ID A0A1U8BGC9_NELNU Unreviewed; 571 AA.
AC A0A1U8BGC9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC104613187 {ECO:0000313|RefSeq:XP_010279213.1};
GN ORFNames=HUJ06_022564 {ECO:0000313|EMBL:DAD21101.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010279213.1};
RN [1] {ECO:0000313|EMBL:DAD21101.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD21101.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010279213.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; DUZY01000001; DAD21101.1; -; Genomic_DNA.
DR RefSeq; XP_010279213.1; XM_010280911.2.
DR GeneID; 104613187; -.
DR KEGG; nnu:104613187; -.
DR eggNOG; KOG0800; Eukaryota.
DR OrthoDB; 988298at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045191; MBR1/2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22937; E3 UBIQUITIN-PROTEIN LIGASE RNF165; 1.
DR PANTHER; PTHR22937:SF122; RING ZINC FINGER PROTEIN_ 69105-67310-RELATED; 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 519..560
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 151..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 63487 MW; 59637DED61542CC2 CRC64;
MGQRNMLCTS QMLDLEMDQQ GQGHVPPEPC ILVGNISDFA HPNIHPVLSA SGNTSNLDPH
HLPDHHDNSI FYGTQYNSHH FHNPVANLDF GGSATSNFYN PYMIPSSSNR MFPVRLNHGS
ADQLPSSSNH GINGVGLDEY ERTSHFMIGA RGSSKRKNAE GIPRSNQHIN GSTSSSSSSS
GVPMNLGLHQ WDEQYRLIAG TLDVGSFAPP EYRGNGIVSV TEGGVRRSVR SRSSPSGLQM
ESILAHNHGH LLQGNYMVQP FHPVNNPWVE QQFESNGGDR GTSSWNCAPA LPYLHGRSVN
GGSLEIGNTM GQGYQEVTNN SNSTILFYPP PMNHQHSQQY HDTHHHHHQL PPAMQGMQGQ
NYGYQHQLPT LPFVHPLNST LLQSSLNPSH NDVVPGPRSQ RPFLPTGFRI YRPNRREVPQ
AAPEEGNRPR FRIVSDNDVA ILEFQGLGDF IDHHSDMRLD IDHMSYEELL ALEERIGNVN
TGLTEEIITR QLKTRTHASS PVYLNLDEPP STDQETETCI ICQVNYENQE KIGTLSCDHE
YHADCIRKWL LVKNVCPICK TTALAVDSKD G
//
