ID D7KNK6_ARALL Unreviewed; 381 AA.
AC D7KNK6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
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_472661 {ECO:0000313|EMBL:EFH69573.1};
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; GL348713; EFH69573.1; -; Genomic_DNA.
DR RefSeq; XP_002893314.1; XM_002893268.1.
DR AlphaFoldDB; D7KNK6; -.
DR STRING; 81972.D7KNK6; -.
DR EnsemblPlants; fgenesh2_kg.1__2615__AT1G23980.1; fgenesh2_kg.1__2615__AT1G23980.1; fgenesh2_kg.1__2615__AT1G23980.1.
DR Gramene; fgenesh2_kg.1__2615__AT1G23980.1; fgenesh2_kg.1__2615__AT1G23980.1; fgenesh2_kg.1__2615__AT1G23980.1.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034332_1_0_1; -.
DR OrthoDB; 400239at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45768; E3 UBIQUITIN-PROTEIN LIGASE RNF13-LIKE; 1.
DR PANTHER; PTHR45768:SF54; RING-H2 FINGER PROTEIN ATL47; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW 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 TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..186
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 13..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 41832 MW; EEDBC782F7C965E7 CRC64;
MSERKIHNFQ LQNENLNQQI SPSPSPITVN HQSNDSSSSS SSSGGNNRIS PIVLFIIVLL
SVIFFICSIL HLLVRYYLKK KRSSLSSSPN ESDQNPEFSE SDTYQRQLQQ LFHLHDSGLD
QALIDALPVF LYKEIKGTKE PFDCAVCLCE FSEDDKLRLL PNCSHAFHID CIDTWLLSNS
TCPLCRGTLF SLGHQFEYPD FNFGFFAGDD GGVRVSPVQK PADNEIGKRV FSVRLGKFRS
SNINNNGEVV VGGGGETSGG CVSSSSLDNR RCFSMGSYQY IVAESDLVVA LCPNNEGLKN
VKEGESNNKD VEGKKINMRS KGESFSVSKI WQWSNKRSKF PNNPSETNLV VCGSSSSYAC
SGSGSAVAAG LALNGRRFQG P
//
