ID F8NHN7_SERL9 Unreviewed; 1767 AA.
AC F8NHN7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=SERLADRAFT_445033 {ECO:0000313|EMBL:EGO29205.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO29205.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO29205.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) 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; GL945429; EGO29205.1; -; Genomic_DNA.
DR RefSeq; XP_007313447.1; XM_007313385.1.
DR GeneID; 18816155; -.
DR KEGG; sla:SERLADRAFT_445033; -.
DR HOGENOM; CLU_000945_0_0_1; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008064; 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; 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; 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}; 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 1716..1763
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 255..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1767 AA; 196326 MW; B13DE1B0854DDA4E CRC64;
MVKGQKSSAS SGTRKKNARK AAGGPQTPEP IPKEKKPKAK GKGQKKEPKK KVYIPPVKPA
PIQPDPLDTM GLVHQLPPEL VVALRALGKK DPVTKAKAIE ELQSKWVDEL KREGDDSPLS
FVLVTMLPVW LHRVPVLFTH PARRIRLLAA SLHASLLRIQ PVREATVGFI QESATIEHVE
SLLGTWCMSS YDIDRQVASF GQKSWSYTFS SQRENDRVVI DMDKLQTITS FIQKALLDPN
GIYLYLNPVP PVAAPPAKKP GSRPMPASKS DNVEHNRSRA EGEEESEMDR NARLRVSAFG
AFRWMLDSRA AISADSLGEL TEFLCNPALW SSLCPAQHCP YVDMESFGFG QPLVRQNAWV
LLSLLMQRWK GSLEHMLPIL STAVLRSAWI DTDVTVRNTM SRPLLLFLKE FPKSWVLDSA
FNSPKHDADS DSEDSDTEEE KEADPVLPRG VGNSGSSLAY NEFLQFLELG CSGSPTEGYP
IVIIILSTIP SSILSASRSS PLGDFFSSFW AALDGRALSS TERKAPSTAF LSSLLESMVF
LLRRVLGGSQ GHTVLLSSTG PQESSIQPTE AAKSVIKEQF VRLWDELAAQ RLRVGEADAG
KLMAQTLVTL NNMDSGLFNE AWEAIVGGVN DKYSVSVSLI SSILKVFADQ FVEETAPAIA
TLKLIGKVVE MSVSQCEKAL DSEDAELSTH ISSLIILIDT FGISLFQRHE FSLRMDDMII
CHALKVLQTS YKLILAYLSY RDDPERCSEL WHSILYGLSG NPHVILSSLP PLLDASRKGI
LAEYLQPEED ELDGVVERIF TQVLDGATQS REVTLIRQLL HTPEHFLSKN GFHNLSQTLV
HSFTSRLVQA LSDPLPELSL HLELIAGVLD THPSVISPDT ILPSVFLAAY LFPISFKQDV
SSTATARTIW TSWVTHAPEN QRSTISNLIK EKLRDLLTEC SMQPKPEHII QLVTEGCPGI
QFDVLADVFP SSEELDSMLS DLPSEPAEPS LALFESLIPP AMEFEDGRLS GATYDRKGYS
PYVRVVSTLL HVLIDSRQLS RDNLWALRHI LALSDFVNDF LRVPSVPSGL LHSTALTSEL
TVMITKAHQL TTYLLTSLTE DALHTKVITA LSDRSKTVDG LPKLIVDLVN HAAAEDTIRD
SRILSSVLQH IFANATKGDA DSWMVLARKF EKTAPQTSLS IMSSITRFAP EPSRLDRYRN
ELAANMLGIS GNKVSTEGLL TLRKLVAVAP DPDSEVVFLP QQRAVNVMKA CQEWITSDEE
VNEEVESMMT LLFYHLAPIL QNVPGSHWEL VFDVIENNLE HCSISDNTTL VTLGRSLQLI
IIIQDLVTTN KALRAEWEER QLSILTLVKN IVTSRLDDAG ISAARSLCRE LALSVIQDDP
KSLVDTNTLA EMCHLLSDPS TVVQKTAYTL LHEAARKKTE YYVIEAAVDT EDAVTAELPM
ELLVLLQRTL QLGDDFTQEN PDDSPESLHT HHQEILGYLL SWMVAFDLFI DASMKVRSSY
FNHMRSLDII STHFIPNIFD ILDIFGGNKK AFKLDVWTTD EYYLDMYEPD SALSARLLAA
HLYYRALVTV PALIRSWVSD CTDKQLLARV IAYTSSYFSP VIIKAELAQV RDSEASTELA
ATENLAVKVA PAASEVTASY TVDEHALELT LRMPSDWPLH RMEIRDTKPV GVSEDRWRGW
VLGVQQIVWQ QNGRVVDGLT LFTKNVTLHF AGQVECAICY SIISMMDGGL PQKPCKTCKN
RFHAGCLYKW FKSSHSSSCP LCRSDIL
//
