ID G1XDG7_ARTOA Unreviewed; 962 AA.
AC G1XDG7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=AOL_s00079g352 {ECO:0000313|EMBL:EGX48713.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX48713.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX48713.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(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. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX48713.1}.
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DR EMBL; ADOT01000139; EGX48713.1; -; Genomic_DNA.
DR RefSeq; XP_011122529.1; XM_011124227.1.
DR AlphaFoldDB; G1XDG7; -.
DR STRING; 756982.G1XDG7; -.
DR GeneID; 22893444; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_000288_26_2_1; -.
DR InParanoid; G1XDG7; -.
DR OMA; NFTHRVH; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000008784; 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: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; cd13279; PH_Cla4_Ste20; 1.
DR CDD; cd06614; STKc_PAK; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF6; SERINE_THREONINE-PROTEIN KINASE CLA4-RELATED; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 54..163
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 168..181
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 524..791
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 12..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 107712 MW; A688B5B3221A8EEE CRC64;
MATSGNYYYS PNSFMNPGPA PKPPSSRPNF PATPIHHQMN TLSIQRSTTA TVGGIQREGW
ASVKDDGFLT MWQKRYLVLR ETALDFHKND IKGSNAALSI PLKDITSVNR VEIKPFSFEM
IRFASSNQTS STNPDAPRKT MFIAVKNDTD LYGWIDDIYS RCPSMGGVSN PTNFAHKVHV
GFDPISGGFT GLPPEWEKLL NASAITKEDY QKNPEAVIEV LGFYTDRQKE DANQVYGMMP
GNGVNEKDLG MNYGAEPNNS SSSLPGSSTP SLSGYGNNQA FQDERLRREE EENRRYEERE
REYKRQMEEK VRREKEERER RDRQERERER ERREMAQQEQ EIEEQERRRE QEEREKERQR
AEKAAREREA RKKAEQQELL LQGGGGGSSS PGYTPKRVAP SAPGGSSARP PANLRQQPTA
LRAAPPAPNG TNGTRAPGQS PPAQPRAPAS PAQQHQRTQG TAQPAGNGIT PLNVKSKKEP
DAATLGAISA KKEQPKTRIS QMSEQQVMDK LRSVVSPGDP NQSYTKIKKV GQGASGSVYV
AKINTNAASE AARQYAHDQP NGKRVAIKQM DLAHQPRKEL IVNEILVMKE SQHPNIVNFL
DAFLKGTSEL WVIMEYMEGG ALTDVIDNNP LEEDHISTIC FETCKGLQHL HSQKIIHRDI
KSDNVLLDAA GHVKITDFGF CAKLTDQKAK RATMVGTPYW MAPEVVKQKE YGPKVDIWSL
GIMAIEMIES EPPYLNEEPL KALYLIATNG TPALKKPDKL SKELKSFLAF CLCVDVKSRA
TAEELLQHDF LQKGCPLHSV VERDEEEVAI MAVREMLMER EPRIRKAVGN KIPLYLIVED
PDEAYAVARG MMGSMTTDAV EESTGEAAKN TGKEMVKYEP RSVSTPPSSE LVRIPKTTMS
IADRRSFSSK PGPSTTTQPS EDVKTRKKER PALFLDLKKE VKPEPEPEKP RKRLWPFRRT
ST
//
