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Database: UniProt
Entry: F9FPQ8_FUSOF
LinkDB: F9FPQ8_FUSOF
Original site: F9FPQ8_FUSOF 
ID   F9FPQ8_FUSOF            Unreviewed;       860 AA.
AC   F9FPQ8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=GB1/RHD3-type G domain-containing protein {ECO:0000259|PROSITE:PS51715};
GN   Name=SEY1 {ECO:0000256|HAMAP-Rule:MF_03109};
GN   ORFNames=FOXB_08388 {ECO:0000313|EMBL:EGU81114.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU81114.1};
RN   [1] {ECO:0000313|EMBL:EGU81114.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU81114.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC       Concentrated in punctae along the ER tubules. {ECO:0000256|HAMAP-
CC       Rule:MF_03109}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03109}.
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:EGU81114.1}.
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DR   EMBL; AFQF01002500; EGU81114.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FPQ8; -.
DR   STRING; 660025.F9FPQ8; -.
DR   PaxDb; 5507-FOXG_00790P0; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
DR   CDD; cd01851; GBP; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_03109; Sey1; 1.
DR   InterPro; IPR030386; G_GB1_RHD3_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008803; RHD3/Sey1.
DR   InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR   PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR   PANTHER; PTHR45923:SF2; PROTEIN SEY1; 1.
DR   Pfam; PF05879; RHD3_GTPase; 1.
DR   Pfam; PF20428; Sey1_3HB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03109};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_03109};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_03109}.
FT   TOPO_DOM        1..742
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   TRANSMEM        743..760
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        764..766
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   TRANSMEM        767..785
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        788..860
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT   DOMAIN          47..286
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51715"
FT   REGION          825..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   860 AA;  95931 MW;  B07A281C45F20408 CRC64;
     MNGHFSAVGE APGAGSYEHG VQVIDEDKEF NTHLNEYLNV TDVAASGFNY HLISVFGSQS
     TGKSTLLNNL FGTDFSVMSE TERRQTTKGI WMSKNKRETS AGTKMSDNIL VMDVEGTDGR
     ERGEDQDFER KSALFALATS EVLIVNIWEH QVGLYQGANM GLLKTVFEVN LQLFLKDKQS
     TPRSLLFFVI RDHLGTTPLG NLRTTLIQDL TKIWSSISKP QGLEGSRIED YFDFGFAALP
     HKILQADKFT EEVQKLGSRF TAGHRHGKPG LHGDQELEGG LFLPEYHRRI PADGFSVYAE
     GIWDQIVNNK DLDLPTQQEL LAQFRCDEIS REVLIDFDVV VTPLEEKQSE ASKLGVPTVL
     PDLGLAGNDA RQKCIKAFEV QASRYHKGVY ARKRHELEGK IDTRLKALYQ GQLAAAHKAG
     VTAFGEAVAN KVKAGQKAGG SYEFAEIVAN EKRKTLDIFG VEAQSLLIEG VSWTNFESQL
     KLFEKELDEE SAKLRKEEMR RLATRVERWV RSRLGDAVGL EFNKLGSGRA GGGAPETGEK
     PDSEKDLWDR VWKVFTGIVK EAEVRFAERA KSFDATQEEV EIGTWRLRRK SWNALREKIE
     EEVMEGNILL KLRENFEDKF RYDEAGVPRI WRPSDDIEGI YTKARESTLT LVPLLSRFRL
     SETYGPPDLP GFVGPQPNGV QASDEEDLTP IGGIDEEDGK SLEEEMTVLS EGKRQDLVVR
     FKKTADGVYV EAKRGAIGGV AQVPWYFYGL LLALGWNEIL TVLRNPFLCL LILVIAGGTY
     VAYTLNLLGP MLSMGNAAMT QGVEIAKQQL RDFIANSDTA RQAVGMPARE DSDNISMDTL
     DSRGKKANTT STEKDDIDDI
//
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