ID A0A067QHK0_9AGAM Unreviewed; 660 AA.
AC A0A067QHK0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=JAAARDRAFT_120371 {ECO:0000313|EMBL:KDQ62967.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ62967.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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DR EMBL; KL197710; KDQ62967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067QHK0; -.
DR STRING; 933084.A0A067QHK0; -.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; A0A067QHK0; -.
DR OrthoDB; 1700376at2759; -.
DR Proteomes; UP000027265; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013896; SNF1_UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027265}.
FT DOMAIN 17..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 511..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 74154 MW; EB904B1200FADAD7 CRC64;
MTTSSQSVFP ASKLGEYTVI KDIAEGTFGK VKMAMHTVTG HKVAMKFISK QVIHATRTKT
RVQREVEYMR TLRHPHIIKL YEVISTPTDI IIVLEYAGGE LFNYIVANGR MPEPQARRFF
QQLMSGIEYS HRLKIVHRDL KPENVLLDDD LNVKIADFGL SNEIKDGDFL KTSCGSPNYA
APEVIRGGLY TGPEIDVWSC GVILYVMLCG RLPFEDEDVQ TLFTKISQGQ YHMPSYLSPD
ARGLINSMLA VDPVKRITVP EILTHPFFTT DLPTYLEPLP PAPGPVLGTL SSLVVPPKQL
DFEIIEGLGR IEEDVVNELA TRMEGVDKEE VWECLRRDDG PQGNAVKVAY MLLRDKKRLG
KNLADFEEQE RAAQLAAMDP RYPISPNALS PTTQDLEENP FESEFNDFDD DDDDDDDDLD
IGLDFSTPEF EVNNFAVLNS SLPEQLPEQH HLTSYASAKR SFPAVKEKKQ HRTKWHFGIR
SRSPPMEVML EIYRTLRALG MEWKEKRDLG GLGGIRKETN GTTNGHANTG RKSGDRRVER
NKDMDGSGYV DLKRAASIYF VETRARVQDV VVLMNLQLYM VDSINYLVDF HHKKSYKASA
EPGAGKFDMA NPDTSLSETA SESGRSLTTE KGLKEEDVVS PFVFMDVACR LILELAGGGE
//
