ID A0A3Q3RJ09_9TELE Unreviewed; 1721 AA.
AC A0A3Q3RJ09;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000002740.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000002740.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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 Ensembl; ENSMAMT00000002795.2; ENSMAMP00000002740.2; ENSMAMG00000001707.2.
DR GeneTree; ENSGT01030000234517; -.
DR InParanoid; A0A3Q3RJ09; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00132; CRIB; 1.
DR Gene3D; 1.20.5.340; -; 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; IPR014930; Myotonic_dystrophy_kinase_coil.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 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; 2.
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; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
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 74..340
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 341..411
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 986..1036
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1056..1175
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1201..1473
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1543..1556
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 622..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1572..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 713..794
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 884..925
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1586..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1721 AA; 194928 MW; 1FFFBD82F11A8822 CRC64;
MSAQVRLKRL EELLLERKAS GSLSVETLLD LLLCLYTEWS SSPLKREKHI TEFLEWVKPF
TTTVKEMRLH RDDFEMLKVI GRGAFGEVAV VKMKRTERVY AMKILNKWEM LKRAETACFR
EERDVLVKGD SQWITTLHYA FQDDNYLYLV MDYYVGGDLL TLLSKFEDRL PEDMAKFYVA
EMVLAIHSIH QQHYIHRDIK PDNVLLDVNG HIRLADFGSC LRMMEDGTVQ SSVAVGTPDY
ISPEILQAME DGMGRYGPEC DWWSLGVCMY EMLYGETPFY AESLVETYGK IMNHEERFQF
PSHVTDVSEE AKDLIQRLLC SRERRLGLNG ILDFKNHPFF SGIDWDNIRT AEAPYIPDVS
SPTDTSNFDV DDDVLKNPDI SPPMSHTGFT GQHLPFVGFT YTTDSCFSDR GSPSRVGLSL
RQEEVGGGAG GQEVEAFERR IRRLEQEKQE LNRKLQESTQ ALQAPARGGT LTRDREIKKL
NEEIERLKKK LADSDRLEHQ LEEAVTLRQD YESSTSKLKT LEKQVKTLRQ EKDDIHKQLS
ESLERLRSQT KELKEAHSQR KLALQEFSEL SERMAELRSS KQRLSRQLRD KEEEMDSLLQ
KLDAIRQEIR KTEKNRKELE AQLDDARAEA SKERKLREHS EVYSKQLETE LQSLKGRGAA
AGGSESQQEL SRLKAELDKK VLFYEEELLR RDSAHSSEIK NLRKDLHESE GAQLAVNKEL
LQLRDKLDKA KRDRQTEMDE AITALKEKYE REKNLLTEEN RKLTSETDKL CSFVDKLTAQ
NRQLEDNVQD LSSKKESVAH WEAQIAEIIQ WVSDEKDARG YLQALATKMT EELETLRSSS
LGTRPLDPLW KVRRSQKLDM SARLELQSAL DAEIRAKQLV QDELRKVKAA NISLESKLKE
SEERNREMGE QVESLKKEME ESRSHSDKGL KLPDFQDSIF EYFNTSPLAP DLTFRVSHMS
LCVYVGLMIP SPTYHSSGLS TPKPKAHQLS IKNFSSPTQC THCTSLMVGL IRQGYACEVC
SFICHVSCKD HAPLVCPIPA EQAKRPQGID VQRGIGTAYK GYIRIPKPSG VKKGWQRAFA
VVSDCKLFLY DVPEGKSTQP GVAASLVLDL RDEEFSVSSV LSSDVIHATR KDIPCIFRVT
SSQLSSQLSS VSLLVLAESE AEKKRWVLIL EGLQSILTKN LLKSQQVHVL HEAYDASLPI
IKTSLSAAVL DRERIVLGTE DGLYVVEVTR DVILRAVDSK KVYQIDLIPK EKIIALLCGR
NRHVHLHPWG VLEGAEPAFD IKLADTKGCQ ALATGVLRPG GPACLLAAVK RQVLCYEITR
LKPHHKRLWE VQAPGIVQWL GMVKERLCVG YPSGFALLAL QGESSPVSLV SPADPSLAFL
AQQPLDALHA LEVGSSELLL CFSELGIYVN GQGRRSRTQE LMWPSSPLAC SNASHLTVYS
EYGVDVFDIH TTEWVQTISL RKIRPLNIEG TLNLLSSEPP RLIYFSNTSS EGDLTIPETS
EHSRKLMMRT RSKRKFLFKV PEEERLQQRR EMRRDPELRS RMISNPTNFN HVAHMGPGDG
MQVLMDLPLS VMPSSQDDSF RDKSRPLSTI SRQQRAKTHI TRTASGGAST RSISEPDQDL
DREPDSDSTK HSTPSNSSNP SSPPSPNSPH RNPTSWIPEG AGLDEASGPL TECLDFTLRI
LLWQGKFKLP AAFILLDLPA GKPHPLVLTQ LLADSCCVLD L
//
