ID A0A1S3YFH3_TOBAC Unreviewed; 1040 AA.
AC A0A1S3YFH3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC107775543 {ECO:0000313|RefSeq:XP_016450777.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016450777.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016450777.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR RefSeq; XP_016450777.1; XM_016595291.1.
DR AlphaFoldDB; A0A1S3YFH3; -.
DR SMR; A0A1S3YFH3; -.
DR STRING; 4097.A0A1S3YFH3; -.
DR PaxDb; 4097-A0A1S3YFH3; -.
DR GeneID; 107775543; -.
DR KEGG; nta:107775543; -.
DR OMA; WFADESN; -.
DR OrthoDB; 10009520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR FunFam; 1.20.120.1750:FF:000005; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 2.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 131..339
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 135..181
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 986..1015
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1013..1040
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 112291 MW; 52AF1D8147A3738F CRC64;
MESDDDMYGG SDVDSATGDD LYGNDVITGN ESDVDSVGGD DDFIGNDSDH LCTGKNFVVL
SDDDIRHLMD DDISKVSSVL SVSKTEASIL LRRYNWSVNK VHEEWFADES KVREAIGLKI
AEKIVQFPDD KLLACGICFE DYSSDGILAS ACGHPFCVEC WRGYISNSIS DGSGCLNLRC
PEPSCKVAVS QDMIDSLTCD DDRKKYYGFL FRSYVEENRK IKWCPAPGCD FAIEFDIGSD
NCDVMCDCSH SFCWNCTEEA HRPVDCETVG KWKEKNLAES ENTNWILAYT KPCPKCKRPI
EKNEGCMRMT CRDPCKYQFC WLCLNSWSTH GYNPCNKYKP GNEDEKKKEM AKQSIVKYTH
YYERWATNEK SRQKAVTDLR RMGEVNVKEL SELQSIPETQ LKFIIEAWNQ IVECRRVLKW
TYAYGFYLPD EEHTKRQFFE FSQGQAEAGL ERLHHCAESE LENYLNVEES NSKTFDDFRI
KLTGLTSVTK NYFDNLVRAL ENGLEDVHSQ GAHGDMPTSS INAAESSKRT SLKNGRDRMP
LKARAEFMRL VRTRNAGLPG INNTASSKHA LVAPGGNING SKNLVISGDN TLRTSNNPLV
AGGTNFMGSK DALVAARSYP MSPQFLQLAG LSSTTDSSNL QLDGGSKVMN IGGGSVTNLA
NAHVAGRNNL TVPKNPLEAG GSNFVGSKDA PVAGRSYAMG SKFLQEAGVT STTGSSNLQL
AGGGKVMNIG GGSVTNLTNA HVARSNNLTV SKRPLEAGNS NFMGSKDALA AARSYVMGSQ
HLQQAGVTST TGSSNLQLAG GSKVMNIGRG TVPNLANAHV AGTNNLTVTR NVAWGSKVMN
FGGGGTNLAN AHVAGSNNLT VSKTPNAAWG SKVMNTGGSG TNLTNAHVAG SNNLTVSKTP
HVAGGSNVMN IGGRGANLAN SHVAGTNNLS VSKTPHMAGS SSRIGGGKKR RTSNAGTALI
INLDDDDLGE TTSTAGASLT QNLIDDLEGW ACNSCTFLNA SSATACLMCS EDTSGSWECE
ICTFVNKKHA SACQMCEHRR
//
