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
//