ID A0A553ICZ9_9PEZI Unreviewed; 1200 AA.
AC A0A553ICZ9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=FHL15_001292 {ECO:0000313|EMBL:TRX98082.1};
OS Xylaria flabelliformis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=2512241 {ECO:0000313|EMBL:TRX98082.1, ECO:0000313|Proteomes:UP000319160};
RN [1] {ECO:0000313|Proteomes:UP000319160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G536 {ECO:0000313|Proteomes:UP000319160};
RA Mead M.E., Raja H.A., Steenwyk J.L., Knowles S.L., Oberlies N.H., Rokas A.;
RT "Draft genome sequence of the griseofulvin-producing fungus Xylaria
RT cubensis strain G536.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:TRX98082.1}.
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DR EMBL; VFLP01000004; TRX98082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553ICZ9; -.
DR STRING; 2512241.A0A553ICZ9; -.
DR Proteomes; UP000319160; Unassembled WGS sequence.
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 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; 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; 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; 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:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000319160};
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..1200
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021766391"
FT DOMAIN 766..1061
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1064..1196
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 60..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..706
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1200 AA; 133408 MW; 9BF2EAD143B1936C CRC64;
MLRRPPGEGR LVAPPRRVLL ALAVLLVPWL QLVNAQQQQQ QQEPQHRSSV QSPHFANIIK
DGASDVDSRD RRGLPRLRQE SPLEGQDEAA PKLATARPKN PIRSRGSSMP ATRQHTNNIP
SFNDASALAT LAPAKPVRAP YSPRQMPSIL AGSGLSSLHS ARSLDNWEVE DYILLATVDG
HLYAADRESG DERWHLQVEQ PVVETIHYRP NASSANDKHR RDRHPLDDYV WAIEPINNGA
VYVWTPSHYG AGLMSTGYTM KELVDEMGHY ATSDPPVVYT GHKKNTLITV DAATGRVLKW
FGQAGSQVDQ SARTCFSPNG RFLENDNQEC SADGTITLSR TEYTVDIHRL DDGRDIATLR
YAEWGPNNFD NDLHKQYHSP PDNRYFTSQH NGRVYAIAHP ASTTSFALEF AVPVARVFDV
ARPVDAPHGS NPELVLLPQP RPPVRDEDSA WVRSHSVFLN QTDSGGWYAM SGQSYPLIVD
GPSAQISRRS SWESEAPLDS AQLPAALIGV HTLGDGIGVP DWSSDTPPGL PSESFSDSNQ
LEDHVQGDPV PTTVPDFDTE LPQIVETVIT LPRYALDWFQ DLFKNPLVLC ILVYVSYRYV
KQARRPSFSD YLKTPTFVQP TDPNNEPRIH VTEELSPLAP NTDEPEAVLP ASEKAAVVQE
AQPALASPDA EANSGQEEQP LEQESPDKKK KAHRGRRGGV KHRKGAKKQR DALDDSPVNG
GPESDGSIPG LQNIGVPPKL EPNITTTMND PEDVSGPIIN IGGIEVNQDN QLGMGSNGTV
VFAGKFHGRD VAVKRMLTQF WDIATQETQL LLESDHHPNV IRYYAMSKND SFLYIALELC
QASLSDVVDR HQLFPDLAQA GNMDLPRVLL QIANGLSFLH DLRIVHRDLK PQNILVTMDR
DGRPRLLVSD FGLCKKLEGG QSSFGATTAH AAGTSGWRAP ELLLDDDARE NTGMSMSSIH
SDSSSQLVSA DVMPNRRATR AIDIFSLGLV FFYVLTKGYH PFDLGDRYMR EVNIRKGQFS
LKPLEVLGDV AYEAKALIET MLRADPKARP TAKDVMAHPF FWSAKERLAF LCDVSDHFEL
EPRDPMSPAL AELEACAPLV CRGDFLKILP KEFVESLGKQ RKYTGSRLLD LLRALRNKRS
HYGDLSDSLK KMVGPIPDGY LGFWTRRFPN LLIVCCMVIY KLNLEQLDTF QEYFKPRRPL
//
