ID A0A3B4UXS7_SERDU Unreviewed; 1677 AA.
AC A0A3B4UXS7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000022695.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000022695.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR STRING; 41447.ENSSDUP00000022695; -.
DR Ensembl; ENSSDUT00000023110.1; ENSSDUP00000022695.1; ENSSDUG00000016488.1.
DR GeneTree; ENSGT01030000234517; -.
DR OMA; CGRSHHV; -.
DR Proteomes; UP000261420; 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 CDD; cd01243; PH_MRCK; 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 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 997..1047
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1067..1186
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1212..1485
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1555..1568
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 616..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 720..801
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 616..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1669
FT /note="Pro 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 1677 AA; 189406 MW; 3CCCA7D77D145854 CRC64;
MSAQVRLKRL EELLLEQKAA GCLSVETLLD LLLCLYTECS HSPLKREKHI TDFLEWVKPF
TTTVKDMRLH RDDFEMLKVI GRGAFGEVAV VKMKHTERVY AMKILNKWEM LKRAETACFR
EERDVLVKGD SQWITTLHYA FQDDNYLYLV MDYYVGGDLL TLLSKFEDRL PEDMSKFYVA
EMVLAIHSIH QQHYIHRDIK PDNVLLDVNG HIRLADFGSC LRMMEDGTVQ SSVAVGTPDY
ISPEILQAME DGMGRYGPEC DWWSLGVCMY EMLYGETPFY AESLVETYGK IMNHEERFQF
PSHVTDVSED AKDLIQRLLC SRERRLGLNG ISDFKSHPFF TGIDWDNIRS AEAPYIPDVS
SPTDTSNFDV DDDVLKNPDI GPPVSHTGFT GQHLPFVGFT YTTDSCFSDC SSVCRAGLLS
RQEEEGGGGG GEGGGQEVEA FERRIRRLEQ EKQELNRRLQ ESTQALQAPA RGGTLTRDKE
IKKLNEEIER LKKKLADSDR LEHQLEEAVT LRQDYESSAS KLKTLEKQVK TLRQEKDDVH
KQLSDSLERL RSQTKELKEA HSQRKLALQE FSELSERMAE LRSFKQRLSR QLRDKEEETD
ALLQKMDAMR QEIRKTEKNR KELEAQLDDA KAEASKERKL REHSEVYSKQ LETELESLKS
QQGRGAAARG AESQQELSRL KAELDKKVLF YEEELLRRDS AHSSEIKNLR KDLHESEGAQ
LAANKELLQL RDKLDKAKRD RQTEMDEVVA ALKEKNEREK NLLTEENRKL TAETDKLCSF
VDKLTAQNRQ LEDDLQDLSS KKESVAHWEA QIAEIIQWVS DEKDARGYLQ ALATKMTEEL
ETLRSSSLGT RPLDPLWKVR RSQKLDMSAR LELQSALDAE IRAKQLVQEE LRKVKAANIN
LESKLKDSEE RSREMGEQME NLKKEMEESR SRSDKGLKLP DFQDSIFEYF NTSPLAPDLT
FRVSHLSTTD IDSTPQKSET TSPSPSPSTT SDNEPKAHQL SIKTFSSPTQ CTHCTSLMVG
LIRQGYACEV CSFICHVSCK DYAPLVCPIP AEQAKRPQGV DVQRGIGTAY KGYVRIPKPS
GVKKGWQRAF AVVSDCKLFL YDVPEGKSTQ PGVVASLVLD LRDEEFSVSS VLASDVIHAT
RKDIPCIFRV TSSQLISQLS SVSLLVLAES EVEKRKWVRI LEGLQSILTK NLLKSRQVHV
LHEAYDASLP VIKTTLSAAV LDRERIALGT EDGLFVIEVT RDVIVRAVDS KKVYQIDLIP
KDKIIALLGG RNRQVHLHPW GVLDGAEPAF DFKLTDTKGC QALTTGVLRP GGPACLLAAV
KRQVQCYEIT PVRPHHKRLW EVQAPGVVQW LGMVRERLCV GYPSGFALLA LQGESSPISL
VSPADPSLAF LSQQPLDALH ALEVGSSELL LCFSSLGIYV DGQGRRSRTQ ELMWPATPLA
CSSNSSHLTV YSEYGVDVFD IHTTEWVQTI SLRKIRPLNV EGTLNLLSSE PPRLIYFSNT
SSEGDLTIPE TSDHSRKLMV RTRSKRKFLF KVPEEERLQQ RREMLRDPEL RSKMISNPTN
FNHVAHMGPG DGMQVLMDLP LVTPLLCAAS SSCRHVLLPH LLPPLTALFI TLTPPLFSPP
LPPVSLPSPP PLRPPPLLRL PDSDSTKHST PSNSSTPDPP SPKLPHTQPA HPGRPGL
//
