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Database: UniProt
Entry: F6H9X8_VITVI
LinkDB: F6H9X8_VITVI
Original site: F6H9X8_VITVI 
ID   F6H9X8_VITVI            Unreviewed;       104 AA.
AC   F6H9X8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Ubiquitin-activating enzyme SCCH domain-containing protein {ECO:0000259|Pfam:PF10585};
GN   OrderedLocusNames=VIT_19s0085g00070 {ECO:0000313|EMBL:CCB49022.1};
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:CCB49022.1, 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673}.
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DR   EMBL; FN595503; CCB49022.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6H9X8; -.
DR   STRING; 29760.F6H9X8; -.
DR   PaxDb; 29760-VIT_19s0085g00070-t01; -.
DR   EnsemblPlants; Vitvi19g02328_t001; Vitvi19g02328_P001; Vitvi19g02328.
DR   Gramene; Vitvi19g02328_t001; Vitvi19g02328_P001; Vitvi19g02328.
DR   eggNOG; KOG2012; Eukaryota.
DR   HOGENOM; CLU_2255117_0_0_1; -.
DR   InParanoid; F6H9X8; -.
DR   Proteomes; UP000009183; Chromosome 19.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          8..57
FT                   /note="Ubiquitin-activating enzyme SCCH"
FT                   /evidence="ECO:0000259|Pfam:PF10585"
SQ   SEQUENCE   104 AA;  11539 MW;  7111A350BFE0EBD1 CRC64;
     MCTVHSFPQN IDHCLTWAQS EFEGLLEKTP TKANTFLSNP TKYASSMTNV KFRQHSSTSS
     DNFHSTNDLK VACFDFLTSF PVTTMHAPLL ALSSSSFKPS SSQL
//
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