UniProt: A0A2H3K6S9

Database: UniProt
Entry: A0A2H3K6S9_WOLCO

LinkDB:  A0A2H3K6S9_WOLCO 
Original site:  A0A2H3K6S9_WOLCO

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (1)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   A0A2H3K6S9_WOLCO        Unreviewed;      1885 AA.
AC   A0A2H3K6S9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=WOLCODRAFT_145160 {ECO:0000313|EMBL:PCH44774.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH44774.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH44774.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH44774.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; KB468168; PCH44774.1; -; Genomic_DNA.
DR   STRING; 742152.A0A2H3K6S9; -.
DR   OMA; QWITSDE; -.
DR   OrthoDB; 179130at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000218811; 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; IPR016024; ARM-type_fold.
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; SSF48371; ARM repeat; 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:UP000218811};
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          1816..1863
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..515
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1885 AA;  207387 MW;  4231F62FB95D19B6 CRC64;
     MAKGKSSASS ATRKKHARKA AAVHGEPAAD PAVPKEKKAK GKDKRSKNEP RKKVYIPPVK
     PAPVRLDPLD TLGLAQTLPP ELTVVLRRLA KKDGVTKRRA LEELVTWIDR AGAEGENETQ
     EVLAEMVPVW LHHLPFLLLH PTRGIRQLAT SLHSSLLTIP HTSARLLSYI LSELEYDQQD
     CILGTWLLAT YDVDRQTAAR ARETWAAHTA FLVPNNTNAS STGSIPRADK LTLDRATLTR
     LWSFLLRALR DPGGLYAALN PTQPSTQPVE LPSSRSQPRK GSPQQKKGAA PTPPRKGPLA
     RMAEEDARRS PSPGAEGGVS PRAEDEEESE GDRRARLRVG ACGAVGWVLG ALAEHGSVGG
     EGEAEKEKEK EKEDALDAAL APLADPLLWT ILHPAQHPPF SPSADGFGHD QPGVRSAAWS
     LLHALLKTCK AVGRIGADAR LLMTLSRVVL RSAWVELDVG VRGVLWVPVL IFLRDFPQCW
     EIEAAPDASR GDAGDAESDE EDEDDEDEGD EEEDRQQSQA AEARGEQGRP VRSTAWREFM
     DFLALGCSGA PVQGYPAVLV VLSTVPDSIL FTPGDQSSSS SIPCEELLVN FWAALDGRAL
     SGLDRKATNK AFLEALCECV VLIVRRLMRP TTDSTRKPGT TSEGDSRTLV SAQVQRIWDE
     LCAKRIRLSG ALAGACLARL VEGMWRADAR LFDAAWTPLA AGVRAVSAAP AQAPAKMEVG
     LFIDVVKTLR QHFDASAAGQ EHSGGSQGTE GDVKGRTPRE AVRELVDEVA EEAIARCESV
     LAGTRGDEVQ GEVVSSVVKV LEGFPDAVFS KAELVQRLDS GLLSNTPRLL ALSSDLLVTY
     LKYNSGNEAS CNTLWQRVLD ALSEHPEHLQ PLLSAAHELP EYLKPQADEG DLSGLVNGFV
     ESMLIGEGKE NIETLKLLLL EPDHFLHKGR AESIVGTLAT AVTDRLHMTM RDASVDLSVF
     DGPLSIFRGY IERGIPRSAS SQGRENVNNF AEQLMPEIFL YAHLLPLCRA VEHFRLTMAQ
     SLWSAWQHGA PEEVRARAMH AVSRRIREVL ADCESIATPD QIVRMLTESY TGDILKDVFP
     TAQEMASMLE TLPSCPADAS IAVLDPLVPL CSPGDEQLLS PDHGPYSSDG FSSYARISYG
     LLLYLLNDRH TAKTNAWTLR HFLALSLYAE ELLVLGTSSN PVFTTSVARS ILEDVKSKVN
     RLSAYLLSSV QPGWHAAVVS TIMADRPDPG LDSVGRLVAE LVRQAQRIDT VRESRILYSI
     LQHALDEATT AEAEQWILLA RKTERTARQM SLAILYAVTQ YAPEPPILDR YRNELAAGMM
     GVPASKANAE GLWLLRRLAA SAPDPESDVI FLPQQRAVNV LKACQQWITA DEDLEEEVDS
     AMTLVFLPLA PILQNVPGGH WDLMFDVLEN NLEDVSLTEP DTLVTLSRTL RLFMATEDLA
     STNKALREMW QQRRLTCLTL IRDLVTAKPE PSQISKPLSV CRELALQALQ DIPDTLLNHS
     MLSKEREQLC HLVMDTSVEV QKSAYSILRE VARKYTEHMV IEAAVDTEVA TRIELPVELI
     KILVRSPDPS LDPESEPLTG YCLAWMLTFD LFSDASFGVK SQFISQLRDL ALVGTHLLPC
     LFSILGLYAG STPFKLGIWE IDQYDLDLYT ADSLCLSLLS AHIYYRALLT VPTLVRSWLS
     DCRDRQLALS VSSYTARNFS PALIHAELVH VRDPEATTEA ADEAFNVRVA SAVNEATASY
     SVDERQLEVT VRFPVDYPLH GIEIRNSTRI GVPEEKWRAW ILGLQQILSY RSGSIVDGFG
     FFKRNIISLF EGLTECAICY SIVSATDGSL PRKPCKTCKN RFHAGCLYTW FSTSHSSNCP
     LCRSEIMLEA GQRRRFAIDR ETRET
//

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