ID B3IX41_LOTJA Unreviewed; 380 AA.
AC B3IX41;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RING-G83 {ECO:0000313|EMBL:BAG50068.1};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305 {ECO:0000313|EMBL:BAG50068.1};
RN [1] {ECO:0000313|EMBL:BAG50068.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18567832; DOI=10.1104/pp.108.118141;
RA Asamizu E., Shimoda Y., Kouchi H., Tabata S., Sato S.;
RT "A positive regulatory role for LjERF1 in the nodulation process is
RT revealed by systematic analysis of nodule-associated transcription factors
RT of Lotus japonicus.";
RL Plant Physiol. 147:2030-2040(2008).
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; AB378641; BAG50068.1; -; mRNA.
DR AlphaFoldDB; B3IX41; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF2; RING FINGER PROTEIN 150 ISOFORM X1; 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 2: Evidence at transcript level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..380
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002789609"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..178
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 205..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 42486 MW; 9B7ADC577E83CA97 CRC64;
MIMQKESPPR RRRFGHIHRH VWLAFLLLLI IQLSMPATAQ TMAPEMEPDS NKSVATIMGI
VALMFLVSGF LSLYSGKCTE RQAGRLTLAH AAAGGSGHRQ LNELSNGLNQ EVIDTFPTFL
YSHVKCLKIG KGTLACAVCL NEFEDDETLR LIPICNHVYH HSCIDLWLAS HSTCPVCRAS
LLPITPDDTA TNLPPPTVSI LMPEDQEEEN SLNEEQERDS ENDNQKSSDH SYTEPLRRCR
TTSHPIRSRS TGFLSSLLSP VDRNRHSVVV QPGEDCERFT LRLPDEVRSQ MLSSTALKRA
KSCVSFTRMS SGTWGYRTRS VGRFGSDHEQ WGCTLTPPNF GWNWNRSVKK SPARCSGVAK
DSEAGERSSD FLCPPQINMI
//
