ID D7SJW4_VITVI Unreviewed; 1052 AA.
AC D7SJW4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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_06s0004g06750 {ECO:0000313|EMBL:CBI15940.3};
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:CBI15940.3, 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=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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; FN594951; CBI15940.3; -; Genomic_DNA.
DR AlphaFoldDB; D7SJW4; -.
DR PaxDb; 29760-VIT_06s0004g06750-t01; -.
DR EnsemblPlants; Vitvi06g00657_t001; Vitvi06g00657_P001; Vitvi06g00657.
DR Gramene; Vitvi06g00657_t001; Vitvi06g00657_P001; Vitvi06g00657.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_004912_0_1_1; -.
DR InParanoid; D7SJW4; -.
DR OMA; ESVACHI; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009183; Chromosome 6.
DR ExpressionAtlas; D7SJW4; baseline and differential.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45958; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR45958:SF14; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 6.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 241..320
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1015..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 117095 MW; 33E2827EABAF6FA6 CRC64;
MTAPALESIL RSLSELCLSD DNFAWENPRR FSAYANRLQL VLNQFLRSSS PEALSPSVQT
TLRGVSGDLS KAVEAVSVYR NRSKIFVLIN CQSLCASLQE HTVAIGGWLA LLESTLPEGS
DLRKKVADLS QDMKQAQFRV SENEERVHCT LQKEGQGRPT SKAVQSAIVM DLARALGIEA
DDHAKLSEQV KLLKTDLASS NPLAERRVLM SLERIMDNWT VHPATSEWNL DFDFEEDAQM
SPFKNFLCPL TKEVMKDPVV LESSQNYERT AIEYWFRRCI EDGRDPTCPV TGQVLKSTEM
KPNIGLAGAI EEWVSRNIEI QLKSAVQCLS ENQPPVDSVE WVLDVIYKIS EEHPSNRYRV
RHAGVVLLMV KVLRNCSKSM GTHMRGKALM TLLSMAKDEE SKNIMLGEGI TRLAIHSLIG
SSEKEKEYAV KLLLEFSRDE AYCTKIASEK GALVLLSSMA GNLEHPALSN LAEEVLKQME
RVEDNVQHLA AAGRFEPLLS RLCEGTDDVK IEMARIMGRM TLTNSSKEQI ARKCAKTLVQ
LLSKPKGRAP SLQALCNLSV LDDNATILVD SAVIPALTDI LFENMDDSEL KELATSIIAN
IVQHPGHWEY SSIDNKGHSM QSETTVFRLL GLLAHVSPQC QVSVLRILYG ISSSPQASES
VVTHIKSGDG IKTIIPFLEH PEVEHRIYAF RLTRILSGTF GEDLANELKP ADKLPLFKEK
LLDNQSTDGE RSDAACILAN LPLSEDEVKT VLGSSFVGWT VVTLKDRLRS TNWRTTRSSS
CLEEGLLGLL LHFTQSPDPQ TVSVVKEHSL MNIFREQLNF PLKPRVKQLA ALGLKNLSES
RRTLISTGDL EVQLSHGFCS SLVFMCGKRP PELPVCAIHN VSCEEDNQFC LLRSNCIKPL
VDLLTDEDTN VQIAAVEALS TLVIDTSNNF KRAVDELEHL GVVEAAITLF TEVRPGILQE
RLLWMIERIL RVESDINRHS LNQSLVRALV EAFKHGNANA KGYAQDALTN LKQLSGVSGK
NSSQSRPRRG ESSREVAIRT MVMLKKMNGR VR
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