ID W9Z8S7_FUSOX Unreviewed; 1254 AA.
AC W9Z8S7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=FOMG_15638 {ECO:0000313|EMBL:EXK27790.1};
OS Fusarium oxysporum f. sp. melonis 26406.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK27790.1};
RN [1] {ECO:0000313|EMBL:EXK27790.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK27790.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum melonis.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXK27790.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK27790.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT 26406.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH659347; EXK27790.1; -; Genomic_DNA.
DR AlphaFoldDB; W9Z8S7; -.
DR VEuPathDB; FungiDB:FOMG_15638; -.
DR HOGENOM; CLU_004875_2_0_1; -.
DR Proteomes; UP000030703; 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 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:EXK27790.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
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..1254
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004934112"
FT DOMAIN 823..1116
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1119..1251
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 81..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 851
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1254 AA; 140920 MW; B7369B6161545C77 CRC64;
MLRRPPGEGR RASQQQRLFI AFAIILLPWL QLVDAQQQHR PVEPALPQLQ RPGGRSQQLA
DDAAHQWAAT PVDLTKSARE TVKNVKRASV PNQRQRQQQQ KIEPVRRNRK REYENDHLII
PDDASALATL APAQSVGAPN PSRYQRSSSI PASGLASPQI ARSLKDWEVE DFVLLATVDG
DLYANDRRTG KERWHLEVDH PMVETKHHRS EKSILDENYH QVDHYVWAVE PNRDGGIYLW
APDSNRGFVK TGFTMKKLVE ELAPYADESS PVVYTGDKKT TMITLDAATG RVLKWFGATG
SHVNEAESCA RPDTLYDENN QECSSTGTIT LGRTEYTVGI QRREDGLPIA TLRYSEWSPN
NYDSDLFQQH QSSLDKKYIT SQHDGKVYAF DYARSEKAEP LFSEHFAAPV ARVFDVCRPG
DATSDSNPDL VVLPQPPMPP QDETHARMRS NSIFLNQTRT GDWYVMSGRS YPLIIHAPIA
QLSRPDWWDI APSWDTINQT KLSKVLVGTH FLDTVNNRGG THTPSLPAGA IEGPEVYDVY
DGNDDLENND SKTTDLTFSD EPTLFTNVKK VPLIAAQSVK DFITNPVVII IFVSLLYFNN
KNIRRHLQRG KRRGFWNELQ NILGFVETPV YTEQPDEVDS SDTDGNVDYL AGSVNEEPKP
AAPRDNLEEK VKESVVPAPE SSNLEPGTSP QTPIKEVELS DREATPKPKR KTPTKRSGDT
PDTPQPQPQA KATATNESQD GGAPEKKKKA HRGRRGGVKH RKGRAQEASL SRGDDPATAT
VEDAVNNAKK LGERPSLEPD VMTVHDDMQS VTGSTIRMGN IEVNTDEQLG TGSNGTLVFA
GKFDGRAVAV KRMLIQFYDI ASQETRLLRE SDDHPNVIRY YSQQIRDGFL YIALERCAAS
LADVVEKPNY FRDLANAGRH DLPNILYQIT NGISHLHELR IVHRDLKPQN ILVNMGKDGK
PRMLVSDFGL CKKLEGGQSS FGATTGRAAG TSGWRAPELL LDDDAREGAM MEASTQSGSG
SVLVDDNMMP RRATRAIDIF SLGLVFFYVL TNGSHPFDCG DRYMREVNIR KGQYNLDLLD
SLGDFAYEAK DLIASMLEAD PKNRPNAKEI MAHPFFWSPK KRLAFLCDVS DHFEKEPRDP
PSPALAELER HAGDVTRSDF LRVLPRDFVD SLGKQRKYTG SRLLDLLRAL RNKKNHYEDM
PEALKRTVGP LPEGYLAFWT VRFPMLLLTC WNVVWNVQWE KSDRFREYYE PAPL
//
