ID A0A0Q3XB31_AMAAE Unreviewed; 939 AA.
AC A0A0Q3XB31;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=AAES_11956 {ECO:0000313|EMBL:KQL61357.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL61357.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL61357.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL61357.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQL61357.1}.
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DR EMBL; LMAW01000001; KQL61357.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3XB31; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
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:SF15; SERINE_THREONINE-PROTEIN KINASE_ENDORIBONUCLEASE IRE2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQL61357.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 540..801
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 804..932
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 402..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 104250 MW; 514B4C8BA85C1D31 CRC64;
MGSKADPGER RAKGCQGLKG GAVTVPETLL FVSTLDGNLH AVSKSTGDIK WTLKDDPILQ
VPVYVAEPAF LPDPNDGSLY ILGGKNKEGL MKLPFTIPEL VQSSPCRSSD GVLYTGKKQD
TWVIVDPKSG EKQTTLSTEA WDGLXPSSPL LYIGRTQYVI TMYDTKSREL RWNATFSEYS
APLCEERYHY KMAHFASSGD GLVVTLDKES GEVLWAHNYG SPVVGIYVWH QDSLXRVPHL
NLAMETLRYL TFHSQDIHVR KWSHQSLKDF TSTKTQLLPA LYVGKHATSF YALTSLVHSS
VALVGITLAR IDGPTTEEVT MRESGECEIT PSTDVKYPQG SITTLRNQWL LIGHHELPPV
VHTTMLRAFP ESLRKTTETI IPRAPSARTL FDDFLAPSSV EEPAIRSKEQ FPSDPAPGEQ
MEMYPDPSAW DLVMAAVGTA LLGGGVLLLL LTRLQRRHVE QQQQLEKQIQ LLQQQQEMLL
PGRASREAAA AEPGLSQGRA SQHSGHQKDL ANGTASPDPA GPAAAEDAEP HVIVVGKVSF
NPKXVLGHGA GGTFVFRGXF EGRNVAVKRL LPECFHLVDR EVRLLRESDE HPHVVRYFCT
ERDKQFHYIA IELCSATLQE YVESPSFDRR GLDPVSLLRQ TMSGLAHLHS LSIAHRDLKP
CNILISVPNP HGQIRAIISD FGLCKKLQGG RQSFSLRSGI PGTEGWIAPE VLQEAPKENP
TCAVDIFSAG CIFYYVLSGG QHPFGDSXRR QANILSGSYQ LSCLEEEAHD KLVARDLIVA
MISPXPQHXP SAPVVLVHPF FWSQEKQLQF FQDVSDRIEK EPAEGPIASA LEAGGRAVVR
TNWRMHISLP LQTDLRKFRT YKGASVRDLL RAMRNKKHHY HELPAEVRAA LGSVPDAFVH
YFTSRFPRLL LHTHRAMRVC AHERLFHSYY CQGPGGDGK
//
