ID A0A3B4ZDJ1_9TELE Unreviewed; 1813 AA.
AC A0A3B4ZDJ1;
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 Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000006525.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000006525.1}
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; 144197.ENSSPAP00000006525; -.
DR Ensembl; ENSSPAT00000006660.1; ENSSPAP00000006525.1; ENSSPAG00000004971.1.
DR GeneTree; ENSGT00940000157091; -.
DR Proteomes; UP000261400; 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 828..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 936..955
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1098..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1548..1778
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 530..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1784..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1721
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-1"
FT BINDING 1578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
SQ SEQUENCE 1813 AA; 204811 MW; 002CAA4496BABEAC CRC64;
YILPVSKDPH RCLPGCQVCQ QLVRCCCGRL VRQHVGFTAS LATKYSDVKL GENPNLSMPE
LEEWSVEKHT EASPTDAYGV INFQGGSHSY RAKYVRLSHD SRPESILRLM LKEWHMELPK
ILISVHGGVQ NFELHPRIKQ VVGKGLIKAA VTTGAWILTG GVNTGVAKHV GDALKEHCSG
SSKKICTIGI APWGVIENRN DLIGRDIIAP YQTLLNPLSK LNVLNNLHSH FLLVDDGTVG
KYGAEVKLRR DLEKHINLQR IHARIGQGVP VVALIFEGGP NLILTVLEYL QESPPVPVVV
CEGTGRAADI LAYVHKQTEE GGGLPDGVET DIIATIKKTF NFSQSDAIHL FQTLMECMKS
KELITVFHIS SEEHQDIDVA ILRALLQGTN ASAFDQLVLT LAWDRVDIAK NHVFVYGQQL
LVSSLEQAML DALVMDRVDF VKLLIENGVS MHRFLTISRL EELYNMKQPP NNPTLLHLVR
DVKQSHLPPN YKITLIDVGL VIEYLMGGTY RCNYTRKRFR IIYNNLHGNS RRSGRHTAGP
ASHLRKNHES FSMQADKKEK TRHNHFIKTA QPYKPKSSTE QNKKRSKEEI VDIDDPETRR
FPYPFNELLV WAVLMKRQKM SLFFWQHGEE NMAKALVACK LCRSMGYEAK KSDVVDDTSE
ELKEYSNEFG TLAVDLLEQS FRQDETMAMK LLTYELKNWS NSTCLKLAVS SHLRPFVAHT
CTQMLLSDMW MGRLNMRKNS WYKVILSILV PPAILLLEYK SKAEMAHIPQ SQDDHQMTME
DSEHNFQNIA EDIQMDVFKE ARSHDQVEVK SDMETHVRSR KLPLTRKIYA FYHAPIVKFW
SNTLFYLGYL MLYTYVVLVK MPELPSPQEW VVILYIFTSA IEKIREMFMS EAGKISQKIK
VWFSDYFNVS DFLAIVTFFI GFGLRLGGGD TFVPGRTVYC LNIIFWYVRL LDILAVNQQA
GPYVMMIAKM VANMFYIVVI MAIVLLSYGV PRKAILYPNE EPSWTLAKDV VFQPYWMMYG
EVYAYEIDVC ANNSDQSVKN LCTAGVWLTP LLQAVYLFVQ YILMVNLLIA FFNNVYLQVK
SISNLVWKYQ RYHFIMVYHE KPVLPPPFIL LCHIYSLFCM CRKRKKENTY GPKLFLTEED
QKKLHDFEEQ CVETYFHEKD DQFHSGSEER IRLTSERVET MCLQLKEVGN KVNFIKRSLH
TLDSQIGHLQ DLSALTVDTL KTLTAQRASE ASKVHNQITR ELSLSKNVVP SIAPVATDTG
PHSKSSVIGK RSVGAYFGSS FPQAGANIAD SLFGTGVEGG HGTESRRRLG PSPGTELGLD
PTLNPALSPE RRGLFGLGHL AAEAGSSGSA GSSAFVQSAV AISPPELRLR GHSLTQSKLT
RPQEPGLSDS PSSLPNVPSP GAQFHISSTP SQPSGSSHPD LALVGLYQQP LQPDNTSVEF
GAFVGKYENE VESGPDGHGH IRAVNSYAGF TEFDRNPAFL HPDSTQSTGL WSSFICSRLI
SCFFVCVCFV AVERNNLMRL SQSIPFTPVP PRGEPVTVYR LEESSPNTIN NSMSSWAQRG
LCAKIEFLSK EEMGGGLRRA LKVLCTWSEY DILKPGHLYI VKSFLPEVVQ TWQSIYKEDT
VLHLCLREIQ QQRAAQKLTF AFNQIRPKTI PYSPRFLEVF LLYCHSAGQW FAIEECITGE
FRKFNNNNGD EIVPTNLLEE TMLAFSHWTY EYTRGELLVL DLQGVGEILT DPSVIKSGEK
GSYDMIFGPA NLGDDAIRNF RAKHHCNSCC RKLKLPDLKR NEYTPDKVTF PQEDPPNPGG
GVKESRQSMR LML
//
