ID A0A3Q1EC88_9TELE Unreviewed; 885 AA.
AC A0A3Q1EC88;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000001083.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000001083.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1EC88; -.
DR Ensembl; ENSAPOT00000015759.1; ENSAPOP00000001083.1; ENSAPOG00000002325.1.
DR GeneTree; ENSGT00940000165262; -.
DR Proteomes; UP000257200; 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; 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:SF30; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000257200};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..885
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018719362"
FT DOMAIN 490..750
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 753..881
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 330..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 98380 MW; C23F8F20556B14FD CRC64;
MTLLFLMCLQ KLPFTIPELV QSAPCRSSDG VLYTGKKQDV WFVVDPETGE KQTSLTTSSS
ESICPNTPLL YIGRTEYVVT MFDTKTQELR WNATYNDYSA PPYDEKQDYK MAHLVSSGDG
LVVTVDRESG DVLWSQNFGS PVIGVYLYSG DSLRHAPHLS LAMETLRFLT FSSASDQTDA
HSTLKWSYQF VKEQASAQAQ LVPTLYVGKL DSHLYASTSL VHQGVSLVPR GLTLARIEGP
VTAEVTVRER GECEITPSTD VRYPPGSTNS HKNHWLLIGH HELPPVAHTT MLRDFPVSLQ
RSGEAVIPPR SSASPASYYH ERYFQTVAGG HSDVNANKGG ADGSTSGQAQ RPATVLPVYM
TQDRLTLAVL TLLLGGWLAF ALTYPTRAAQ QLKAQRQLEE AFESRLQQMQ TNMQTSTQTN
TQTATSVSSD VTLSTDANVS SDSLTASPDP PPGPHSHNNS TSDGDKNGSS GQNLAAEGNS
EEVQVGKISF TTAEVLGHGT AGTFVFRGKF DGRHVAVKRI LPECFEVAER EVQLLRESDT
HPNVIRYFCT ERDRLFTYIA IELCAATLQQ YVEDPSCFSE LSPITLLEQT MCGLSHLHSL
NIVHRDLKPR NILLSGPSAL GRVRALISDF GLCKKIPDGR SSFSLRSGIP GTEGWIAPEV
LRDTPGNKPT AAVDVFSAGC VFYYVISRGQ HPFGDALRRQ VNILSGEYSL SHFMEDIHDD
VIAQDLTEQM ISAEAESRPS TACVLKHPFF WSPEKQLLFF QDVSDRIEKE PAESPIVVRL
ETAGRAVVRT NWRMHISVPL QTDLRRFRTY KGNSVRDLLR AMRNKKHHYH ELPPEVQETL
GELPEGFVSY FTSRFPRLLM HTHAALHICS HERLFHPYYL PPTFK
//