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
//