ID F0XPD9_GROCL Unreviewed; 819 AA.
AC F0XPD9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CMQ_7406 {ECO:0000313|EMBL:EFX00404.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX00404.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00023596}.
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DR EMBL; GL629801; EFX00404.1; -; Genomic_DNA.
DR RefSeq; XP_014169886.1; XM_014314411.1.
DR AlphaFoldDB; F0XPD9; -.
DR STRING; 655863.F0XPD9; -.
DR GeneID; 25980947; -.
DR eggNOG; KOG0670; Eukaryota.
DR HOGENOM; CLU_000288_5_5_1; -.
DR InParanoid; F0XPD9; -.
DR OrthoDB; 232702at2759; -.
DR Proteomes; UP000007796; 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-EC.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14135; STKc_PRP4; 1.
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 InterPro; IPR044092; STKc_PRP4.
DR PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR PANTHER; PTHR24058:SF103; MITOGEN-ACTIVATED PROTEIN KINASE-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:0000313|EMBL:EFX00404.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Transferase {ECO:0000313|EMBL:EFX00404.1}.
FT DOMAIN 489..813
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 819 AA; 90353 MW; 537299C9CB6285BA CRC64;
MASTRSSADE GEIVEGHRAE QSKAKTHAAP AASALHRDGN RPSVDRRDRN HRGRSPRSPE
RPGAGAGVPY RNLSPRGLKR QRDDRNRDRD RWDNRRGGRR YEDESVRDRR DRELRYDDTG
NRGKRQRTRS RSPPPPADRG NNGRGWNDRS RQDRGRDGGR DGGRDRDWGD RSGRRPYDVH
QAESVPGQGP QQRSARSAAA AAGLAGNGVA KSVKGVSFHL SGESGPVRPG KELPVPQDWA
EPEPIDEEAE IRRRRQRREE ILKKSRASTP LQAVSIQADK AAAPTAVESN TQVKSPETGN
NTPRSGETPK QSVAVEDAFA DSAIVDSSLT RGEAAESEGL LDLADDRAFM DALGKHAIGD
GPDVEDGPSA ADYDPTVDME IDERRDELRH GLTAAVEMDL SSEAADVTAP DTGNNDGGDD
SDEDDMFAED FVEKKYVAPT TTANGTADTA AAKDAAAAAA PANGGGILEG DDQQGYYKIR
PGEVLDGRYQ VLTALGKGMF SGVGRARDIA SADGKREVAI KIMRNNDALR KGGYTEIAIL
EKLNEADAND KKHIVRFERA FDYRGHLCMA FENLSMNLRE VLKKFGNNVV INLTGVRVFA
YQIFVALAHM RRCSIIHADL KPDNILVNET RTALKICDLG TAIDRSDAVT AHNEITPYLV
SRFYRAPEII LGMPYDHAID MWSIGCTLYE LYTGKILFAG ESNNQMLRAI MEIRGKISAK
LYRRGDLWPM HFDDMGGFLS QEHDKFQAKT TVKTLTVIKP TRDLRTRLLA ASAGMDDAET
KELNQFHDLL DRCLSLNPDK RILPGDALKH PFFTQRSAR
//
