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Database: UniProt
Entry: M7U5Z5_BOTF1
LinkDB: M7U5Z5_BOTF1
Original site: M7U5Z5_BOTF1 
ID   M7U5Z5_BOTF1            Unreviewed;      1620 AA.
AC   M7U5Z5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=BcDW1_9299 {ECO:0000313|EMBL:EMR82023.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR82023.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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}.
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DR   EMBL; KB708057; EMR82023.1; -; Genomic_DNA.
DR   STRING; 1290391.M7U5Z5; -.
DR   HOGENOM; CLU_000471_0_0_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000012045; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039795; LTN1/Rkr1.
DR   InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR   InterPro; IPR001841; Znf_RING.
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; SM00184; RING; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367090}; 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          1567..1613
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   COILED          1177..1204
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1620 AA;  181232 MW;  EEFBDF6C7E406423 CRC64;
     MGKRQFKSQA SSTRASTATG AGFGFGFTTK ATRLSYLTEP SNLSAISDAN VILSFKNLSK
     KDATTKSKAL EDLRTFVQNQ PNEQGGTEEA ILEAWVDAYP RISIDNSRRV RELSHSIQYE
     LLKSARKRME RYIPKVVGSW LAGTYDRDRA VARSAMDGLT SFLDTDAKMN LFWKRCQNEI
     LDYAEEALNE TPNTLSDERS VPTEEANEKY FRVNSASVSL LANLLAKLGD DDMLKYQDRY
     EKVIFGNKKL WTLASCEDAT ARKSTDKLLV LCLEKQTQLV ENNLGTISRA FISEALRSSQ
     LTSALQLLQT LHQLTKQFPQ VWTSAYKAKR STATGDLISF VQKGSQGSSP AYWQTLRALV
     AILPISVLPQ TPDSILEFLE VFRKSINQRE ESRANSSEAW LAYGETSNIC IVNLPSSQQA
     EIVQKSTYPM FAHYLHPSPE TSEWLIRNNT PSSTISAFIS RLGKNSNLQN SLAEEWQKLA
     QEFVTRIQTS MPEQSKDYSS SQDAVMAEGH RWFSLLSDIF KLKDLTVDQN PLLQPSGHII
     DSTLQVIISR NGKPYSAGAV LESALRYSPQ LMEASPSILE TVKSFMETHL PKLLLSPSSS
     YLTSSLDQFR LISGQQDSYK SIWQTAIDAL LSTPRNLQRQ KTITALISSN DISDLVRDDQ
     ALQDLLLETS RDVVEGNNDE WALFEAAVIF NGFSKPTERL LLQNLISVLN ASNPNVNHVF
     QALELLSKRR PEAIRDGDAH VDLITKLLAL TELSDSDLGK RATNLRSVVD NESGATTSSV
     VHILRENLEN ANPQSLTIDT LVQQAEAIIT TLDDSSHHPE LFPNATKWSE ALAPLLDQAP
     NPTLGVMRPF AGAVFLARAQ SGNDGSRPGR DLDGYSVALR MAMYSAHLIR DHPDRLSKDA
     LVEIIYLMCL TVELANDQLD LLENNKLFVL SSEEAIAGVR DFVDRIYQDS WSFIVLHSKA
     WQDGFESGSP LEFSGVVHTL ISKLINTSCG NTSTSFYSAR VLSHLLPKLV EQHGWQVGGE
     DWISSLDILK SSTSNIFGAV AILTGLHETL SSSQLVSNLC NRIISDVAGA NAQSEETLGR
     LVLLNATLSV YDNDDLPVAQ NRLVFAVKQI LSWTPEISDT NYQLSSESCL ALQKLLPAIK
     SVYGSYWEKT LEFCIKIWES MENEDHQDQK LPMMGMALKL FSNLQSLQDA NDDLEDARAQ
     YGETASHCLI KLTKLPRSKS TQPIEFVDNI LSRLVINIPS SHINDISEFY PLVASENRMV
     QSAAFSVLHR AIPAEQAEIS VNVLLEKKDA QLPEELLSLL LDAPSIRNFD DEELAEFPPS
     IRSYLLSWHL VYDAFSTASW KVRKDYCNHL QSENCLGSFL TFLFDVLGHS DGTPLNLEKA
     HFDESYIRTY DTSLADGETN ERNFQWLLIH LYHLCLRHTG DLAKAWFSDC QSKQTRQAVE
     TWTEKYFTPL LISDKLDEID EWATSKEAKE GGEKELEIKT SKGARSIFAS YEIDDTSIQI
     AIRFPSNYPF YNVKVEGINR VAVPEKKWRS WLLIVQGAIT FSNGSLIDGL TTFRRNVEGS
     LKGHTECAIC YSIISSDKKT PDKKCGTCKN TFHGQCLFKW FASSNQSSCP LCRCAFNYGR
//
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