ID A0A3Q1BWR5_AMPOC Unreviewed; 1911 AA.
AC A0A3Q1BWR5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000019337.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000019337.1}
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=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 Ensembl; ENSAOCT00000029101.1; ENSAOCP00000019337.1; ENSAOCG00000024599.1.
DR GeneTree; ENSGT00940000157091; -.
DR Proteomes; UP000257160; 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 Reference proteome {ECO:0000313|Proteomes:UP000257160};
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 847..868
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 1646..1876
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 547..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1819
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-1"
FT BINDING 1676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1772
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1805
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1821
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1829
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1864
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
SQ SEQUENCE 1911 AA; 215907 MW; D25F1A49BFA674CC CRC64;
MSQKPWIEST FTKRECVYIL PVSKDPHRCL PGCQVCQQLV RCCCGRLVRQ HVGFTASLAT
KYSDVKLGEN PNLPMPELEE WSVEKHTEAS PTDAYGVVNF QGGSHSYRAK YVRLSHDSRP
ESILRLMLKE WHMELPKILI SVHGGVQNFE LHPRIKQVVG KGLIKAAVTT GAWILTGGVN
TGVAKHVGDA LKEHCSRSSK KICTIGIAPW GVIENRNDLI GRDIIAPYQT LLNPLSKLNV
LNSLHSHFLL VDDGTVGKYG AEVKLRRDLE KHINLQRIHA RIGQGVPVVA LIFEGGPNVI
LTVLEYLQES PPVPVVVCEG TGRAADILAY VHKQTEEGGG LPDGVETDII ATIKKTFNFS
QSDAIHLFQT LMECMKSKEL ITVFHISSEE HQDIDVAILR ALLQGTNASA FDQLVLTLAW
DRVDIAKNHV FVYGQQLLVS SLEQAMLDAL VMDRVDFVKL LIENGVSMHR FLTISRLEEL
YNMKQPPNNP TLLHLIRDVK QSHLPPNYKI TLIDVGLVIE YLMGGTYRCN YTRKRFRIIY
NNLHGNSRRS GRHTAGPGSH LRKSHESFSM QADKKEKTRH NHFIKTAQPY KPKLESSTEQ
SKKRSKEEIV DIDDPETRRF PYPFNELLVW AVLMKRQKMS LFFWHHGEEN MAKALVACKL
CRSMGYEAKK SDVVDDTSEE LKEYSNEFGT LAVDLLEQSF RQDETMAMKL LTYELKNWSN
STCLKLAVSS HLRPFVAHTC TQMLLSDMWM GRLNMRKNSW YKVILSILVP PAILLLEYKS
KAEMAHIPQS QDDHQMTMED SEHNFQNIAE DIQMDVFKEA RSHDQVEVKS EIETHVRSRK
LPLTRKIYAF YHAPIVKFWS NTLFYLGYLM LYTYVVLVKM PQWPSPQEWV VILYIFTSAI
EKIREMFMSE AGKISQKIKV WFSDYFNVSD FLAIVTFFVG FGLRLAGGDA FVPGRTVYCL
NIIFWYVRLL DILAVNQQAG PYVMMIAKMV ANMFYIVVIM AIVLLSYGVP RKAILYPNEE
PSWTLAKDVV FQPYWMMYGE VYAYEIDVCA NNSEQSVRGL CTAGVWLTPL LQAVYLFVQY
ILMVNLLIAF FNNVYLQVKS ISNLVWKYQR YHFIMAYHEK PVLPPPFILL CHIYSLFCMC
RKRKKENTYG PKLFLTEEDQ KKLHDFEEQC VETYFHEKDD QFHSGSEERI RLTSERVETM
CLQLKEVGNK VNFIKRSLHT LDSQIGHLQD LSALTVDTLK TLTAQRASEA SKVHNQITRE
LSLSKNVVPS IAPVATDTGP HSKSSIIGKR SVGAYFGSSF PQAGANIADS LFGTGVEGGH
GTESRRRVGP SPGTELGLDP TLNPAFSPER RGLFGLGHLA AEAGSSGSAG SSAFVQSAVA
ISPPELRLRG HSLTQSKLTR PQEPGLSDSP SSLPNVPSQG AQFHISSTPS QPSGSSHPEL
ALVGLYQQPL QPDNTSVEFG AFVGHKDSLD LHHSTPKEFS TSSRQQSPTT QTRSQVQPEG
HGHIRAVNSY AGFTEFDKNP AFLHPDSTLT KKDRSRVSAE DILIHEDPRA ALLERVQVKS
AQAISLRAPG EDTLSAAVSL YTPRHSHLGA RKDSIGSPFK PMESYQYSAV ERNNLMRLSQ
SIPFTPVPPR GEPVTVYRLE ESSPNTINNS MSSWAQRGLC AKIEFLSKEE MGGGLRRALK
VLCTWSEYDI LKPGHLYIVK SFLPEVVETW QSIYKEDTVL HLCLREIQQQ RAAQKLTFAF
NQIRPKTIPY SPRFLEVFLL YCHSAGQWFA IEECITGEFR KFNNNNGDEI VPTNLLEETM
LAFSHWTYEY TRGELLVLDL QGVGEILTDP SVIKSGEKGS YDMIFGPANL GDDAIRNFRA
KHHCNSCCRK LKLPDLKRNE YTPDKVTFPQ EDPPNSGGGV KESRQSMRLM L
//
