ID A0A0A2VJV0_BEABA Unreviewed; 1614 AA.
AC A0A0A2VJV0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BBAD15_g8252 {ECO:0000313|EMBL:KGQ06430.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ06430.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ06430.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ06430.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ06430.1}.
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DR EMBL; ANFO01000816; KGQ06430.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2VJV0; -.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_000471_0_0_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030106; 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 SMART; SM00184; RING; 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:UP000030106};
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 1553..1599
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1614 AA; 177592 MW; 0A64617B9FF18086 CRC64;
MKRIQGRSAG GSRAAFGAGF GGFGGQGSGS SLSYLTEPPS FTAIADPNTV VSLKNVLKKD
STTKTKALDE LLAYVQAHPH DKDGGVEDAI LDVWTQVYPR VSIDNARRVR EQSHQLQFEL
VKSARKRMER HIPKVVGAWL AGLYDRDRAV ARAASDGLGS FLTSPEKADA FWKKCQPQIL
AFALEAIQET QDSLSDERST TKEDAEAKYF RVINASLSLV LRLLQRMDDS DMDRCRDSYE
EYFASDSVWK SITVADPSVR RSTCQLLVSC LDRKLSYADS VECRQAMITG GLKTSQVGSA
NEYILALAKL TKDHPDSWEA STKSKKSSTA RLHAFIAKGS QGSRAIFWES LDTLLSLLPR
SVVNLDSESE LLNSLRSGIE HREEPRSNAE LAWKCYSNAA QRALQSLNET DACELVKSHI
FPLLENFLYL PAGRSSSIGL STLGDIYGAA TASSPAVATA VGEELTRLGA KLCTHLSGSL
PSVSKEYQSS QEKVGEEGRR WFQLSKELHQ RSKSGIPSEL VDRPSLTIIS QCVSLLESRN
MKPFGAARTL EQALRSTPHL FSGDAGVRIS NFFLAAAEDY MDKLVESSSA AILLTCLDLS
SSIENLSTLY KSTWRAWVNE TLSLTPGEKR NDVLAGLISQ KAAADLAQSN QAVQAQVLEQ
ATAAVDGTGG SKSLLAAAVS SGTFSSEHIQ TLAKHAIDVL QQKPSAGPLD ILAIVASEDP
KLLSENDDLH TSLVAVLLGL SELDGNASVA GKAAKVRALM DQHTDSKLPT VGIILSNLER
ATPQSLDIET LVKQAKEASS TAVPLENLLP STNIWMEQLK PFFDLPINPV LSISSPIGGA
TTLSTSSPTL TKKTLRVPRD RRGRSVPARM AIYLSLLTTE GIDLTKLPSQ FLVELLYLQC
ITVQLISDQI TLGDRNGLFF NLDSEESMRE ADTVITSLRL LLNKYTAEKE WWVTGKGDFE
AELIRELANL LVQQSKSLSP TAAYSSRALS ELLQATAESQ GLSTSLEEHF VKSEYLKSTS
DTVLVSAAIL AGLGESLQAS KQISTFCNRL VSDVAGASAD GERTKSILSL LTLCSRLYES
GGLPVANNRI VFAVRQITSW LEEPELLDAQ ISTEICRTLA SLLPCMKDVY GSYWEKTVAF
CLDTWRNESE FDLEDLLPLV HASLKLGRVL ETISEPNDDM EDALKDLDAD KPAALVELMR
LLRDVDTPAA EIVTTVLSRE VGKIKVRQIP DLGDIYPLLA SESRDIQTAA FGLLHRAIPA
QQEQASVDVL LDKMDARLPD ELLSLLLDAP TLESYSDESL TQFPLAIRCY LLSWKLVFDA
FSGASFKVRN DFAENLKTEN YVGPLLDFTF DVLGHSAAHA LNLDKENLSL EHIYNYDVTL
ANADTEEKSM QWLLVHLYYL VLKYTPGLFR TWYIDCRSKQ TRIAVEAWTT KYYSPLIIGD
NLDEVQQWAD AQEPPAMDEQ ELQVRVSKAA REVTAGYEVD ESQASIVIKV PASYPIESVT
VSSLNRVAVT DRKWQSWIMT TQGVITFSNG NIIDGLQVFK RNIIGALKGQ SECAICYSII
STDKRMPDKR CTTCKNLFHR TCLYKWFQSS NQNTCPLCRN PIDYLGADTQ KRRQ
//
