ID L8FTR8_PSED2 Unreviewed; 1188 AA.
AC L8FTR8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=IRE protein kinase {ECO:0000313|EMBL:ELR03949.1};
GN ORFNames=GMDG_06477 {ECO:0000313|EMBL:ELR03949.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR03949.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) 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}.
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DR EMBL; GL573331; ELR03949.1; -; Genomic_DNA.
DR RefSeq; XP_012744916.1; XM_012889462.1.
DR AlphaFoldDB; L8FTR8; -.
DR STRING; 658429.L8FTR8; -.
DR VEuPathDB; FungiDB:GMDG_06477; -.
DR HOGENOM; CLU_004875_2_0_1; -.
DR InParanoid; L8FTR8; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000011064; 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-EC.
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 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 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; 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:ELR03949.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011064};
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..1188
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003989199"
FT DOMAIN 751..1050
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1053..1185
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 57..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..690
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 131908 MW; 17613F5596737F96 CRC64;
MPRRPPAEGT TASRILLAVV ILLSPWLIDA QQQQQNASRD VGDQYKSSRE AIKTDPIATL
EATTLGNKAQ RLESPVSAGR AKGTPGANKN KRENNGNDAS AIVAFAPAGS AVRAPSTGRS
SIGNNAGLSP QSARSLEDWD VEDFVLLATV DGKLYARDRK TGTQRWALDV DRPVVQTTYH
ERNGTDGEEH QPVDDYLWIV EPSADGSLFV YIPGGPQPGL VNTGLTMKKL VEEMVPYADT
EPAVVYTGDK VTSLWTIDAR NGAVLKWFGS AGSFSPGAAT CDRPDGFQDP DGEECSTRGT
LTLGRTEYTV GIQGKDGHPI VTLKYAEWGP NNYDQDLLRQ HRSTLDGKYM YSSHDGGVFA
YDLTRSRDRG ALYNARLPSP VIRVFDVARP VDADTKNPEL IILPQPIPPL VDDSHESIRH
ARIFVNHTET GDWYAMSGNS YPLVIDGPEQ AQCDTANWLE RARFHEPVNN AQLQKALVGL
HSIDGRRHEP LLTISGPTDQ DDKLQSKNET IHKDAVANMT SPALGPKPSV LYHVRQLPTT
AVTSIIELVN NPITTLLLLT LLFWYNRDIA RWIKSTCNKY INIISKLTGR LEEDEDVDDF
SNIDAPLKQD APVPETLPDV ATVGSSDPSD DAKPPTTNKQ DDKPADVANE ARREPLEEVT
ANDGSRPPKQ PKAEGKKAHR GKRGGLKHKK GQRQTPSSDG PIPSSPATVE DAVRDAKMLG
GSTRIEPDVE TLPNGVNEIS GPILRMNSLE VNMDKLIGTG SNGTMVFEGK FDGRDVAVKR
MLIQFFEIAS QETKLLRESD DHPNVIRYYA QQQSQGFLYI ALELCSASLA DVIEKPQLHR
DLAQSGERDL PNVLYQITNG LQHLHNLRIV HRDLKPQNIL VSMGKDGRPR LLVSDFGLCK
KLEGEQSSFR ATTAHAAGTS GWRAPELLLD DDLREGSVTA MESTLSSSHS TSGIPLVSGD
LMPNRRATRA IDIFSLGLVF FYVLTKGSHP FDCGDRYMRE VNIRKGEYKL SPLDVLGDYA
FEATDLIRSM LEQVPKARPT AKQVMSHPFF WSAKKRLNFL CDVSDHFEKE KRDPPSDALI
ELERWAPEIT RGDFMKPLGK EFTDSLGKQR KYTGSRLLDL LRALRNKKNH YEDMSDKLKK
DVGPLPEGYL SFWTRKFPNL LIGCWNVVYE VRWDEVDRFR EYYEPALL
//
