ID A0A0F4YPK1_TALEM Unreviewed; 1651 AA.
AC A0A0F4YPK1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=T310_5799 {ECO:0000313|EMBL:KKA20187.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20187.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA20187.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20187.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA20187.1}.
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DR EMBL; LASV01000282; KKA20187.1; -; Genomic_DNA.
DR RefSeq; XP_013326799.1; XM_013471345.1.
DR STRING; 1408163.A0A0F4YPK1; -.
DR GeneID; 25318139; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053958; 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; SM00184; RING; 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:UP000053958};
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 1599..1645
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1651 AA; 184080 MW; 9170B06036CB2AE0 CRC64;
MSKKFKSQAS SSRAAAGGFG AFGGSFGGFS SISSSHSHAP SSLSYVAEPP DLSKISEPQL
VVAFKNLLKK DDITKTKALE DIRDYILKLE DRSDSLEDGV LEAWTRVYPR TSIENSRRVR
QLTHTIQGLL ASLAGKRIVR HLSKVVGAWL AGLYDNDRPV SRSVVESLTR VFATEEKRSN
LWKVYQGPIL EFVDDVILHQ TALTLSDERV VKPDDAEAKF ARVSATAILL FNRILSTASP
QELDKDSPLI HTLLSSKSLW AFAHHEDPFV RRAIYNLLRS SLAKGFDAID WKIISGAFIG
KSLSTPQLGS ASEFSETLLQ LTQARPQIWT TDYAGKSPAV KRLNQYIQRG SQGAAESYWP
NLVQLLQAVP LEVLAKFGTK GDEEVQFGYS QASSLMDAFL DGLSSRDEPR HNLKTGWRSY
IDTGIWLATL LDEGDKVKFV QGQITPIFEQ YISGTQGESR WTLPPQSAEE ICAGGFVRLA
EHGHEVTLRS LWTHVTEDLL KAVKISSPEQ SKDFKPSQDA VCAKANRFFS LEAAVLALAS
QSTTGSRILS TFQEASLPLL EGSLQSLHTR NGKPYGAAAM IEEAIRNVPE IVKSSQPLVS
SLKEKIPALL FTPSADRIMS IILLCRRWDG FDSVFQESLE RMTETELDES NMPALQKLLS
MIDLKEIQDR PRLDSIVMRS LDKALRGKRN EWPLLYAVVE NNTLPDSLLD RIVLSIVDAL
SSEDNVTEAL FGLSQIATRS PATLRRFRKE VHGSKLLARL LYLTESPDDE IAQGAEALEK
KLKDTVSGDV GAESNIDILK HSFREVGPES LSVDSLVNIA EELFRTAKPE EQHELAKNIL
PSRQSWKDSL EPFLGLPPRP STAITSPLGG IVYLIDHNLS DSFWQKLEGV SRDSDRCSSA
FRLASYVAKV LSLPNVMESL GAEERETLFY YFPLAIQLID DDLSIEGCTG ITGLEDSEDR
EEYMEIVNRG RSIISSWIHS DARLNSEDRN SISEALFNFW ERSLESLEDT SPESYRVGEA
FAKIMSEAET RKSTKSMDSW VELLKEIRKI NVVRAAATLL VWRHSIMSNP AGTRLCNELV
ADVTGINPQK DPIEGLQKLS LLNILIQGEE NVVESIPTQR LVFLVKHLIQ CLQSGVESIN
IKAETFKVLT VVLRLLSEIY GSHWADTIEI LNTTWKETSG GDEALPALHG SFRLFASLKS
MANGEGNDDL EDAWAESKAE LIKNLVSTLH KLGMLTAPLK VWRWSGRLTV SIADFSSSFH
QPRDMTVDLL RRQLSTVPVD SLPGVSDLFP LLAAKSRGIQ RAAYEVLHRF IPPAQQQVSF
DVALSKTTVN LPDELLSLLL EAPTMESLIA SSGDDKVWIG VRSYLLSWKI VFDHFPNASL
PVQESYLSNI KEHGSLNPLL DFIFDFLQKS HGKLLDASKF NIRSFEPDES ESAEKETQWL
LVHLYFLSLK YLANLTKTWW IDSKKRIKGP VESWTEKYIS PLVIEDALTS VSEWITTQDP
DEERQLSVKV SVKAAELVAS IPVDEESPPV AMAVNLPPAY PLQPALVTGR SRVLVDEKKW
RSWMLTIQGV IMFSNGNLVD GLLAFRKNVQ GALKGQSECA ICYSVISTDM QTPNKRCATC
KNTFHSVCLF RWFKSSNQST CPLCRNNFVY V
//
