ID A0A5D6XL20_9STRA Unreviewed; 1253 AA.
AC A0A5D6XL20;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=PRKR-like endoplasmic reticulum kinase {ECO:0000256|ARBA:ARBA00041500};
DE Flags: Fragment;
GN ORFNames=PybrP1_004975 {ECO:0000313|EMBL:TYZ59330.1};
OS [Pythium] brassicae (nom. inval.).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC Globisporangium.
OX NCBI_TaxID=1485010 {ECO:0000313|EMBL:TYZ59330.1, ECO:0000313|Proteomes:UP000323770};
RN [1] {ECO:0000313|EMBL:TYZ59330.1, ECO:0000313|Proteomes:UP000323770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:TYZ59330.1,
RC ECO:0000313|Proteomes:UP000323770};
RA Kaundal R., Smith E.A., Mohammadi M., Stanghellini M.;
RT "Complete genome sequence of Pythium brassicum P1, an oomycete root
RT pathogen: insights into its host specificity to brassicaceae.";
RL Submitted (AUG-2019) 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:TYZ59330.1}.
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DR EMBL; SMMQ01003147; TYZ59330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D6XL20; -.
DR Proteomes; UP000323770; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProt.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR PANTHER; PTHR11042:SF189; SERINE_THREONINE-PROTEIN KINASE DDB_G0283301-RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF01011; PQQ; 1.
DR SMART; SM00564; PQQ; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000323770};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1253
FT /note="PRKR-like endoplasmic reticulum kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5022813326"
FT DOMAIN 744..1111
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 101..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 773
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1253
FT /evidence="ECO:0000313|EMBL:TYZ59330.1"
SQ SEQUENCE 1253 AA; 136651 MW; 751F41722D75CAA3 CRC64;
MAIGGGAGGR RRSRRVLLLA GALLATASSL PIALSASANR PNSPPRAWRT HPIELATADR
AVALQAHDIV VAGGVDGRVY ALNAWTGDTL WTFDSGGPMV DSSACGGGAP SQPQEPNRAA
QQQDPVHIIN LDTGEPERAA WADDGEQEGN LLGADERAMI EKRPRSAEMM AAGSAVLSEL
VPSYDGRLYH LSKAKKVKEL EMTMVDIINA NGPVRLADSG EDSDGLSDVI LFGEKRTEIF
ALDAASGLIQ PYHPIPAAGL HPATATASIL FGRAEFTTRA VHARNASATR CFKIAEYFLQ
FTAQPRCSRL DVGKPKSGSF VPEILVLPKD PDATEDDEGS TLAAYDPYTN QQLWEIEFPR
FDVLAVYGVS AARGTTFFQW NVDGPSSRAS LKQRNELAIR DGAVEKASIS SATEPTQQLQ
QLPEVASGEQ SRGDSSVAKP ASKQLTRVVP RNWVSMESQY RLRLLGDNYY LESSSEDGSN
LSGSEVSAKE AQFDDTRMDE LFAESIARRR KRRIFWEPIV NDGKRGVFIT YYHVGAMMVG
VMVGCLLIAW GCYVKGLSAS IAQSAIKSMD GNQFFMSHVH QLTIERPGEE NITISSVISR
PLLMSVLDHP LSLIADEESS SATRRRVSGI DVDIDAATEA ELMEKFARVA AMEAASALVG
STYSSTTATM MQLEYDASAD STAPVSSALV STESSAKDSD SSTSKSESSL ARKGSDASSS
DSSHATDAEA LFPFVCQSRF ANEFEEISAI GKGGFGQVIL AENRLDGRKY AIKRVGLHLK
NQTSKTLQKF LREVKILALL DHPNIVRYYQ AWLEKVEDSV SGLFGAPSDA DSSLTGAPGR
NYSMSNLLAP VSEMEFSENQ RSQMDFYSEG GRLDDDDDGG FEWERDSSAG ANEDQGWREE
DLIQSNSARQ RRRRRNVVAV NESAKESSTS DGLSAKNCDH WLFIQMQYCA GRNLGDYLAL
PNRPMHLPKL LKIFEHHVAA SSTTISSGGQ HIYSSSVWSV SMSNMSENEV TGGVGTYLYA
SPEQVAGKKY NAKTDVYSLG MILFELCHER FTTTMERYIA LRNARENKLP EEFRWKKVSP
ELLRMIARML SHDPSARPSV DEAVKWGQEM YEASLYQHAM SAMRSPLNPP RGFGDMAAAS
FDLLSLDGVS STFSFHVEAK TESVDGESGA AGGDRQLPNH NLLKEICDVI AHVGEDKVEI
KKCGLQLQAG VQILEFVLEA RLDEESDRER TGGDAYDYKA VVVAIEKLAG VHR
//