ID F6H1B8_VITVI Unreviewed; 734 AA.
AC F6H1B8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN OrderedLocusNames=VIT_18s0001g10260 {ECO:0000313|EMBL:CCB45827.1};
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:CCB45827.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR EMBL; FN595227; CCB45827.1; -; Genomic_DNA.
DR RefSeq; XP_002282892.1; XM_002282856.3.
DR AlphaFoldDB; F6H1B8; -.
DR STRING; 29760.F6H1B8; -.
DR PaxDb; 29760-VIT_18s0001g10260-t01; -.
DR EnsemblPlants; Vitvi18g00762_t001; Vitvi18g00762_P001; Vitvi18g00762.
DR GeneID; 100267740; -.
DR Gramene; Vitvi18g00762_t001; Vitvi18g00762_P001; Vitvi18g00762.
DR KEGG; vvi:100267740; -.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_024479_0_0_1; -.
DR InParanoid; F6H1B8; -.
DR OrthoDB; 988298at2759; -.
DR Proteomes; UP000009183; Chromosome 18.
DR ExpressionAtlas; F6H1B8; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF184; OS04G0185500 PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 687..728
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 78554 MW; 00524CA4DA24D82A CRC64;
MQGQKGAIGS LPETLNFDHG STSSGAGLDQ QLCWNNMRNP AENRLADYMQ PPSDTNLAFL
NSISHGGQNL SGWSLGEPSS INTQNIVSCD ECKTEHGWAT SVSGCAGAGP RLEEHRCEPS
NVLSLDNVNV NPSSNQIVNG PLFLQSSSSD AIAQNLNLNA GFVGSGGDDR QGLECPNLYK
SSGSENLPSA SSSSDPFGPR ILSGGYLVEE NDGRAGSSLE GRRLSCKRKA LEGNIGQSSV
GGSSSSFQRT ENNVWHAVVP ARYNAGNGLS ISSPSGNIIG ASPAEQVNPR LGLGVRGVAT
DSLPVLNVPG SAESSHRNFR MRINPSHQQD SVPHNLFSAG GSVRHSNVSS HQQSTRLIPV
NHAPDLRSTP AADNASSQSQ SVVNHAPNLP RTMQSFRWSG ASSSRHGNSS SPLISGERDA
APREESSSRS MPRNTLEHSM FLPAIDLRSL PQNPTNRNLA GGNMTTPGNS ASTSRTGSSS
GVNSSSAPTW GPPRDPPSQY SRRLSEYVRR SLFSSVGADS GGQSSNYSPL HSGPSPSSQE
VAPSSGAGNQ GHHQSYPRSA LLMERHGDGV LGIPYSLRTL AAASEGRSRL VSEIRNVLDL
MRRGEDLRFE DVMILDQSVF FGVADIHDRH RDMRLDVDNM SYEELLALEE RIGDVCTGLS
EETILKQLKQ RKYWSVARGA EVEVEPCCIC QEEYGDGEDI GTLECGHDFH YGCIKQWLMH
KNLCPICKTT ALGI
//
