ID A0A0K0DVZ3_STRER Unreviewed; 1438 AA.
AC A0A0K0DVZ3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-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|ARBA:ARBA00032366, ECO:0000256|RuleBase:RU367090};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000141000.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000141000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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 AlphaFoldDB; A0A0K0DVZ3; -.
DR STRING; 6248.A0A0K0DVZ3; -.
DR WBParaSite; SSTP_0000141000.1; SSTP_0000141000.1; SSTP_0000141000.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000035681; 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; 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:UP000035681};
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 1387..1434
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1438 AA; 167004 MW; 17960E7AE1BC3DB4 CRC64;
MGKGNSGSKV KTASSLRAAE NLISKGFSGG FIGFNAVGGS NVDGVIEESD LIIENLGEEY
SHELKILLKK IEKKDKLTKE KGIKELKEVV LKDNVSENKI IYNAYAVMFP KLCGHASPTI
RSLALDLLKI LISLLKKDAS KKLKLVMPYI IFSTSDASSQ VKRQGDSLIE VCFPGKRSQI
FITFKEQLND LCMQVINKTH KLMKPQKFVE DETDKQREGR LIAQSLGTLL KLIEYSNDKE
YNKKLSEKFS NPVIINYLTS LTVLVKATYL ELILKLSKDN EDIFIETKLS SIILSNLDND
DILLCKAAFN CFLKFAQNDK YFEKIDINKA IIPKIVKIVR KCYIKWSFIS DNLLPIFDII
YSLLEREIEK KTADSFVQSI NEIFKYSFFT SEGDTNLVNY LLEYFKRLLD YCFTINDSTI
TKCVLDLGIW IFKKGKEKKI MENKKFDMLV DYIIDGLVKK FPDFEDFSIK FYEGTNCQKF
KKDLLSFPQV STELYLSLTK DKSNDSQNIS LEPLFKRFTD TEDQTIKVQI LQKSLNESNE
KELCEYFEKH LDLNDPFTCL AVIQAIDDNN INKLNIVTIK NCILVIYNAV GNKKISGLVF
ESLKHLYKYF DDNACEKAFL SLIKVPSPDV YLALLDLLAN INYIPNIEGN LICFLFKILT
KIKKGISLEC SERFKKIFDT YNDGTYNIEE TNKIYESFLK SKKISRIIEF SENAAILSDC
NFLPFLIWDD KFDEYSKFLS KNFYSLLYKD VNEFNCEENI KDVNTEETFS LLLKKCLIIK
QIIKSDNQYD ENRGKKSVLL MMAFNRILQL IKQDSYMKDL ELDYTFDLEK YNPNELNLAL
TIEYRNYPCY KYLLTENKEI DVKKPTSKEL RTLIENNELK NKIYLDDDWE EWLFLYTEDK
KKLESLNYIL NVFLEDADIF NVYSLENADD FRVCGLVTLF SYCVENIENI ISNDNNISMQ
LFRNSIRLGC DIITKREKAA KKIRGYHTVA ENYELKEWIF VIQSVFPNIL KIFTHLNNIS
FSFYISNINL INSISNCIIT IIDQVKCDEI VNEPNMEMED STKKYIYIFT ELMQNKFSAH
IQIVAASLFH TVLPLYFYYE NKKLIDETKK ESENITAEKC VAILPPVITA LLKKIDLEQI
KIDNENNGLP TTYIPFELLL WNSLIYFFKT LEADEKLLYM EALDSELVSI GLGITMFYLP
DAPFNRENSS KKHFKEIPKF RNCPEDSYLT LSNYACYVFY QTLKTIPVFI RQWINLLPNS
TKGSIKDYIV KYFSPSIIDE ELNNSSTWKE KSGSRLSIKV YKVIKTIEAF YEIEPGSGMN
LRIILQDDYP LSLPIVETDK SVVAKKINNK WLMQVSTYIS HQNGLIISGL QQWKRNFDKH
LEGIENCSIC IMIVNSVNNQ LPRVKCKQCK HKFHAQCLYK WFDTSNNSSC PLCRTEFI
//
