ID W7MB76_GIBM7 Unreviewed; 1212 AA.
AC W7MB76;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=FVEG_05820 {ECO:0000313|EMBL:EWG44845.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG44845.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG44845.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
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).
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; DS022248; EWG44845.1; -; Genomic_DNA.
DR RefSeq; XP_018751036.1; XM_018894056.1.
DR AlphaFoldDB; W7MB76; -.
DR GeneID; 30063778; -.
DR VEuPathDB; FungiDB:FVEG_05820; -.
DR OrthoDB; 1630at2759; -.
DR Proteomes; UP000009096; Chromosome 2.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EWG44845.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009096};
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};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1212
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004896473"
FT DOMAIN 782..1075
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1078..1209
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 84..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..706
FT /note="Basic and acidic 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 1212 AA; 136631 MW; 9BD7C15B18D3EA74 CRC64;
MLRRPPGEGR RALQQQRLFI AFAIILLPWL QLVDAQQQHR PVEPGLPQLQ RPGGRSQQLA
DDAVHQWAAT PVDVTKSARE TVKNVRRASV ANERQRQQKN EPARKNRKRE YEPEKEHIII
PDDASALATL APAQSVGAPN PSRRSSSIPA SGLASPQIAR SLKDWEVEDF VLLATVDGDL
YANDRRTGKE RWHLEVDHPM VETKHYRSER SILDENYRQV DHYVWAVEPN RDGGIYLWAP
DSNRGFVKTG FTMKKLVEEL APYADESSPV VYTGDKKTTM ITLDAATGRV LKWFGATGSH
VNEAESCARP DTLYDENNQE CSSTGTITLG RTEYTVDIQR RDDGLPIATL RYSEWSPNNY
DSDLFQQHQS SLDKKYITSQ HDGKVYAFDY ARSEKAEPLF SEHFAAPVAR VFDVCRPGDA
TSDSNPDLVV LPQPPMPPQD ETHARMRSNS IFLNQTRTGD WYVMSGRSYP LIIHAPIAQL
SRPDWWDIAP SWDTINQTKL SKVLVGTHFL DTVNNRGGTH TPSLPAGAIE GPEVYDVYDS
HDDFENNDSK TTDLTFSDEP TLFTNVKKVP LIAAQSVKDF ITNPVVIIIF VSLLYFNNKN
IRRHLQRGKR RGFWNELQNI LGFVEAPVYT AQPDEVDSSD TDGNVDYLAD PANEEPKPAA
PRESLEEKVK ESVVPTPESS KLEPETLPHT PIKEIELSDR EATPKPKRKT GKRRGGVKHR
KGRAQETSLS RGDDPTTATV EDAVNNAKKL GERPSLEPDV MTVHDDMQSV TGSTIRMGNI
EVNTDEQLGT GSNGTLVFAG KFDGRAVAVK RMLIQFYDIA SQETRLLRES DDHPNVIRYY
SQQIRDGFLY IALERCAASL ADVVEKPNYF RDLANAGRHD LPNILYQITN GISHLHELRI
VHRDLKPQNI LVNMGKDGKP RMLVSDFGLC KKLEGGQSSF GATTGRAAGT SGWRAPELLL
DDDAREGAMM EASTQSGSGS VLVDDNMMPR RATRAIDIFS LGLVFFYVLT NGSHPFDCGD
RYMREVNIRK GQYNLDLLDS LGDFAYEAKD LIASMLEADP KNRPNAKEIM AHPFFWSPKK
RLAFLCDVSD HFEKEPRDPP SPALVELERH AGEVTHDFLK ALPRDFVDSL GKQRKYTGNR
LLDLLRALRN KKNHYEDMPE ALKKTVGSLP EGYLAFWTVR FPMLLLICWN VVWSVRWDGS
DRFREYYEPA AL
//
