GenomeNet

Database: UniProt
Entry: F4PEH7_BATDJ
LinkDB: F4PEH7_BATDJ
Original site: F4PEH7_BATDJ 
ID   F4PEH7_BATDJ            Unreviewed;       162 AA.
AC   F4PEH7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=E3 ubiquitin-protein ligase listerin {ECO:0000256|ARBA:ARBA00017157, ECO:0000256|RuleBase:RU367090};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU367090};
DE   AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000256|RuleBase:RU367090};
GN   ORFNames=BATDEDRAFT_33847 {ECO:0000313|EMBL:EGF76376.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF76376.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF76376.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase. Component of the ribosome
CC       quality control complex (RQC), a ribosome-associated complex that
CC       mediates ubiquitination and extraction of incompletely synthesized
CC       nascent chains for proteasomal degradation.
CC       {ECO:0000256|RuleBase:RU367090}.
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         ECO:0000256|RuleBase:RU367090};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367090}.
CC   -!- SUBUNIT: Component of the ribosome quality control complex (RQC).
CC       {ECO:0000256|RuleBase:RU367090}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000256|ARBA:ARBA00007997,
CC       ECO:0000256|RuleBase:RU367090}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL882897; EGF76376.1; -; Genomic_DNA.
DR   RefSeq; XP_006682986.1; XM_006682923.1.
DR   AlphaFoldDB; F4PEH7; -.
DR   STRING; 684364.F4PEH7; -.
DR   GeneID; 18240240; -.
DR   HOGENOM; CLU_096579_0_0_1; -.
DR   InParanoid; F4PEH7; -.
DR   OMA; WMLTISA; -.
DR   OrthoDB; 179130at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039795; LTN1/Rkr1.
DR   InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12389:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1.
DR   PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM01197; FANCL_C; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367090};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU367090};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367090};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          112..159
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   162 AA;  17809 MW;  F5B446E73713650D CRC64;
     MELKSAETYD TRDTEALGIR VSMWSCEVTA SYTIEDAVLE LVIQLPSSYP LRLAQVGSGK
     GGGRAAGINE ARWRAWVLSV SAVMASQNGS IIDALTVFNK NISMHFKGIE DCAICYSVVS
     AIDRALPNKQ CKTCKNQFHG SCLYKWFKSS GQNTCPLCRQ PF
//
DBGET integrated database retrieval system