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Database: UniProt
Entry: A0A1Y2WQR5_9PEZI
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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}.
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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
//
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