ID Q0WRP6_ARATH Unreviewed; 375 AA.
AC Q0WRP6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN OrderedLocusNames=At5g43420 {ECO:0000313|EMBL:BAF00203.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:BAF00203.1};
RN [1] {ECO:0000313|EMBL:BAF00203.1}
RP NUCLEOTIDE SEQUENCE.
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA Hayashizaki Y., Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AK228255; BAF00203.1; -; mRNA.
DR RefSeq; NP_199155.1; NM_123708.3.
DR AlphaFoldDB; Q0WRP6; -.
DR SMR; Q0WRP6; -.
DR EnsemblPlants; AT5G43420.1; AT5G43420.1; AT5G43420.
DR GeneID; 834362; -.
DR Gramene; AT5G43420.1; AT5G43420.1; AT5G43420.
DR KEGG; ath:AT5G43420; -.
DR TAIR; AT5G43420; -.
DR HOGENOM; CLU_040108_1_0_1; -.
DR OMA; ERSFCEC; -.
DR OrthoDB; 469361at2759; -.
DR PhylomeDB; Q0WRP6; -.
DR ExpressionAtlas; Q0WRP6; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; 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; IPR044600; ATL1/ATL16-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46913; RING-H2 FINGER PROTEIN ATL16; 1.
DR PANTHER; PTHR46913:SF1; RING-H2 FINGER PROTEIN ATL16; 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 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 TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..180
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 42316 MW; 52966E8C2340D691 CRC64;
MDLSNRRNPL RDLSFPPPPP PPIFHRASST GTSFPILAVA VIGILATAFL LVSYYVFVIK
CCLNWHRIDI LGRFSLSRRR RNDQDPLMVY SPELRSRGLD ESVIRAIPIF KFKKRYDQND
GVFTGEGEEE EEKRSQECSV CLSEFQDEEK LRIIPNCSHL FHIDCIDVWL QNNANCPLCR
TRVSCDTSFP PDRVSAPSTS PENLVMLRGE NEYVVIELGS SIGSDRDSPR HGRLLTGQER
SNSGYLLNEN TQNSISPSPK KLDRGGLPRK FRKLHKMTSM GDECIDIRRG KDEQFGSIQP
IRRSISMDSS ADRQLYLAVQ EAIRKNREVL VVGDGGGCSS SSGNVSNSKV KRSFFSFGSS
RRSRSSSKLP LYFEP
//
