ID D7LEK0_ARALL Unreviewed; 659 AA.
AC D7LEK0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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_483804 {ECO:0000313|EMBL:EFH58329.1};
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000256|ARBA:ARBA00024209}.
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DR EMBL; GL348716; EFH58329.1; -; Genomic_DNA.
DR RefSeq; XP_002882070.1; XM_002882024.1.
DR AlphaFoldDB; D7LEK0; -.
DR STRING; 81972.D7LEK0; -.
DR EnsemblPlants; fgenesh2_kg.4__2864__AT2G46495.1; fgenesh2_kg.4__2864__AT2G46495.1; fgenesh2_kg.4__2864__AT2G46495.1.
DR Gramene; fgenesh2_kg.4__2864__AT2G46495.1; fgenesh2_kg.4__2864__AT2G46495.1; fgenesh2_kg.4__2864__AT2G46495.1.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_414687_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046948; ATL20-22-like.
DR InterPro; IPR025287; WAK_GUB.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46279:SF14; RING-H2 FINGER PROTEIN ATL20-RELATED; 1.
DR PANTHER; PTHR46279; RING/U-BOX SUPERFAMILY PROTEIN; 1.
DR Pfam; PF13947; GUB_WAK_bind; 2.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..659
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003102624"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 613..655
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 659 AA; 73817 MW; 7E2233699F8621D7 CRC64;
MTFSKQLFLY LFFLFPLLHA SHTNQCSSSS CGLDDVHVRF PFWLLSKQQE FCGHAGFNLQ
CTSSLTTALK LPNFGTFLVR EIDYISQQIR LHDPESCLAR KLLTFDISGS PFSALYLASY
TFLSCPNEVA KSSRFDSIPC LGNSTTSFLA TTSLDLAKSM LPSCQIVKTS TIPVSRRVTA
GKSRFSTDVN DKDLWLKWDS PSCSNCERDY LRCGFISNTS LQVKCFPFEK SGNNNTRLQV
LKIMILSIIG PVMIFATCIA IGVCTSERFA SRIQRNVAIA ALQPNEVIIT TGLDESTIES
YKKMELGESR RLPGTNDIVC PICLSEYVSK ETVRPLRCGP LDVPIRFPFC DHAQFNLHCT
DLNKTVLELP MSGTFLVHDI DYRRQKIYIN DPENCLAKRL LTFNISGSPF SPRFEIFYTF
LTCPNEVVLP SWYPSIPCLS NSTSSFFATS NFALAQSMLP SCQIVKRLHV PSNSPFGETR
FSSYLNNQNL LLEWDSPDCR GCEVDYLRCG FKNKASLEIK CFDAKKSGHL SSGVLVLVIS
LSAVTVFVFP TCIAIRLYNS ESFDSLAIAA ATVMQQPREV MTTRGLDQST IETFKKMELG
ESRRISGTNG IVCPICLSEY ASKETVRFIP ECDHCFHVKC IDVWLKIHGS CPLCRNSRA
//