ID A0A1Y2WQR5_9PEZI Unreviewed; 1215 AA.
AC A0A1Y2WQR5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=K445DRAFT_15558 {ECO:0000313|EMBL:OTB11497.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB11497.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB11497.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB11497.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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 EMBL; KZ112962; OTB11497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2WQR5; -.
DR STRING; 1001832.A0A1Y2WQR5; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000243732; 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: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 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; 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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954:SF6; ENDORIBONUCLEASE; 1.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01011; PQQ; 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; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000243732};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1215
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012531104"
FT DOMAIN 782..1076
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1079..1211
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 93..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 810
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1215 AA; 135175 MW; 211E04612632B1A4 CRC64;
MLRRPPGEGR LVVQQHKVLL ALAVFLLPWL QFVDAQQQQP RQQSPPEPAS IANLVSDYSK
DNNIVVDKHD VHARDVPILR HDSFGTERVV GNLATATPSK ARNHREAPAA SRRNSVTTKK
QRLRNVPFPN DASALATLAP APSVRAPNSP RYLPSLLAGA GLSSPQTARS LEKWEVEDYI
LLATVDGHLY AVNRESGDER WHLQVEQPIV ETIHRRPNGS VADGRDGHDH HPLDDYIWAV
EPTRNGALYV WTPSGFGNGL MSTGLTMKQL VEEFGSYAVQ NPPVVYTGHK KTTMITLDAA
TGRVLKWFGQ GGSQVDQSAT CFPPNGRFVD SDSEECSDSG TITLSRTEYI VNIHRSDDGR
EIATLKYAEW GPNNFDNDLH QQYRVTQDNR YFTSQHDGKV YALVYPTGVT SFALQFSVPV
ARVFDIARPE DAPPGSNPEL VLLPQPVPPA RDEDSARARS HSVFLNQTES GSWYAMSGWS
YPLIVDAPAA QLNLRNRRDS ENPWDTLDTT WVNKALVGTH ILGNARAAAQ WPSSIPPSLP
SSPFTPESDN DDNESAVPTP FPDIGSDPPG IVDSIVALPQ YAADKTVDFF MNPILFPVLI
YLLFRYYKDL VRWSKRRIKP KQYLDTVTYV RPTDPAVNPQ PEAADEIVQA PVVEVDEKQQ
EPSVTEPESA EKAALITVTA VELEPAPVDE NREQQQTEGE SPEKKKKAHR GRRGGVKHRK
GAKKQRDTAE SSGENGTPDA GEGIPGLQNI GMPSKLEPNV TIVNNDPEDV SGPIVKIGGI
EVNQDEQLGM GSNGTIVFAG KFHGRDVAVK RMLTQFWDIA TQETQLLLES DHHPNVIRYF
AMSKNDSFLY IALELCQASL SDIIEKPALF QDLARAGEMD LPRVLLQIAH GLGFLHDLRI
VHRDLKPQNI LVTMGRDGKP RLLVSDFGLC KKLEGGQSSF GATTAHAAGT SGWRAPELLL
DDDARESSNM SMTSTHSDSS QLISADVMPN RRATRAIDIF SLGLVFFYVL TKGLHPFDCG
DRYMREVNIR KGQFSLKPLD VLGDVAHEAK ALIETMLRSD PRARPSAKDV MSHPFFWSAK
ERLAFLCDVS DHFELEPRDP PSKALMELEA CAPQVCRGDF LKVLPKEFVE SLGRQRKYTG
SKLLDLLRAL RNKRFHYGDM SEPLKKIVGP LPDGYLSFWT RRFPNLLIVC CTVIYKLNLE
ELDTFKEYFK PRTPL
//