ID I1RP25_GIBZE Unreviewed; 1243 AA.
AC I1RP25; A0A098E045;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=FG05775.1 {ECO:0000313|EnsemblFungi:CEF86977};
GN ORFNames=FGRAMPH1_01T18735 {ECO:0000313|EMBL:CEF86977.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF86977.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF86977, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF86977};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF86977, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF86977};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:CEF86977.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF86977.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4] {ECO:0000313|EnsemblFungi:CEF86977}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF86977};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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; HG970334; CEF86977.1; -; Genomic_DNA.
DR RefSeq; XP_011324364.1; XM_011326062.1.
DR AlphaFoldDB; I1RP25; -.
DR STRING; 229533.I1RP25; -.
DR EnsemblFungi; CEF86977; CEF86977; FGRRES_05775.
DR GeneID; 23552938; -.
DR KEGG; fgr:FGSG_05775; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G18735; -.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_004875_2_0_1; -.
DR InParanoid; I1RP25; -.
DR OrthoDB; 1630at2759; -.
DR PHI-base; PHI:1225; -.
DR Proteomes; UP000070720; Chromosome 3.
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; 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; IPR018391; PQQ_beta_propeller_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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000070720};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1243
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010124418"
FT TRANSMEM 1204..1226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 813..1106
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1109..1240
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 73..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 841
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1243 AA; 139139 MW; 17B69EB4ACB55C8B CRC64;
MLRRPPGEGR RPQQKKLFAL VAVVILLPWL QLVDAQQQHR QVSELQRPAG SHPSDDTVQW
AVTSIDAAKA RETVNQVKRP FTASQPRQKE DTRKNRKRDN QRIPDDASAL ATLAPDSRSV
GAPNPSYLRS SSAFASGLAS PQIARNLKDW EVEDFVLLAT VDGDLYANDR RTGKTLWHLE
VDQPMIETKH YRSEESTLDE NYRAVDHYVW AVEPNRDGGI YMWAPDSNHG FIKTGFTMKK
LVEELAPYAD DNSPVVYTGD KKTTMITLDA ASGRVLKWFG SGGSHVNEAE SCSRPDTLYD
AGNLECSSTG TITLGRTEYT VGIQRRDDGL PIATLKYSEW SPNNYDSDLF QQHHSSLDKK
YITSQHDGKV YAFDYTRSEK VPVFSEHFAA PVARVFDVCR PGDATSESNP DLVVLPQPPM
PAEDETEDRM RSNSIFLNQT RAGGWYVMSG QLYPLIAHAP VAQMSRSDWW DIAPPWDTLN
QTKLSKVLVG THYLGNADKR GSFHAPSLPA GSIEVPEVHD VYDDHDEFQH DSQPHTEVGF
ANEPTLLDKF RSIPDSAAKS IKDFITNPVV IIIFVSVLYY NQKNIRRHLK RGKRRGFWRE
LQDILAITET DSVNENFVDD AQSTGTDIDA DSTPEPISEE VKPEILGKQL EESTKEPPVP
APESSKLEPD AFPHTPVKEV ELSDREATPK PKKPVAEGNV ETPVKIANDL QSTLQNQSQN
KNTPANANQN GAPPEKKKKA HRGRRGGVKH RKGRAQEGSQ SRGDDPASAT VEDAVNNAKK
LGERPSLEPD VMTVHDDMQS VTGSTIRMGN IEVNTDEQLG TGSNGTLVFA GKFDGRAVAV
KRMLIQFYDI ASQETRLLRE SDDHPNVIRY YSQQIRDGFL YIALERCAAS LADVIERPHY
FRDLANAGRH DLPNVLYQIT NGISHLHELR IVHRDLKPQN ILVNKGKDGK PRLLVSDFGL
CKKLEGGQSS FGATTGRAAG TSGWRAPELL LDDDAREGAM MELSTQSGSG SVLADDNTTP
RRATRAIDIF SLGLVFFYVL TNGSHPFDCG DRYMREVNIR KGQYNLDLLD SLGDFSREAS
DLISSMLEAD PKCRPTAKEV MAHPFFWSAR KRLSFLCDVS DHFEKEPRDP PSSALAELES
HASDVTGDFL KALPRDFVDS LGKQRKYNGA RLLDLLRALR NKKNHYEDMP EALKRNVGAL
PDGYLAFWTV RFPSLLLICW NVVWAIRWDK TDRFREYYEP AAL
//
