ID A0A2S7QN48_9HELO Unreviewed; 1181 AA.
AC A0A2S7QN48;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=CJF32_00005730 {ECO:0000313|EMBL:PQE27977.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE27977.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE27977.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE27977.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PQE27977.1}.
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DR EMBL; NJPR01000070; PQE27977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7QN48; -.
DR STRING; 2070412.A0A2S7QN48; -.
DR InParanoid; A0A2S7QN48; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000238813; 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 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; 2.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 2.
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, ECO:0000313|EMBL:PQE27977.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000238813};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1181
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015548694"
FT DOMAIN 747..1043
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1046..1178
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 574..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..679
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1181 AA; 132885 MW; B55FC66A2B8DBA46 CRC64;
MGRPKACGEV VNNIFIFTAF VLILPWLVEA QQQQRSALKQ HESLPEVVNP EVLRTPLEAT
KIKTVETSVN LPRRKNTLSL NAKTHNRVDV SADSAPLAPS HLAKSGSLTS AGWGSSQPSA
RDLQDWEVED FVLLATVDGS VWARDRRTGK QKWRMNLPDV SMISTKHYRR NRSSALDEGY
ISSWTIDDYV WIVEPTEHGG LWIYRPDVPN GGLVNTGLTM KKLVDEMSPY QSDDPEVVYT
GSRKTQMVHI DATNGKVLQV FGGDYVVENR DESCTPNDNF MGRTADECQH PTLWLGLSRY
KVDIVGKDTR PIATLIYNEW GPNVQDAKKY GDKYHETLDS KYILAGQDGQ VMSFDRDRGR
DHEFLFQQKL PSPVVRVFDI FRPWGTEEKN PKLMMLPQPK PQSAAEDELL EMDQDRNSRV
VINLSDDGSF YAMSGKSYPL AVAGSQAQCY QRGLWKHESW QNLDEPELAE ALTGIHCIDE
QSEPRLTISG PLFEENQSQP SVPDLAPGLA PSPTIIQSFQ RLPRLAIDSL VEFVKNPVLF
LFLMILLISY QREIRAWIGR HGLKQWKATL TREERPLAVS TSQKSEDKKT ITLDDGSTTR
LPDIPEDKVV EPTTQDDAVA VLEPHGTKPV LVAPVEDMLI NEVSSSSEAV QDTSESLLAS
PEKKKERKRG RRGGVKHKKQ GNRSSTDGEK EVPRKPVTQK PPPTVEDAVR DAQNMFPPRK
LEPDIQTVSN DPAEVSGPII RIGALEVDQD KLVGTGSNGT MVFEGKFDGR AVAVKRMLIQ
FYDIASQETK LLRESDDHPN VIRYFAQQQA AGFLYIALEL CPASLADVIE KPHLHRELAR
GGEKDLPNVL YQIANGLQHL HNLRIVHRDL KPQNILVAMG KNGKPRLLVS DFGLCKKLEG
EQSSFRATTA HAAGTSGWRA PELLLDDDVK QGAAMIDTST DGGGSGSILV SSDVMPNRRA
TRAIDIFSLG LVFFYVLTKG SHPFDCGDRY MREVNIRKDN FNLAHLEVLG DYAFEAKDLI
ASMLAKEPKS RPVAQQVMAH PFFWPAKKRL NFLCDVSDHF EKEKRDPPSP ALQELEKWAP
DVCQGDFLKP LGKEFVDSLG KQRKYTGTRL LDLLRALRNK KNHYEDMPDK LKKDVGPLPD
GYLSFWTRKF PNLLIVCWNV IYEVQWDEID RFREYYEPAG L
//
