ID A0A2G5HFX4_CERBT Unreviewed; 834 AA.
AC A0A2G5HFX4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CB0940_09712 {ECO:0000313|EMBL:PIA91441.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA91441.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA91441.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA91441.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA91441.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKMD01000106; PIA91441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HFX4; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000230605; Chromosome 7.
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:0000313|EMBL:PIA91441.1};
KW Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:PIA91441.1}.
FT DOMAIN 76..174
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 179..192
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 544..813
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..520
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 33..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 92234 MW; 68C1D4D4CB2039A1 CRC64;
MAGNQPNTLY RPDQFMNPGP APPPPTDRRP KVTLTPNVYN TPGNPNLKYV GNDSDSSLNA
SQSSLGRTAT SNGEMTVIKD GWAKVKEEGG GFMKAFWNER FLVLREKQLD FLKSSSTNKT
TSVIYLKDVS HVTRSDNYPY SLEITRDGNK IWILKFDTDT EVYNWMDNIY DRCPQMGGVS
HPTGFSHRVH VGFDPVTGGF VGLPVEWERL LKGSALTKDD MAKNPQAVME VLQFYTDKLQ
VRADDPKSYP SLTPTPSAEN NANKQLGYSA GNGVTPPRPQ PPGASRQDSN YSATSQSRAP
GSGYGSGASR DQSTDRRNED ERRRRQEEQR ERQRRLDEEQ ERRRREQEDR EYNESLPKHK
LPLAKQEVGG GGYSDSSSRD ASPGNGQSRY NASRPAPPAP SQSKSGSTLP IRNLQAQRAA
PSPPQNGGST PAKKPGAPAQ SPYAVKQPSP ANGGQSRKDE APLTRKPSET GHQKQPSASG
QVKPLNVATK QPTGKPDAVK QAEAALTKKD PEPKKEVRMS AMSDAQVMDR LRSVVTLSNP
LESYNKQKKI GQGASGSVYV ARVRENAPSS TAQNLIKQYG PKAQVAIKQM DLRSQPRKEL
IVNEIIVMKE SRHDNIVNFL DAFLQEETFE LWVVMEFMEG GALTDVIDNN ASITEDQIAT
ICLETCKGLI HLHAQNIIHR DIKSDNVLLS SRGAVKITDF GFCAKLTEQR SKRATMVGTP
YWMAPEVVKQ KEYGSKVDIW SLGIMAIEMI ESEPPYLNEE PLKALYLIAT NGTPRLKKPE
KLSKELKAFL SVCLCVDVKS RATAEELGRH EFLQHGCSLA SLSELLRFRK GGGH
//
