ID D7SLV1_VITVI Unreviewed; 878 AA.
AC D7SLV1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN OrderedLocusNames=VIT_15s0021g02140 {ECO:0000313|EMBL:CBI16629.3};
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:CBI16629.3, 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|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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DR EMBL; FN594952; CBI16629.3; -; Genomic_DNA.
DR RefSeq; XP_010661359.1; XM_010663057.2.
DR AlphaFoldDB; D7SLV1; -.
DR STRING; 29760.D7SLV1; -.
DR PaxDb; 29760-VIT_15s0021g02140-t01; -.
DR EnsemblPlants; Vitvi15g00606_t001; Vitvi15g00606_P001; Vitvi15g00606.
DR GeneID; 100241021; -.
DR Gramene; Vitvi15g00606_t001; Vitvi15g00606_P001; Vitvi15g00606.
DR KEGG; vvi:100241021; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_002640_1_0_1; -.
DR InParanoid; D7SLV1; -.
DR OMA; THIEIMT; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009183; Chromosome 15.
DR ExpressionAtlas; D7SLV1; baseline and differential.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 826..865
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 COILED 47..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 242..272
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 416..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 481..529
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 769..803
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 100232 MW; 5511C64ED5CE5B9C CRC64;
MGSTGEPDRK RRHFSSLSPT AATAKKMPFL PVSEDKKLDT AVLQYQNQKL KQKLEAQKVE
CSALENKFSQ LKETQQSYNT TLTLVNKTWR ELVDNLETCS VHLKDSASAG RHVKLPSTTE
DGNSCLQDAF LSRLIETGAT ESCSANDFSD RMEEDRPTSC GKTKNSLSNI VSTINDLWCL
KDGLYAAVLE ALPEDGLCNK KISSDLHAEV NNMRLAFGDL HLKHKSVTRD MQSHRDIDAK
NKAELKRLRG ELESTVAELE ESNCKLVTLK AERDAAKGAF FPILSLGSKN VAGDKARDKQ
KDLHDMEATL KELLDQSSSR LLELKALYEE RIGILKQLSN LQNTLKNVKC ISSSSAYVLV
TDQLEKSKAE VVHYQALFEK LQVEKDNLVW REKEVNMKND FVDVFRRSSV VTDSRLSELR
IEIQNQINER NLIEIKLEEA SREPGRKEII AEFKALLSSF PDNMGTMQNQ LRKYKEAASD
VHSLRADVQS LSSVLERKEK ELETLSTRSA DQVADIRKLQ ALIQDLEESD IQLKLILEMY
RCESVDSRDV LEARDKEYKA WAHVQSLKSS LNEHSLELRV KTAIEAEALS QQRLAAAEAV
IVDLRQKLEA SKRDMFRLSD VLKSKHEENE AYLSEIETIG QAYDDMQTQN QHLLQQITER
DDYNIKLVLE GVRSRQLQDS LLMEKQTMER GFQRATTSLG FFDMKAGRIE DQLKMCSDQV
QKLAEDRLQS LGTLANFQKR LLDVTRLSQQ ARESLEESQS KVDKSRVSLG ELQIELEKER
FEKKRTEEEL EVVRRKASRL RAQTEGSSIV DKLRQELREY RDILKCGICH ERPKEVVITK
CYHLFCNPCV QRIIEARNRK CPVCSASFGP NDVKPVYI
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