ID A0A165LF18_9APHY Unreviewed; 1153 AA.
AC A0A165LF18;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=DAEQUDRAFT_718191 {ECO:0000313|EMBL:KZT64332.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT64332.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT64332.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT64332.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429132; KZT64332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165LF18; -.
DR STRING; 1314783.A0A165LF18; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
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; 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; IPR002372; PQQ_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; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
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:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1153
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007861628"
FT DOMAIN 719..1016
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1019..1151
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 126315 MW; E93C0D8046EED036 CRC64;
MSIRALLVAL LAAGKCIGEP VVSPWTANRD LSTDVDVRHN SYRPAPVSNA VNGLDLLDIV
LVASIDGRLH ALNRTSGDFI WSMKASSGTE PATLGPLVRT KHPDIDPDIT DDGSALGEVY
LVEPQSGDIY IMSTPDSPLQ RLPFSMPQLV DMSPFIFPSD DDGRMFVGRK ETSLLLVELE
TGRVKTMNHE CPWDPFQDLA EPAEFDLDLD DLEGSDPPKR ASSPTEVFIG RTDYHIAIHT
RPSRASPVRP PVQNLSFSVY GPNNQDLSIQ SVYRRTADNA YIQPLPNGEI ISFTSGAAHS
ADPNMEPTTE FAWGRAFSTP IVAVFDILRS PQRQQPLALL QPRLHLEDIL PSAELQKAAA
RQSLPFDAAF VGIVEETGSL FAMGPDTYPL VIFGDAGLGR FLDAAPRDTH FDDEFGRDQD
LPEELDSVAR RAKERRLRKM CREGSTDLRC LTGVRRLEAG TQSRFSRLLD AAPSESNANA
NAQGPQERSA MSAQVVLDPD QASAVGASNS ALFAFAVCAL ALLVAFVWTG LRRKSSKPSP
LNLAVVAGSQ EREKPVEKSV EEHAPDALPP TESNAVQNNP ALVNSPVRRR TMSTASRPGT
PRPSTPNKRP SDIVLLDPTA DLDGDAAEGD ESEKDGETEQ PAKRKGVRRK RGKKKRGGTA
GGGADDEKEN GDGVANDDVP NSHANGKADI GKAVVHVVSE SAAVVPPPSA STPVMPSLIV
SDTILGFGSH GTVVYKGSLQ GRAVAVKRLL QDFVTLASRE VDVLQESDDH PNVIRYYYQE
SRANFLYIAL ELCPASLADV IERPDEFQEI VGAFDPKRAL RQVTAGLRHL HALKIIHRDI
KPQNILISHA KRGAGHRMLI SDFGLCKKLD VDQTSFLPTA HGVMAAGTVG WRAPEILRGE
VKLDDTTGDD SHSGSSRGSV GTPRVGTPTG RPTRLTKSVD IFALGCLYYY VLTNGGHPFG
DRFEREVNIL KNAKSLEGLQ CFGEEGSEAA DLISRMLSPE AYDRPDTTSC LLHPYFWDPG
KRLTFLQDAS DRFEIMCRDP RDSNLTTLEM GAAQVVGNDW HSRLDKLFIE NLGKFRKYDG
KSVQDLLRAL RNKKHHYQDL PDNVKRLLGS MPEGFLAYFT RRFPNLFLHV HRVVADSSLR
TESMFRTYFD LSD
//
