ID A0A135UV01_9PEZI Unreviewed; 847 AA.
AC A0A135UV01;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Sey1 {ECO:0000313|EMBL:KXH64172.1};
GN Name=SEY1 {ECO:0000256|HAMAP-Rule:MF_03109};
GN ORFNames=CSAL01_08190 {ECO:0000313|EMBL:KXH64172.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH64172.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH64172.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH64172.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH64172.1}.
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DR EMBL; JFFI01001005; KXH64172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UV01; -.
DR STRING; 1209931.A0A135UV01; -.
DR OrthoDB; 1606at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
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}; GTP-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03109};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03109};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03109,
KW ECO:0000256|SAM:Phobius}.
FT TOPO_DOM 1..734
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TOPO_DOM 756..758
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 759..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 780..847
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT DOMAIN 47..279
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000259|PROSITE:PS51715"
FT REGION 663..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..847
FT /note="Basic and acidic residues"
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 847 AA; 94996 MW; 41B8A18D7A3852B2 CRC64;
MNGHFAAVGE EPDAQNYEHG IQVIDDQKDF NSHVATYLQK VRVAEAGFNY HLISVFGSQS
TGKSTLLNNL FGTDFSVMSE TMRQQTTKGI WMSKNKKEAG MAENIIVMDV EGTDGRERGE
DQDFERKSAL FALATSEVLI VNLWETQVGL YNGANMGLLK TVFEVNLQLF LKDKQSSLRS
LLFFVIRDHL GTTPLANLRN TLVQDLTKIW SSISKPQGLE NSRIEDYFDF AFAALPHKIL
QADKFTTEIQ NLGRRFTAGH RMSGASTQEF DGGVFLPEYH RRIPADGFSL YAEGIWDQIV
NNKDLDLPTQ QELLAQFRCD EISREVLIGF DNAVVPLEEK QSESARAGKP AVLADLGVTG
RESREKCLKA FEIQASRYHK GVYTRKRQDL EAKIDGRLKT LYNAQLSAAH KAAIASFSEH
VSGAVKAGQK SGAAYEFAEI VTEEKKKTLE FFKTEAESLA IPGIAWSNFK SQYVLFEKEL
DDVSGKLRKE EMRRLATRVE RWVKSRLGDA IGLEFNKLGS GRAGSGAPET GEKPAEKDLW
DRIWTVFVDI VKDAQGRFTD RAKSFEATQD EVEVGLWRLR RKSWVALREK IEEEVMEGNI
LLKLRENFED KFRYDEAGVP RIWRPTDDIE GIYTKAREST LTLIPLLSKF KLSESYGPPE
LPAWIGNQPR GVEPSDEEDL TPIGGVDEED GKSLEEEMTV LSESKRQDLV IRFKKTADGV
YVEAKRSAIG GVAQVPLYFY ALLVALGWNE IVAVLRNPFL FVFLILLAGG TYVAYTLNML
GPMYQMANAA ANQGVEIGKA KLREFIENSD TARNALAMPA RDSDSISMDT LDSRGKKKSA
EDDIDDI
//
