ID A0A1I8BZ05_MELHA Unreviewed; 1707 AA.
AC A0A1I8BZ05;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Meloidogyne hapla (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne.
OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig78.frz3.fgene2};
RN [1] {ECO:0000313|WBParaSite:MhA1_Contig78.frz3.fgene2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR WBParaSite; MhA1_Contig78.frz3.fgene2; MhA1_Contig78.frz3.fgene2; MhA1_Contig78.frz3.fgene2.
DR OMA; SYCEGYL; -.
DR Proteomes; UP000095281; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd00132; CRIB; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 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.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..192
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 193..265
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 904..954
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 973..1141
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1169..1471
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1535..1548
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 290..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..401
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 426..488
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 546..620
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 721..776
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 293..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1707 AA; 193548 MW; 582F85D8942B6129 CRC64;
MDYYVGGDLL TLLSKFEDEH GHVPEHMAKF YVAEMVLAID SIHRLGYVHR DIKPDNVLLD
INGHIKLGDF GSCLRRKSDG TVCATTAVGT PDYISPETLR AVEDGRGRYG AECDWWSLGI
CMYEMIYGET PFYAESLVDT YGKIMNHEEM FEFPEEVEIS DDAKDLISHL ICSRDKRLGS
NGLEDFRSHP FFFDIDWENI RSMNAPYKPE VSSPTDTSNF DPSVIANDFT PCETQPPKVT
AAFSGLHLPF IGFTYTSESV FSDRLNLLDS IQLLLRSFSG VNCTQFSSPI KLNRRTETEK
QDEDDKEPPP REPQPPEFSL PDQQGHIVAQ LKDENQILRK MLEDEKNQRP VKQVGIEELE
KKIRDSKEKN RQLILDKQDL QKELEEISER YNSQAREWKN AIKQRDVALR DFEETNSELV
ETKTSLSSCE QNFKEKDALA RQLQEKCDIY KSELRSALAS RAEADAKLAL LTKELANERS
TKNVLESKFG EESSESIQVE QDNYVESDNC GDGTGDELLK TYKEKQLFEF EEKKRNDAIG
YFKGKIEDLQ QLLNEQKLAE QKLRGEHEED KLSWNRQHQE HLFSVEKLFS TRVKALEAEL
KDLRIENEQM HGVNNRLEQE LLCQQRMGVQ IQEIIQFVAD GKERQELLQD VTSRLAGELE
SFKKGLSIQA PQNSATREQQ QSNGSYANTP ISIVESPLRT WGSRRMNKQA KYGRFEAQQH
LEAEIRAKQR AQEESRQART RCDELERELV EMRRKLEKQR DEYERIMDEN TTLKQQHWAI
RHWPQRLEAI SQGTIGEVEH KQYRFNAGIF NNSAVSIPST PPNTRSCLID DPEGQLFQPK
VAMIGGHHQQ YPFHPQFYEN ARFYTSYRQD DSLSSLGSPT SSIFRSATSP KAIQSLNNAF
NGKGHHFVHA SLRTPTKCIA CTSVLIGADR QGMFCQDCHV ACHVSCLTKV PADCPVPLEM
RRSDGIDMVR GTGTAYQGAV KTPKYGGVKR GWQKTYVFVC DFKLYLYDCQ TDKNGKVTAI
EPQIRQILDM KDPDFKVSSA TENDAIHASK SDLPKIFKVV FSQIHDFHSC TAVFEPENSN
NKSATMRSHG STSSGGSAAA AFEQSQYQKE CALISQQYSL LMAESKEEAE KWVVALNELR
DLFCRSGFLR KDTFVVRELY DLSAFPSQLR NVKCAAVIDQ GRFVIGLADQ GLLSVELDRE
VLIPVGGESE NKKKNVEEVE YDAEEQLLIV LIPTAALDGR DLKWIKVQET RGCHLLCWGT
GPHVTNTSAN RQHYFATALN KSVLVFQINR SERRHSAMRE RAIPGQPQSL SISQGRLFVG
YPSSFRVWDL LDNSQISLVN LEDGSLQFLN QTLHDAEMII SVWPQRDSDN DKSIDTKHPE
LQQSREERPK EYLLVFQKLG LYVDANGRRS RSQELMFPCR GSTQSSFAYR TSHLLHFSEH
QICVFKVQTA EWVQTINLRL SRPLHSNGLF VLCQILDLPH LVMLGSNQPA PVEKLFLSFS
ESKQVGLPLR KRKFTVRSAK DDARCRGDRR SQLPISGPSN FMHVVHMGPG NVLDLKNLAE
LNASNSPGCS TGGSNANIAE RNFRQQLGQQ QPLMRSTSTS SGSTQGQSTT TLSWMPTVTG
AIPSTRPLSS HSRNSEASSL GKTTGKFTQQ QLLKYQQQQQ SQELESNDDY YLEPILKKGQ
QPSTAGASPA APPAPPSIPQ PKIPDDK
//
