi.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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:1990139; P:protein localization to nuclear periphery; IEA:EnsemblFungi.
GO; GO:1902002; P:protein phosphorylation involved in cellular protein catabolic process; IEA:EnsemblFungi.
GO; GO:1990802; P:protein phosphorylation involved in DNA double-strand break processing; IEA:EnsemblFungi.
GO; GO:1990804; P:protein phosphorylation involved in double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
GO; GO:1990801; P:protein phosphorylation involved in mitotic spindle assembly; IEA:EnsemblFungi.
GO; GO:1990803; P:protein phosphorylation involved in 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:0072434; P:signal transduction involved in mitotic G2 DNA damage checkpoint; IEA:EnsemblFungi.
GO; GO:0007130; P:synaptonemal complex assembly; IEA:EnsemblFungi.
GO; GO:0016192; P:vesicle-mediated transport; IEA:EnsemblFungi.
InterPro; IPR011009; Kinase-like_dom.
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:UP000054538};
Kinase {ECO:0000256|RuleBase:RU000304};
Nucleotide-binding {ECO:0000256|RuleBase:RU000304};
Reference proteome {ECO:0000313|Proteomes:UP000054538};
Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
Transferase {ECO:0000256|RuleBase:RU000304}.
DOMAIN 4 289 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
SEQUENCE 294 AA; 33852 MW; 6B16E5BE96D8A755 CRC64;
MDRYAKIEKV GEGTYGVVYK AKDVTTNQIV ALKKIRLEAE DEGVPSTAIR EISLLKELKD
DNIVRLLDIV HADQKLYLVF EFLDVDLKRY MEHANSSGSP ISIEISKKFT HQLSSGLLYC
HSHRILHRDL KPQNLLIDKR NNLKLADFGL ARAFGIPMRT YTHEVVTLWY RAPEVLLGSR
HYSTAIDMWS VGCIFAEMVM RGNPLFPGDS EIDQIFKIFR ILGTPNEQVW PGVSQLPDYK
ETFPQWSKQE LRNIVPNLDD MGIDLLARTL TYDTAKRISA KRALVHPWFE DYNL


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