ID A0A3B3C6R2_ORYME Unreviewed; 1909 AA.
AC A0A3B3C6R2;
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 Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000012772.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000012772.1}
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR629601-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR629601-3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Alpha-type protein kinase family. ALPK subfamily.
CC {ECO:0000256|ARBA:ARBA00025760}.
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DR STRING; 30732.ENSOMEP00000012772; -.
DR PaxDb; 30732-ENSOMEP00000012772; -.
DR Ensembl; ENSOMET00000020219.1; ENSOMEP00000012772.1; ENSOMEG00000014236.1.
DR GeneTree; ENSGT00940000157091; -.
DR OrthoDB; 201873at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd16971; Alpha_kinase_ChaK1_TRMP7; 1.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR Gene3D; 1.20.5.1010; TRPM, tetramerisation domain; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029601; TRPM7_a-kinase_dom.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF8; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 7; 1.
DR PANTHER; PTHR13800; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL, SUBFAMILY M, MEMBER 6; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR629601-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR629601-3}.
FT TRANSMEM 863..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 925..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 955..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1096
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1644..1874
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 572..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1817
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-1"
FT BINDING 1674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1770
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1803
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1819
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1827
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1866
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
SQ SEQUENCE 1909 AA; 216042 MW; E71AA765BBC6C4FB CRC64;
MSQKPWIEVT FTKRECVYIL PVSKDPHRCL PGCQICQQLV RCCCGRLVRQ HAGFTASLAT
KYSDVKLGEN PNPPMPELEE WSVEKHTEAS PTDAYGVINF QGGSHSYRAK YVRLSYDSRP
ESVLRLMLKE WHMELPKILI SVHGGVQNFE LHPRIKQVVG KGLIKAAVTT GAWILTGGVN
TGVAKHVGDA LKEHCSRSAK KICTIGIAPW GVIENRNDLI GKDIIAPYQT LLNPLSKLNV
LNNLHSHFLL VDDGTVGKYG AEVKLRRDLE KHINLQRIHA RIGQGVPVVA LIFEGGPNVI
LNVLEYLQET PPVPVVVCEG TGRAADILAY VHKQTEEGGG LPDGVETDII ATIKKTFNFS
HSDAIHLFQM LMECMKSKEL ITVFDISSEE QQDIDVAILK ALLQGTNLSP FDQLVLTLAW
DRVDIAKNHV FVYGQQLLVS SLEQAMLDAL VMDRVDFVKL LIENGVSMHR FLTINRLEEL
YNTKQSPNNP TLLHLVRDVK QSNLPPNYKI TLIDVGLVIE YLMGGTYRCN YTRKRFRIIY
NNLHGNNRRS GRHAVGPGSH FRKNHEAFSM QADKKEKTRH NHFIKTAQPY KPKLDSSAEQ
NKKRSKEEIV DIDDPETRRF PYPFNELLVW AVLMKRQKMS LFFWQHGEEN MAKALVACKL
CRSMGYEAKK SDVVDDTSDE LKDYSNDFGT LAVDLLEQSF RQDETMAMKL LTYELKNWSN
STCLKLAVSS HLRPFVAHTC TQMLLSDMWM GRLNMRKNSW YKVILSILVP PAILLLEYKS
KAEMAHIPQS QDDHQMTMED SEHNFQNLHE DIQMDVFKEA RSHDHVEAKH DMETHVRSRK
LPLTRKIYAF YHAPIVKFWS NTLFYLGFLM LYTYVVLVKM IETPSTQEWV VIVYIFTSAI
EKIREMFMSE AGKISQKIKV WFSDYFNVSD FLAIVTFFIG FGLRLGGGEA FIPGRIVYCL
NIIFWYVRLL DILAVNQQAG PYVMMIAKMV ANMFYIVVIM IVVLLSYGVP RKAILYPNEE
PSWTLAKDVV FQPYWMMYGE VYAYEIDVCA NNSEESVRPL CAAGVWLTPF LQAVYLFVQY
ILMVNLLIAF FNNVYMQVKS ISNLVWKFQR YHFIMAYHDK PVLPPPFIFL CHVYSLFCMC
RKRKKESTYG PKLFLTEEDQ KKLHDFEEQC VETYFHEKDD QFHSGSEERI RLTSQRVETM
SLQLKEVGNK VNFIKRSLHT LDSQIGHLQD LSALTVDTLK TLAAQRASEA TKVHTQITRE
LSLSKNVVPS IVPMSTDSKS SAIVKHSVGA YFGSSFPQTG ANIADSLFGI GADLGAVTEN
RRRVAPSFGE EQGLDPTTNL PLSPEKKALI GLEYLAAEAG SSGSAGSGAF VHSTGAVSPP
ELRLRGHSLT HSKLTRPQEL PLSESPSSLP NVPSQGAQFH ISSTPSQPSG SSHPELSLAG
LQQQPLQRDS SSVEFGAFVG HKDSLDLQQP TPIETSSRRQ SPTTQTKSQL QGQPEGRGQM
RAVNSYAGFT EFDRKPAFLH PDSTLTKKDR SRVSAEDILI HEDPRAAVLE RVQVKSAQAT
SLRAPGEETL NVSAAVSLYA PRHSHLGVRK DSIGSPFKPM ESYQYSAVER NNLMRLSQSI
PFTPVPPRGE PVTVYRLEES SPNIINNSMS SWSQRGFCAK IEFLSKEEMG GGLRRALKVL
CTWSEYDILK PGHLYIVKSF LPEVVQTWQS IYKEDTVLHL CLREIQQQRA AQKLTFAFNQ
IRPKTIPYSP RFLEVFLLYC HSAGQWFAIE ECITGEFRKF NNNNGDEIVP TNLLEETMLA
FSHWTYEYTR GELLVLDLQG VGEILTDPSV IKSGEKGSYD MIFGPANLGD DAIRNFRAKH
HCNSCCRKLK LPDLKRNDYT PDKVTLPQDD PPNSGGGVKE SRQSMRLML
//
