ID A0A3Q1G0N3_9TELE Unreviewed; 1673 AA.
AC A0A3Q1G0N3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000024171.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000024171.1}
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 Ensembl; ENSAPOT00000009504.1; ENSAPOP00000024171.1; ENSAPOG00000006654.1.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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: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 CDD; cd05597; STKc_DMPK_like; 1.
DR Gene3D; 1.10.287.1490; -; 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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE/THREONINE-PROTEIN KINASE MRCK ALPHA; 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; 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 SUPFAM; SSF69322; Tricorn protease domain 2; 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 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
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..239
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 240..310
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 952..1002
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1022..1142
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1168..1440
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1512..1525
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 528..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 608..720
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 786..841
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1551..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1673 AA; 189303 MW; AB83AA5752A0807D CRC64;
MKILNKWEML KRAETACFRE ERDVLVNGDC QWITTLHYAF QDDSNLYLVM DYYVGGDLLT
LLSKFEDRLP EEMAKFYLAE MVLAIDSVHQ LHYVHRDIKP DNLLLDMNGH IRLADFGSCL
KLMEDGTVQS SVAVGTPDYI SPEILQAMED GKGKYGPECD WWSLGVCMYE MLYGETPFYA
ESLVETYGKI MNHKERFQFP QQITDVSEDA KDLIRRLICS REHRLGQNGI EDFKQHPFFT
GIDWDNIRTC EAPYIPEVSS PTDTSNFDVD DDCLKNSETM PPPSHTAFSG HHLPFVGFTY
TSKCTISDRG CLRQLAGEPG KAGLDQVDVE VQRSLEDSLA TEAYERRIRR LEQEKLELSR
KLQESTQTVQ ALQHPTGEGI VSTNKEVEIR SLKSEIDILK KQIADSGQLE KQLEDVTSAR
RDLEDSSKHI KTLEKQIKSV TQERDDFQKD LMEASEKLKS QSKELKEAHS QRKLAMHEFS
ELNEKLTDLR SAKQRLTRQL RDKEEEMESQ SQKVEALRLE VRKAERAKKE MDAQAEEQAA
ETQKEKKLRE RNEQYSRQLE EELEGLKVKQ AGSSAAPASA DQSQEVARLR GEMEKKTLLY
EEELGRREAQ HCTELKALRK ELRDAESQHL TLQKEILMLK DKLDKTRRES QSEREEFETE
YKQKYERERV LLTEENKKLS SEVDKLTGMF EDVSSSNRQL EDEMRELADK KESVAHWEAQ
ITEIIQWVSD EKDARGYLQA LATKMTEELE GLRNTSLGAR ATDMPWKMRR FAKLDMSARL
ELQSALDTEI RAKQSIQDEL NKVKANSIST ECKLQEVESK NQDLLAEIDR LKKETEELRL
RRGVKHQDSQ NSFLAFLNAP TSALDQFDRS PSVGPTSKGR RVDSMDNFTP SNTPSREDDP
KSHLKSRSRS PSMASDMEPI ELIDHPPRSV QTPTMRSGGY GSIGRSSPKP KAHQFIVKSF
NTPTKCNQCT SLMVGLIRQG CTCEVCNFSC HVTCADKAPA VCPVPQDQTK GPLGIDPQRG
IGTAYEGHVR VPKPTGVKKG WQRAMAVVCD FKLFLYELGE GKATQPSVVV SQVIDMRDEE
FSVSSVLASD VIHASRKDIP CIFRVTASQL SPSSSHKPSI LILADSDQER NKWVGLLNEL
HRILKKNKLK ERFVYVPKEA YDSTLPLIKT TQSAAIIDHE RVALGNEEGL FVIHVTKDEI
IRVGDNKKVH HIDLIPQEQL LAVISGRNRH VRLFPTQALD GRETESYKLA ETKGCQTVVS
GPVRNGSLTC LCVAMKRQII CYEVNKSKGR HRRLRELQAP GPVQWMGLLS ERLCVGYQSG
FMRYSVHGDT SPVSLLHHED HTLAFIPQQG LDALCAVEIS SKELLLCFSA IGVYVDSQGR
RSRQQELMWP AVPNAACYNA PYLSVYSENA VDVFDVNTME WIQTIPLKKV RPLNVDGSLN
LLGLETVRLI YFRNKMAEGD ELVVPETSDN SRKQMVRSMN NKRRFSFRVP EEERLQQRRE
MLRDPEMRNK LISNPTNFNH VAHMGPGDGI QILKDLPMNV RVQESRAGFS GSVSIPSITK
NRAEPGRSMS ASSGLGIRSS SQNGSALRRE LSGGSYGSKR QTMTSPSESS LSSGGGMDCG
DAPLSQFDRE DSDSPRHSTA SNSSTFSSPP SPASPHKTKS LSLESTDRMG WDT
//