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Database: UniProt
Entry: A0A3Q1G0N3_9TELE
LinkDB: A0A3Q1G0N3_9TELE
Original site: A0A3Q1G0N3_9TELE 
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
//
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