ID R4XAZ9_TAPDE Unreviewed; 778 AA.
AC R4XAZ9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Protein sey1 {ECO:0000313|EMBL:CCG82749.1};
GN Name=SEY1 {ECO:0000256|HAMAP-Rule:MF_03109};
GN ORFNames=TAPDE_002890 {ECO:0000313|EMBL:CCG82749.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG82749.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG82749.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(2013).
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:CCG82749.1}.
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DR EMBL; CAHR02000098; CCG82749.1; -; Genomic_DNA.
DR AlphaFoldDB; R4XAZ9; -.
DR STRING; 1097556.R4XAZ9; -.
DR VEuPathDB; FungiDB:TAPDE_002890; -.
DR eggNOG; KOG2203; Eukaryota.
DR Proteomes; UP000013776; 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:UP000013776};
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..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TOPO_DOM 684..686
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 687..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 708..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT DOMAIN 38..269
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000259|PROSITE:PS51715"
FT REGION 747..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ SEQUENCE 778 AA; 88119 MW; 4F55FC6B5C05959D CRC64;
MASSNGARPL DSWQIITGDK EFRDVQDYMQ NCGLAHAGFN YNVVSVFGSQ STGKSTLLNK
LFGTHFATMD TVSRQQTTKG IWIARAIDSN ILVMDVEGTD GRERGDDQDF ERKSALFSIA
TSEVLVVNMW ETQVGLYNGA NMGLLKTVFE VNLQLFQHSQ TKTERSLLLF VIRDHLGTTP
LDNLSATIIA DLQKMWMSLQ KPDGAEQSEI SDYFDFRFVG LPHKVLMEQA FNDSVHNLRQ
NFTQKDGEEA IFNPVYHKRI PADGFSQYAK GVWEAIEANK DLDLPTQQEL LAQFRCDEIA
TVAMATFDSK IEETEKAIQP GVVLPDLGNK MSSALSASLA VFDSDASRYH NTVYTKKRSD
LITSCEARLH TLYRSQLASK RKLCLQDYEK AVMECVRHSK SYDFRSLTEG ETRKALEEFE
SEARECCIEP MTWQYAEDKL LLESELSEIT SKLRLEETKR INDQLYRSLK STYEEIITTE
FNTLDSTLWD RILEKCIDAT LLQSSKDLDQ KLQALGVPVS DRSRSTENFS RRAWRLLRNR
VGEETTESHL LLRLREHFEN LFRFDKDGVP IVWKAGDDVD GKYRTAREKT LELIPIFTRL
QKSDGTPPSI PASTSEDDDF NEDSILRIMS SSRQVDLISR FRRTADAVYV EAKRSTVSSV
ASVPLYFYGL LLVLGWNELM ALLRNPLYFI TIIFAGLVAY AVYTLNLSGP VEQVARAMFG
TVFDIVKIKL RDALEISQES VPELLHSTGT NSTRAAARRS ATEDIALDDL SPEGKKDS
//
