ID I3KS58_ORENI Unreviewed; 1641 AA.
AC I3KS58;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000023954.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000023954.2}
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}.
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DR STRING; 8128.ENSONIP00000023953; -.
DR Ensembl; ENSONIT00000023975.2; ENSONIP00000023954.2; ENSONIG00000019024.2.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_3_1; -.
DR OMA; CGRSHHV; -.
DR Proteomes; UP000005207; Linkage group LG15.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP 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; 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; 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:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1614..1634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..280
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 281..351
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 980..1101
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1127..1399
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1469..1482
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 537..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 609..736
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 819..867
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 904..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1641 AA; 185063 MW; 92525FF6D19199C0 CRC64;
MSAQERLKRL EKLLLEQRAA GCLSVEALLD LLLCFYTECS QSPLKREKHV TDFLEWVKPF
TTTVKDMRLH KDDFEILKVI GRGAFGEYLV MDYYVGGDLL TLLSKFEDRL PEDMAKFYVA
EMVLAIHSIH QQHYIHRDIK PDNVLLDVNG HIRLADFGSC LRMMEDGTVQ SSVAVGTPDY
ISPEILQAME DGMGRYGPEC DWWSLGVCMY EMLYGETPFY AESLVETYGK IMNHEERFQF
PSHVTDVSED AKDLIQRLLC SRERRLGLNG ISDFKSHPFF NAIDWDNIRS TGAPYIPEVS
SPTDTSNFDV DDDVLKNPDI GPPVSHTGFT GQHLPFVGFT YTTDSCFSDR SSVSRAGLRV
QIETDGGAGG EEVEVFEKRI RRLEQEKQEL NRKLQESTQA LQAPARGGTL SRDKEIKKLN
EEIERLKKKL ADSDRLEHQL EEAVSLRQDY ESSASKMRSL EKQVKSLRQE KDEVHKQLAD
ALERLRSQTK ELKEAHSQRK LALQEFSELS ERMAELRSSK QRLTRQLRDK EEEMEALLQK
MDGTRQEIRK MEKSRKELEA QLDEAQTEAS KERKLREHSE VYSKQLEAEL QSLKSQQGRG
VAAGGAEFHQ ELSRLKAELD KKVVFYEEEL LRRDSAHSSE IKNLRKDLQE SEGAQLTANK
ELLQLRDKLD KAKRDRQVEM EEALTALKEK HEREKNLLTE ENRKLTTETD KLCSFVDNLT
AQNRQLEDEL QDLASKKESV AHWEAQITEI IQWVSDEKDA RGYLQALATK MTEELETLRS
SSLGTRPLDP LWKVRRSQKL DMSARLELQS ALDAEIRAKQ LVQEELRKVK ASNINLESKL
KETEERSKEM VEQMETLKKE MEETRSRSDK GLKLPDFQDP IFEYFNTSPL APDLTFRPSD
IDATPAKSDT TPPSPSTGSE NEEIKAVPSS PSPIYQSTAL TTPKPKAHQL SIKTFSSPPQ
CTHCTSLMVG LIRQGYACEG MQRESALHIR IPKPSGVKKG WQRAFAVVSD CKLFLYDIPE
GKSTQPGVAA GLVLDLRDED LSVSSVLASD VIHATRKDIP CIFRVTSSQL ISQLSSVSLL
VLAESEVEKR KWVRILEGMQ SIVTKNLLKS QQVHVLHEAY DASLPIIKTT LSAAVLDRER
IALGTEEGLF VVEVTRDVIV RAADSKKISQ IELIPKEKII ALLCGRNRQV HLHPWGVLEG
AESSFDAKLA DTKGCQAMAA GVLRPGGPPA FSMSRFQVQC YEITPGKPHH KKLWEVQAPG
LVQWLGMLRD RLCIGYPSGF ALLALQGESS PISLVSPADP SLSFLAQQPL DALHALEVGS
SELLLCFSQL GVYVDGQGRR SRTQELMWPA TPLAFCSNSS HLTVYSEYGV DVFDIHTTEW
VQTISLRKIR PLNVEGTLNL LSSEPPRLIY FSNTSSEGDL TIPETSDHSR KLMVRTRSKR
KFLFKVPEEE RLQQRREMLR DPELRSKMIS NPTNFNHVAH MGPGDGMQVL MDLPLSVMPS
SHDDSIKDKP RPLSSISRQQ RSKTHITRTA SDFGGGASSR SICDPDEMDR EPDSDSTKHS
TPSNSSNPSS PPAPTPPTAA SSPSTAWTPK PEAPPLPERV GLWTESLAFT LRVLLWRGVF
ALPAAFYFVG FYLLGSPTPC F
//
