ID A0A3B3UG63_9TELE Unreviewed; 1047 AA.
AC A0A3B3UG63;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000011597.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000011597.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3B3UG63; -.
DR Ensembl; ENSPLAT00000019043.1; ENSPLAP00000011597.1; ENSPLAG00000014780.1.
DR GeneTree; ENSGT00940000165054; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd09769; Luminal_IRE1; 1.
DR CDD; cd10422; RNase_Ire1; 1.
DR CDD; cd13982; STKc_IRE1; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 5.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1047
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017279807"
FT DOMAIN 554..815
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 818..946
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 372..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 118124 MW; E6D33BC833FBF4E9 CRC64;
MATPIKIVWC TFGFCSASTV ALPESLLFVS TLDGNLHAVS KKSGSIKWTL KEDPVLQVPT
HVAEPAFLPD PNDGSLYSLG GKNNEGLTKL PFTIPELVQA SPCRSSDGIL YMGKKQDLWY
VVDLLTGEKQ QTLTSSFAEM LCPSSSLLYL GRTEYTITMY DTKNRELRWN ATYSDYASTL
PDDDMKYKMA HFVSNGDGLV VTVDSETGDV QWVQNYNSPV VAMYIWQRDG LRKVPHTNVA
VETLRYLTFM SGEVGRITQW KYPFPKEKKP KNKFMATLYV GKYSTSLYAS PSLVHDGVTV
VPRGSTFPLL EGPDSQETEE DKECVITPST SVKFNAGLRE RNRINFMRNY LLLIGHHETP
PEAHTKILET FPENFPRNQG NVIPPTTDKK GEEKVNDSGM DDRQPSTSIQ EPGTSSRTAR
PEAPVDSMLK DMATIIFSTF LLAGWVAFVI IYPKSVHKQQ QLQHQEFQRQ MEERLELLQR
QQPFSPADVG LAPDGDFLDV ARTRSDCSDH SSPNVTPRAS NHSNLSVSEV GSSIYEHEDG
EEDFSTVRVG NITFHPKQVL GHGAEGTMVY KGQFDNRPVA VKRILPECFS FADREVQLLR
ESDEHPNVIR YFCTERDRQF QYIAIELCAA TLQEYVEKKD FNRHGLEPVM LLQQTMSGLA
HLHSLKIVHR DLKPHNILVS MPNAHGRVRA MISDFGLCKK LAVGRHSFSR RSGVPGTEGW
IAPEVLSEDF KDNPTYAVDI FSAGCVFYYV VSQGSHPFGK SLQRQANILL GGYSLDYLQS
DKHGEIVARD LIEQMLSMDP QRRPSAESVL KHPFFWTLEK ELQFFQDVSD RIEKEPLDGP
IVRQLERGGR AVVKGDWREH ITVPLQTDLR KFRSYKGGSV RDLLRAMRNK KHHYRELPIE
VQETLGSIPD DFVSYFTSRF PHLLMHTYLA MRTCAPERPF LPYYPTAEQL QKTQSQGLQR
LTEPCTQPLP DHTTLPTLQT QESTPLTQCG QSLPSSREHP VPSDFSVHAA HPEVLGLTPP
SENVSQWPAV PLRPEVLAIL DDKTSAN
//