ID V4LVG6_EUTSA Unreviewed; 383 AA.
AC V4LVG6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=EUTSA_v10006034mg {ECO:0000313|EMBL:ESQ43903.1};
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:ESQ43903.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ43903.1, 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. ATL subfamily.
CC {ECO:0000256|ARBA:ARBA00024209}.
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DR EMBL; KI517455; ESQ43903.1; -; Genomic_DNA.
DR RefSeq; XP_006402450.1; XM_006402387.1.
DR AlphaFoldDB; V4LVG6; -.
DR STRING; 72664.V4LVG6; -.
DR EnsemblPlants; ESQ43903; ESQ43903; EUTSA_v10006034mg.
DR GeneID; 18020327; -.
DR Gramene; ESQ43903; ESQ43903; EUTSA_v10006034mg.
DR KEGG; eus:EUTSA_v10006034mg; -.
DR eggNOG; KOG0800; Eukaryota.
DR OMA; LRCTDQG; -.
DR OrthoDB; 535723at2759; -.
DR Proteomes; UP000030689; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046948; ATL20-22-like.
DR InterPro; IPR025287; WAK_GUB.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46279:SF15; RING-H2 FINGER PROTEIN ATL22; 1.
DR PANTHER; PTHR46279; RING/U-BOX SUPERFAMILY PROTEIN; 1.
DR Pfam; PF13947; GUB_WAK_bind; 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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW Signal {ECO:0000256|SAM:SignalP}; 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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..383
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004724065"
FT TRANSMEM 246..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..372
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 383 AA; 42808 MW; 977D6539D26D8B8E CRC64;
MTFSKQIPLL LFLFFFPLRT ASSDPKPCYT SSCRHGEMDG RINVRFPFWL FPKQPESCGQ
TGFNLLCTDH QETTIKLPNS GTFLVRDIDY RLQRIRLNDP KKCLAKRLLT FDASGSPFSP
LHLLNYVFFS CPREEDVNHS LYKPIHCLGN STSSFYATRL ELAASMPPSC RIFKKSLIPV
SEPMAYMAGF AGDLNDQDLW LKWDSPNCSV CEAKANLRCG FINNTTLQVQ CVSSVNSGLH
NTSLQVLQII CFSLIGPVFA LTFCVGLVMC SSQRVSSQIQ HAMISGSVTP QPSDQVITRT
GLDESTIESY KKVELGESRR LPTGSNDVVC SICLSEYATK ETVRCLPECE HCFHTGCIDA
WLKLHSSCPV CRSNPSPSRE MCN
//