ID D7KXV0_ARALL Unreviewed; 317 AA.
AC D7KXV0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ARALYDRAFT_338432 {ECO:0000313|EMBL:EFH64460.1};
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 -!- 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};
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DR EMBL; GL348714; EFH64460.1; -; Genomic_DNA.
DR RefSeq; XP_002888201.1; XM_002888155.1.
DR AlphaFoldDB; D7KXV0; -.
DR STRING; 81972.D7KXV0; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_2000531; fgenesh1_pg.C_scaffold_2000531; fgenesh1_pg.C_scaffold_2000531.
DR GeneID; 9324264; -.
DR Gramene; fgenesh1_pg.C_scaffold_2000531; fgenesh1_pg.C_scaffold_2000531; fgenesh1_pg.C_scaffold_2000531.
DR KEGG; aly:9324264; -.
DR eggNOG; KOG1571; Eukaryota.
DR HOGENOM; CLU_050604_2_0_1; -.
DR OrthoDB; 5475152at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009941; C:chloroplast envelope; IEA:EnsemblPlants.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022170; MUL1-like.
DR InterPro; IPR044231; SP1/SPL1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47568; -; 1.
DR PANTHER; PTHR47568:SF2; E3 UBIQUITIN-PROTEIN LIGASE SP1-RELATED; 1.
DR Pfam; PF12483; GIDE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
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 SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..317
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101243"
FT DOMAIN 270..305
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 317 AA; 35478 MW; EFA07E5E49D89417 CRC64;
MIHLAGFTCC LGGIALYLLS RNTGGVVKSI TRVNHLKDLE QLVESKVFPL IIAVSGIVGS
ETPIKCEHSD ILGVFLKKTA EQQVLSRNWR FSWVRKSTLM QPMTKEVPWF LDDGTGRVNV
AVSQGEIGLA LTVGSDVFEK AEPVSLVQGT LDYLKGLKIL GVRRVEHVVP IGTPLTIVGE
AVKDGMGNVR IQKPEQGPFY VSYVPLDQLI SKLGEWSRRF KYASMGLTVV GVILLSKPVI
KYILKKIEDT LERRRRQLLQ KRVVDVPDLC VICHDQKYNT AFVQCGHMCC CLTCSLRLTT
CPLCREQIQQ VLKIYRH
//
