UniProt: A0A0P1BPG6

Database: UniProt
Entry: A0A0P1BPG6_9BASI

LinkDB:  A0A0P1BPG6_9BASI 
Original site:  A0A0P1BPG6_9BASI

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (4)   
   PROSITE (1)   
All databases (16)   

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ID   A0A0P1BPG6_9BASI        Unreviewed;      1624 AA.
AC   A0A0P1BPG6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH17942.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH17942.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; CCYA01000265; CEH17942.1; -; Genomic_DNA.
DR   STRING; 401625.A0A0P1BPG6; -.
DR   OrthoDB; 179130at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000054845; 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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12389:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1.
DR   PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 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   Ligase {ECO:0000313|EMBL:CEH17942.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
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          1572..1621
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..384
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1624 AA;  173008 MW;  A2E4F1BEB9482F54 CRC64;
     MPKTAGKGKS SATPATRKKN ERAALKKQGI DPDTVGKGKG AKGGPQQQRV QKKKKNQKKI
     FVPPPKPPPP PPDPLDDMGL ASLLPAGLVV LLRRASKKDV ITRTRACEAL LSWVRGSDEE
     GITASDDERR EAEVTWLPCW AHLFPRLSIS PTRRLRSLAA SIHAVLLTQG HTRAEMLNTP
     AYVESTLGPL VVLAHDTDRG VARGAKTALE GFVQWTTATA DQRLDAREQL YTLLPHLRLL
     LLSPSPAAAL RETAPAANSS NASGSGTPVP HAPVRFDSGL ARDAKARDDA NVEEDIRATD
     GRLAAGAAGA LAWVVSSHPA PLPMEQFEEL LTSAEMWSLL TPPDIVKLEL PAPPVPAPEA
     VKAKRSKKRP PSPPPPPPLP PIGSETPLAR ARAWSLVSSL VSSGTPALLD AALPVFAPLA
     MPAFWAERDA TDPANVPLRA RAALEPAQPF SGAVRRLAAF SEDLCLVKTI LARSRTSLHA
     LAKQGTSSLA LSRAVRTLAA IGASGAPNGL DNAVRELVLD STGTAANVLC ASTEEASIAP
     LVSLIGSLLH TFPEAHVNAE EGIANALASA ARNVLPQALR DAHVPGAAAA NFYASYLPLV
     QDGNERGEVW TNALESISSP AGLDAEALEA LFSAAETLSA SLLSEENVTS ARLDEQVLTL
     GTAVFNGTEQ PSGSERAVLS RLLDRPLPFV TQATSNALLG LLVQALGSHS TNEESKRHAS
     TLLALLEAWC TTRERLQKLV SDPTLRPASA AVFCLAHLEP SPEYGTAATR LWNALAAEPT
     AGVAAVALLR ERILQPGTSL RALLRAGEAL PPTADGSSLL LSEAELASFF TEACASRPRS
     ELAVLDPLVP YGNADDINSK AATEGKQEYD AAGLSTYARA VAVMIQVLSK AGKGARATPW
     ALPHLILFAI AAEDATSLHA ASPFFFAPGA HTQALAKYAT DAVSVATAMI SGLAGDLDDH
     WHLGTTDALR KPSAATKGLA AALHSLWYRN ESQAARVLSR LLAGILSFSA ATEAAGIAWL
     RLAQGATDSK HSSAAAVLKV VKPLVLSSPV YERVRNELAA RLAGIPPTRV EKEGLPLLRL
     LLAAAPPEDA PVALVPQQRA IFLLQAVQKW YASDEAELGE ESFVRLSQIF SELLPIVDNM
     PGSHLELILD VLEAQLEAGG WTADGLPTTQ AALRLLEQVQ QRAARAQALR EVWNARQAEV
     LSMLRPLFLD QPLESGINVP LSETTALLAR LVRRLPDSAF KQEGDETRLT TLLQAPDGRV
     QLTAYRRLAT FVRSRVSDLV VEAAVDPTHA GKAAALSVQL TQQCSSAPGA GLPIADIGRY
     AEEAMEEPQT TLAFFLSWLA LFEHFEEASL ALKSAFAAQI EQMELLSNGF LPTTFGLMLR
     KDSTGRPWDP RGWALDEVFL DDVDPYAPGT LQLLAGHLFH RALGHLAVGV RNYVMSMRDR
     ALSSSITSLT TRHFSPVLAG AELAHLRSGD ARSTLEGEGL SIKITTANEV VATYTVDEQD
     MQIGVSFPND FPLHGVEVRD IKRVGVSEAR WRSWLLATQQ LLTGKNGLVF DALLLFKRNA
     EAMFAGYEGS ECAICYSIIG GESGSLMLPT KKCATCKKPF HSSCLLRWSL TSGSSTCPMC
     RSIL
//

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