ID A0A0D9P6H7_METAN Unreviewed; 845 AA.
AC A0A0D9P6H7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=H634G_03145 {ECO:0000313|EMBL:KJK81882.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK81882.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(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};
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. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; KE384725; KJK81882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9P6H7; -.
DR STRING; 1291518.A0A0D9P6H7; -.
DR Proteomes; UP000054544; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR CDD; cd06614; STKc_PAK; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 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|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 261..274
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 566..817
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 845 AA; 92024 MW; 55EE7F919A12C6DD CRC64;
MDGPASSFNG HSQRRKLVKK PPSHTYTRSS SGLDDSHSLG SRRSSQSLRR APSAPAVRSS
IANTSSSSSP RHPTASQWPS NASPSIAQGD FLATSNPPSG PGLITSSLSS PSNPAASPYP
ALAHRPNRLS DSLARRHSKE PSDDLLGAPF DGAAILSRIE SVKYTAPRES VQRPPASPAL
AKPITGTRNV NPALRASQSF SNMEPAITEK IQGGKAPDGA AAAPKRYSDE GKDSKPPMIR
KKSGFSGFVT SLVGSQKKPT ISAPENPVHV THVGYDSATG QFTGLPKEWQ RLINESGIPE
KERRENPQTM VDILQFYKET TERPPEDQIL EKFHHAGPAE NRSYNTPTSP NMYPTNYMGS
FENPRAPPPV PPSRSHGRDM MPSRPAPKPP VSISNRSGPS SAYPTKDSGI GMSQQPDDYS
PQSKDSSPML PEEHRSRSNS RANGQSPYSP LTPSSAQVAA YQQQQFVQQQ HEQALAQAQA
AMSGHVGRAP SKRQPQPQAS VPAPHQTAAY ARAVDANGHS NASRQQAGPG AVPGARPRQR
ARQSNGIDVV TSLKRICSEG DPREVFRGFQ KIGQGASGGV FTGFERGTNR LVAIKQMNLE
QQPKKDLIIN EILVMKDSSH PNIVNFIDSY LCAGELWVVM EFMEGGSLTD VVTFNIMTEG
QIASVCRETL KGLQHLHSKG VIHRDIKSDN ILLSNEGSIK LTDFGFCATI NEAQNKRTTM
VGTPYWMAPE VVTRKEYGRK VDIWSLGIMA IEMIEGEPPY LTESPLRALW LIATNGTPQI
KNEAELSLVF RDFLCFALKV DPEKRASAHD LLRHEFMKQC VDLAQLAPLV RAAREQRAQE
KARKQ
//
