ID A5B1G2_VITVI Unreviewed; 428 AA.
AC A5B1G2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=VITISV_028611 {ECO:0000313|EMBL:CAN69574.1};
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:CAN69574.1};
RN [1] {ECO:0000313|EMBL:CAN69574.1}
RP NUCLEOTIDE SEQUENCE.
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT vinifera L.): coping with a highly heterozygous genome.";
RL PLoS ONE 2:e1326-e1326(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; AM443321; CAN69574.1; -; Genomic_DNA.
DR ExpressionAtlas; A5B1G2; baseline and differential.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd16521; RING-HC_MKRN; 1.
DR Gene3D; 6.10.250.3220; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF14608; zf-CCCH_2; 2.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 3.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 64..91
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 174..201
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 243..301
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 330..359
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 64..91
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 174..201
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 330..359
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 93..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48070 MW; 0AD1D03EF55329CF CRC64;
MAIINLWPPK TLRMCEFSPS LNFAESLSKR LGFDFDERVS IYRISVXRCR RGFNASSLHM
EXVLKGTIIC TFYQKGVCSY GGRCRYEHVK VSHSQPSAPS SSTSSHQLLV PDSASLTHPS
RTVTNGLIPA PGVPPEPSAS SRPLFPPTQP AWNQESGDQD FLENNIGEPR TDRPADQSIC
SFAAAGSCPR GEKCPHIHGD LCPTCGKHCL HPFRPEEIEE HLRTCEKKQK HLEALKHSQE
IECSVCLDRV LSKPTAAERK FGLLSECDHP FCISCIRNWR SSSPASGMDI NTALRACPIC
RKLSYFVIPS VIWYSTKEEK QEIVDSYKAK LRSIDCKHFD FGNGTCPFGT SCFYKHAYRD
GRLEEVVLRH LGAEDGHVMI AKNIRMSTTM NYEGNVCYFT LDAEDLNCQC HSPVIFKNCL
VEWNSNKD
//
