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Database: UniProt
Entry: D7LDL8_ARALL
LinkDB: D7LDL8_ARALL
Original site: D7LDL8_ARALL 
ID   D7LDL8_ARALL            Unreviewed;       561 AA.
AC   D7LDL8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=ARALYDRAFT_902186 {ECO:0000313|EMBL:EFH57438.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   EMBL; GL348716; EFH57438.1; -; Genomic_DNA.
DR   RefSeq; XP_002881179.1; XM_002881133.1.
DR   AlphaFoldDB; D7LDL8; -.
DR   STRING; 81972.D7LDL8; -.
DR   EnsemblPlants; scaffold_401687.1; scaffold_401687.1; scaffold_401687.1.
DR   GeneID; 9315399; -.
DR   Gramene; scaffold_401687.1; scaffold_401687.1; scaffold_401687.1.
DR   KEGG; aly:9315399; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_009823_3_1_1; -.
DR   OrthoDB; 3084186at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd22583; Rcat_RBR_ARI7-like; 1.
DR   CDD; cd23141; RING-HC_ARI6-like; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF444; E3 UBIQUITIN-PROTEIN LIGASE ARI7-RELATED; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF21235; ARI1_UBAl; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
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:UP000008694};
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:PRU00175}.
FT   DOMAIN          133..345
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          137..181
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  63796 MW;  0424CD63287769BA CRC64;
     MDSEEDMLDA HDMESGEDDF YSGGTDDCND SDDGEPDYGF VEEDADDSAM IASHRSQKNF
     CVLREEDIRR HQMDDIERVS VVLSITEVEA SILLRHFHWS VGRVHDEWFA DEERVRKTVG
     ILESPVVPPS DDSELTCGIC FDSYPPEKIP SVSCGHPFCT TCWTGYITTT INDGPGCLML
     RCPDPSCLAA VGHDMVDKLA SEEKEKYNRY FLRSYIEDNR KMKWCPAPGC DYAIDFVAGS
     GSYDVSCLCS FSFCWNCTEE AHRPVDCSTV SKWILKNSAE SENMNWILAN SKPCPRCKRP
     IEKNQGCMHM TCTPPCKYEF CWLCLGAWMD HGERTGGFYA CNRYEVAKQE GQYDETERRR
     EMAKNSLERY THYYERWASN QTSRQKAMAD LQQAQTQNLE KLSDKQCTPE SQLKFILEAW
     LQIIECRRVL KWTYAYGYYL PDHEHAKRQF FEYLQGEAES GLERLHQCVE KDLAQFLNAE
     GPSKDFNDFR TKLAGLTSVT KNYFENLVKA LENGLADVDS HAACSSKSTS SKSTACSSKT
     RGKGKGSSRT GGSSRNPDDN L
//
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