ID A0A2J6L1T5_LACSA Unreviewed; 357 AA.
AC A0A2J6L1T5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=LSAT_2X12880 {ECO:0000313|EMBL:PLY81286.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY81286.1};
RN [1] {ECO:0000313|EMBL:PLY81286.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLY81286.1}.
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DR EMBL; NBSK01005314; PLY81286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6L1T5; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_2X12880_mrna; cds-PLY81286.1; gene-LSAT_2X12880.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_2X12880_mrna; cds-PLY81286.1; gene-LSAT_2X12880.
DR OrthoDB; 366944at2759; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF108; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 277..320
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 39782 MW; D5D5F71C8F4924A8 CRC64;
MAETPPPSQS QPSPPPSQPP SPPHPISAAV PNNPHTEYWC YHCEKSVAVE ALPDHPDVIC
FECKLGFVQS ISIPPSHIGD LMDDEIPPLS NEIVQFLRAI ASPEDENDLP LPDSAVDVSV
HVFGGVEESD ENTDNHHEDD ADENRNRGNR DREGSDDENE EDEEDELRQR QRRHHLRLRL
HDHGLSAGRH DRILDWAELL LQLEDQSVTF GQQRLESEDD YIGNPGDYID ATGYDSFLQT
LAESDSNDKR GPPPASKSAV QALQTVEVNA MTSSESCAVC KDGMFNNEQM IVKQLPCGHM
YHGVCIMTWL DSRNTCPICR HELPTDDPEY EEERKQRLMA MASTIDHGCS SSSGSGV
//
