ID V4N885_EUTSA Unreviewed; 377 AA.
AC V4N885;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=EUTSA_v10013842mg {ECO:0000313|EMBL:ESQ41916.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ41916.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ41916.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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. LOG2
CC subfamily. {ECO:0000256|ARBA:ARBA00025721}.
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DR EMBL; KI517464; ESQ41916.1; -; Genomic_DNA.
DR RefSeq; XP_006400463.1; XM_006400400.1.
DR AlphaFoldDB; V4N885; -.
DR STRING; 72664.V4N885; -.
DR EnsemblPlants; ESQ41916; ESQ41916; EUTSA_v10013842mg.
DR GeneID; 18018928; -.
DR Gramene; ESQ41916; ESQ41916; EUTSA_v10013842mg.
DR KEGG; eus:EUTSA_v10013842mg; -.
DR eggNOG; KOG4265; Eukaryota.
DR OMA; EEPNCTM; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045195; LOG2-like_mRING_C3HC5.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996:SF26; E3 UBIQUITIN-PROTEIN LIGASE LUL3-RELATED; 1.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 322..361
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 42271 MW; 184D788C4225C6C0 CRC64;
MGISFSNRRR DNYHRRHHNH LPPPPPPPHY YSDPPSQPPP QPPHNEYSYT QNHLVSTPQL
SLPPPQPSQP PSHPPPNINY GAYGHSYNQN QYYPPQQPPP YYSGYHHNGW NQMMRPVHFG
PPPVNQAPPP YASAKKVRND VNVHKDTVRL EADDLNPGHH LVSFVFDAVF DGSFNIIFFA
KEEPNCTMVP HFPEAFPPTK VPFKKGTAQK FLQPSGTGTD LGFFSLDDLS KPSPEDIYPL
VISAEIVISP SSVSEESLVH KQITQAGLEK TNDGSFKVKV MNQILWIEGV RYELRGELYG
IDNSTTQGSV ASGLEDTGGK ECVICLTEPK DTIVMPCRHL CLCSECAKEL RFQSNKCPIC
RQAIKELLEV EVGITEH
//
