ID A0A067PS31_9AGAM Unreviewed; 343 AA.
AC A0A067PS31;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=JAAARDRAFT_130580 {ECO:0000313|EMBL:KDQ57544.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ57544.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; KL197719; KDQ57544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067PS31; -.
DR STRING; 933084.A0A067PS31; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; A0A067PS31; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000027265; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48012:SF34; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU000304};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000027265};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304}.
FT DOMAIN 10..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 343 AA; 38050 MW; E488349D9FBF0471 CRC64;
MTQQSVHQLY KRLKTVGKGA YGSVHKGVHL ATGNIVALKI INLDTDSDDV GDIQREVALL
TQLRDAPNVT KYYGCYLDGP RVWIVMEYAQ GGSVLNLMKA SRDGTLEERY VVVIVREVLA
GLSYLHKSGV IHRDIKAANI LITDVGKVMI CDFGVSALLP TATSKRNTFV GTPYWMAPEV
FQTVPAYDTK ADIWSLGIVI YEMIKGSPPH ANLQAAQLLQ LIPKAKPPRL AEADGSKDMR
DFVVNCLREL PSDRLPADEL TKTKWIKSAG KVSISILKDL VLQYDAWIQS GGTRASLAEP
LDWEEDEENE YVLTSSPPPR LQRSDVPYQA SRCNTGRRKH MGI
//
