ID A0A178ARS2_9PLEO Unreviewed; 1613 AA.
AC A0A178ARS2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=IQ06DRAFT_294692 {ECO:0000313|EMBL:OAK99317.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK99317.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK99317.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK99317.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441714; OAK99317.1; -; Genomic_DNA.
DR STRING; 765868.A0A178ARS2; -.
DR InParanoid; A0A178ARS2; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000077206; 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; 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; 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:UP000077206};
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 1561..1607
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1613 AA; 177461 MW; 681CB4B03D4E20F5 CRC64;
MSKRAAKSAS SARAASTFGS SAFGSSASTA FGVASSALSY VSEPPDLSAI SDPNVVVYFR
NLSKRDSTTK AKALEDIQAY VAKEPVEEGL LEAWVKIYPR TSIDNSKAVR QNAHILHGQL
AASAGKRIAK HMPPSVAAWL CGLYDADRSV VEAAQSSLRQ VFTTPEKIQN IRKAYQQPIL
EYCRDAIDKE SAATLSDERT VTPDDAEAKY SRVISACIAL LGSLLANLQR EELSKYQTDY
ENLLGDKKLW EFASSNDASI RRSLHRFLKT CLAKEPEAVS ANLETISKSY LSVALNSDQT
NSAFEYIDAL ITLTTDHPTV WTEHYKSKTS VDRRLRQFLK KGSQSGPRDY WARLPILLRA
IPGEALPANA ADAAELLNAL QSGIIKKDEP KYHHEAAYTA YIEILALING RLPDEDKTKL
LGEMVLPLIT QYLHPTVETS QWTIPSNATT LLNKAMGVDG MAAMLAERWP ACAKQLVDAI
KTSAPEQSKD YERSQTSIGQ HANRFATLQE QALKISAFAP VKPIFAQASA SVVDEALGVL
KNRNGKPYGA AAAIAAILGR NNTLIESTQT QQHLETFLHT ELPALVGSPS STYLIDLLYS
CSSTTTFNDT WSGTLKAILK LPESPAKPKA LEALLTSSRI PNTFDLAASD AELQAFLRQS
VRESVQGSLE WDTFNRVMQS PAKIIAPETS ADILTQLTQS LTISEQATHS LQGLRQITRS
NPSMLKEFVS TSSGSQLLQS LLLASESPND EVAQGAAAVN SSIQTMLSSG SETKQSMYDL
IHQGLREATQ TSVSVETLVD LAKQQVQGAQ DWDTLQNIFP RVEDWDHALA PFLGVAPPPS
LAITNPLGGA LYLVGSDQTV ANVEISRDVD GYSAAYRITQ YVTRLLKEHD QFPVQKIPAG
TRDLYLRNIS LTVQLADDNL GLAGANGLWA DYNADVETDA MTFISDAQAF IAQETKRLSS
TWSEGDGFMP GAIAFLDQAA EDTSAKAYYK ARAHSVLVAD AIEAAGWRNT QTTQLQEALR
SIRKTKAVLP IVAFTNAFKE PLSASKSCER MCNEIIADLT GLDIEQKETE GLRQLIQLNS
LLYGQEGIIE SIAKQRLVFF VKHVIPWLEM AGPRKSVKAE LCRALTVLLP LMSDMYGDHW
TNILSSLAGS WAATTKLESD TGVDSPIPHV HASLKLYAQL RALTQTEEPN DDLLDAWKET
EQTVADGLIN LLKHSQHFPD EFHQPLKMVN DVLARQIAKV SLKNLESTEE LFPLLYVESQ
PVQQTAFNIL HKQIPEAQEQ ISIDAALEKT TARLPEELLS LIIDAPTTSA LAEANFERSV
PLPLRGYLLS WLLVFDHLEH ASFKVKNDYV DHIKEGDYLP GLLNFTFDFL GHAHNKPVDV
SKFDITTYEP DVESPRRDLQ WLLTHLYFLC LKHVPSLTKS WFIDCKSRAT VVTLEPWTEK
FISPPVISAA LASVATWSTS QQDSEPDSPF TVKVSSRARE ITASYLVDEQ TMSMRISLPP
SFPLSNASIE SLARVAVNET KWQSWLRTSL GAITIFNGSL IDALTTFKRN VDGAMKGQTE
CAICYSIVGS DRRLPEKRCG TCKNLFHGGC LFKWFKSSGS SSCPLCRNPF NYG
//
