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Database: UniProt
Entry: B2VS14_PYRTR
LinkDB: B2VS14_PYRTR
Original site: B2VS14_PYRTR 
ID   B2VS14_PYRTR            Unreviewed;      1607 AA.
AC   B2VS14;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 75.
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=PTRG_00353 {ECO:0000313|EMBL:EDU39791.1};
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU39791.1, ECO:0000313|Proteomes:UP000001471};
RN   [1] {ECO:0000313|Proteomes:UP000001471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(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; DS231615; EDU39791.1; -; Genomic_DNA.
DR   RefSeq; XP_001930686.1; XM_001930651.1.
DR   STRING; 426418.B2VS14; -.
DR   EnsemblFungi; EDU39791; EDU39791; PTRG_00353.
DR   GeneID; 6339514; -.
DR   eggNOG; KOG0803; Eukaryota.
DR   HOGENOM; CLU_000471_0_0_1; -.
DR   InParanoid; B2VS14; -.
DR   OMA; IYGSHWE; -.
DR   OrthoDB; 179130at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001471; 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   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:UP000001471};
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          1555..1601
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   1607 AA;  178226 MW;  5E8998EAC71BEE18 CRC64;
     MSKRSAKAQA SSARATTTPT FGAFGGATQA FGASSSTLSY VSEPPDLTAI SDPNVVVYFR
     NLSKKDSTTK AKALEDIQAY VSALQEPVED GLVEAWIKIY PRTSIDNAKA VRQNAHLVHG
     HIALSAGKRM AKYMPKSVAA WLCGLYDSDR SVVEATQTSL RQVFNSPEKL QSIRKAYQQP
     IMEYCRDAID KESTTTLSDE RIVSKDDAEA KYSRVISACI SLLGSLLANL QSEELSKYET
     DYKSVFCDKK LWNFASYSDA RIRRSTHRLL KTCLAKEHVS IKDNIDIISK AYLAEALKSD
     QTGSVSDYID SLTLLTTKYP SVWTTDYTSK TAVERRLRQF LQKGSQFGPR DFWDRLTELF
     KVIPKEVLPT QETEAAELLR ALHIGIVRKD EPKYNAEAAF SAYLDIAGLL LQPLEGTERT
     KLLQEMVLLI LTQYLQPSLE NSQWSMPANA TNLFSKALRI EGMKVVLEEQ WPLMSKQLID
     NIKTSAPEQS KDYEKSQTGV VQQATRFAIV QDHALQIDNL ATLRPVLIDS CASIVAEALE
     VLKNRNGKPY GAAGTVAAIL KRSPSLISST QAEQDLELFI QQDLHTLVLS PSSSYLIDVL
     YSKSDCAFFK DAWSASLKAV LKETDSPGKT KALESILTSS RIPSAFDLAT SDPELQKYII
     ANVREAVEGE AEWDSFSRML SSPAKVLAPE TTDDILAYMT KSLSISQQAP YSLQGLRQIV
     KSKPSMLREF LARPQGSALL QGLLVASESP SDEVSQAATA VNASIRTLLS SSSDSTQSMY
     DLIQQGIRDA TSTSVSVETL VDLAKQSVKT GGDWTEISKV FPSLEDWNAA LKPFLNAPPR
     SSLAITNPLG GAVYLVKSTQ PLLQAETTPR DSDGNSSAYR MTQYVTRLFK NPELFPIDNV
     PRELRDAYLR NIAVAVQLAD DNLGLAGSNG FWSHYDSYAE ADAMTFMSDA QSFVAQELKS
     LVATWGSNNP DASLMTWADK LLSDIDVDAT SVTYYNARTY SVLLTDAIEI AAWKNAHTSQ
     LQEILKATRK NKNFFQILAL INAFREPLSE AKACERMCNE IVADLTGLDI EKDWPVALHQ
     IVLLNSLLNQ DGILESIAKL PGKLCPARCS LASTRRPCSS SEGRVVPRFN GDWSTILNAL
     AGIWSSTKEL EANESETGSS IPLIHASLKL YAKLRTLTEE EETNDDLLEA WKEMEQPVAD
     GLINLLKHSQ HFPDEFHQPL KMVNDVLARQ ISKVSLKHLD STEELFPLLY VESQPVQQTA
     FDILHKQIPA AQEQISIDAA LEKNTARLPE ELLSLIIEAP KVATLAEANL DRSVPLPLRG
     YLLSWLLVFD HLEHASFKVK NDYVEHIKEG EYLPGLLDFA FDFLGHMHNK PVDVSKLDIT
     TYEPDAEPPK RDLQWLLTHL YFLCLCHVPS LTKTWFKNCK SRALVVALEP WTERYVSPPV
     IVAALEAVNT WSEEQSAAEP DSPFTVKVAS RAREITASYT VDDQTMSMRI SLPAAFPLAN
     AHIEGINRVA VSETKWQSWL RTSLGAITIF NGSLIDALTT FKRNVDGAIK GQTECAICYS
     IVGSDRKLPD KKCGTCKNLF HGVCLFKWFK SSNSPSCPLC RTNFHYA
//
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