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Database: UniProt
Entry: D7TJ83_VITVI
LinkDB: D7TJ83_VITVI
Original site: D7TJ83_VITVI 
ID   D7TJ83_VITVI            Unreviewed;       567 AA.
AC   D7TJ83;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=signal-recognition-particle GTPase {ECO:0000256|ARBA:ARBA00035672};
DE            EC=3.6.5.4 {ECO:0000256|ARBA:ARBA00035672};
GN   OrderedLocusNames=VIT_08s0007g03160 {ECO:0000313|EMBL:CBI30309.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI30309.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00035589};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00035589};
CC   -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005450}.
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DR   EMBL; FN595991; CBI30309.3; -; Genomic_DNA.
DR   RefSeq; XP_002276439.2; XM_002276403.4.
DR   AlphaFoldDB; D7TJ83; -.
DR   STRING; 29760.D7TJ83; -.
DR   PaxDb; 29760-VIT_08s0007g03160-t01; -.
DR   EnsemblPlants; Vitvi08g01444_t001; Vitvi08g01444_P001; Vitvi08g01444.
DR   GeneID; 100247624; -.
DR   Gramene; Vitvi08g01444_t001; Vitvi08g01444_P001; Vitvi08g01444.
DR   KEGG; vvi:100247624; -.
DR   eggNOG; KOG0780; Eukaryota.
DR   HOGENOM; CLU_009301_6_0_1; -.
DR   InParanoid; D7TJ83; -.
DR   OMA; IDKTMMD; -.
DR   OrthoDB; 892at2759; -.
DR   Proteomes; UP000009183; Chromosome 8.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   CDD; cd18539; SRP_G; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR   Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1.
DR   HAMAP; MF_00306; SRP54; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR   InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR   InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR   InterPro; IPR004780; SRP.
DR   InterPro; IPR022941; SRP54.
DR   InterPro; IPR000897; SRP54_GTPase_dom.
DR   InterPro; IPR042101; SRP54_N_sf.
DR   NCBIfam; TIGR00959; ffh; 1.
DR   PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR   PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1.
DR   Pfam; PF00448; SRP54; 1.
DR   Pfam; PF02881; SRP54_N; 1.
DR   Pfam; PF02978; SRP_SPB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00962; SRP54; 1.
DR   SMART; SM00963; SRP54_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR   PROSITE; PS00300; SRP54; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Signal recognition particle {ECO:0000256|ARBA:ARBA00023135}.
FT   DOMAIN          347..360
FT                   /note="SRP54-type proteins GTP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00300"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   567 AA;  62137 MW;  5E158724BC55DDBC CRC64;
     MEAVPFSTVA SRPFSSTSPS LSTPKSLSRR STNTRCSWTA SKLPLPLSSR NPFTREVWSL
     VKSKSVSVRR QMPGVIRAEM FGQLTSGLEA AWTKLKGEEV LTKENIVEPM RDIRRALLEA
     DVSLPVVRRF VQAVSEQAVG VGLIRGVKPD QQLVKIVHDE LVKLMGGEVS ELVFAKSGPT
     VILLAGLQGV GKTTVCAKLA FYLKKQGKSC MLVAGDVYRP AAIDQLVILG EQVDVPVYTA
     GTEVKPSQIA KQGLEEARKK NIDVVIVDTA GRLQIDKAMM DELKDVKRAI NPTEVLLVVD
     AMTGQEAAAL VTTFNVEIGI TGAILTKLDG DSRGGAALSV KEVSGKPIKL VGRGERMEDL
     EPFYPDRMAG RILGMGDVLS FVEKAQEVMR QEDAEELQKK IMSAKFDFND FLKQTRAVAR
     MGSMTRVLGM IPGMGKVTPA QIREAEKSLK MMEGMIEAMT PEEREKPELL AESPVRRKRV
     AQDSGKTEQQ VSQLVAQLFQ MRVRMKNLMG VMEGGSIPAL SNLEETLKSE QKAPPGTARR
     KRRSESRKQF AEPASSRPSP RGFGSRN
//
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