ID A0A3B3T6F7_9TELE Unreviewed; 563 AA.
AC A0A3B3T6F7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Serine/threonine kinase 3 {ECO:0000313|Ensembl:ENSPKIP00000038742.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000038742.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000038742.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the NIPA family.
CC {ECO:0000256|ARBA:ARBA00007230}.
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DR AlphaFoldDB; A0A3B3T6F7; -.
DR STRING; 1676925.ENSPKIP00000038742; -.
DR Ensembl; ENSPKIT00000019736.1; ENSPKIP00000038742.1; ENSPKIG00000016383.1.
DR GeneTree; ENSGT00940000154984; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR CDD; cd06612; STKc_MST1_2; 1.
DR Gene3D; 1.10.287.4270; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR008521; Mg_trans_NIPA.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF23; SERINE_THREONINE-PROTEIN KINASE 3; 1.
DR Pfam; PF05653; Mg_trans_NIPA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 439..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 300..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 563 AA; 62652 MW; B2F8CFA5C8E4B1E6 CRC64;
MEPSAPKSKL KKLSEDSLTK QPEEVFDVLE KLGEGSYGSV YKAIHKESGQ VVAIKQVPVE
SDLQEIIKEI SIMQQCDSPY VVKYYGSYFK NTDLWIVMEY CGAGSVSDII RLRNKTLTED
EIATILKSTL KGLEYLHFMR KIHRDIKAGN ILLNTEGHAK LADFGVAGQL TDTMAKRNTV
IGTPFWMAPE VIQEIGYNCV ADIWSLGITS IEMAEGKPPY ADIHPMRAIF MIPTNPPPTF
RKPELWTDEF TDFVKKCLVK NPEQRATATQ LLQHPFIKNA KPVSILRDLI TEAMDIKAKR
HQEQQRELEE DEENSEEEVE VDSHTMVKTS SESTGTMRAT GTMSDGAQTM IEHGSTMLDS
DLGTMVINSD EEEEEDSTMK RNATSQQAQR PSFMDYFDKQ DPKGKAQENC NQNRPDSYHI
AKNVFPDNWK VPQDGDFDFT YLIGIVIAIC GNFLISISLN IQKYTHMRQA QSGSKPYYTS
SLWWCGIALM GIGELGNFAA YGFAPASLIA PLGCVSVIGK APPSVGHALL LHPVCCLFRA
RSGSGGTVEL PQHLSHTNPS CAG
//