ID A0A195CNB2_9HYME Unreviewed; 1225 AA.
AC A0A195CNB2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
GN ORFNames=ALC62_07025 {ECO:0000313|EMBL:KYN02241.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN02241.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN02241.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN02241.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN02241.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-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; KQ977513; KYN02241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CNB2; -.
DR STRING; 456900.A0A195CNB2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000078542; 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 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:UP000078542};
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 1175..1222
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1225 AA; 142013 MW; ED2DDEE1CCC8D735 CRC64;
MKIIVSDLRT MMIFVRYALD QSVKNFYFIQ ELPKFILIII HNLMTPSNSS RSAELLGTAM
PNFVGFSAVK DGGYVPVLPG LSLCSINEVE MNSIDSNFQV TLKKMSKKDA TTRFKALQEF
TTLCQDAELS TVEGMLPFWP RFYCALSIDI DHRVREATQL AHAALVKRVG KGIALYLKQL
AGAWFTAQYD TYPPAASAAI NSFNSTFPPW KIINAIIHCQ CEILLYISNN VIMHTAQTLS
TQKSLTKEEM EAIYERVLTA NLYGYNGYFK KVPLDEIDKT LEIHDKILSS SRFWKLAKHD
SLPIKTAFFN VLTSIMENAE KLLENEKKRT VTTIMNSLDE SEPAILSVVW ESMLTATTKI
DDWHLVVNIN KLVLPKLWHT LRSGGQCCAS TVYPNLLPFV SQFPKFNVDL TDLYTNFFNN
MRQGFSVKSV QMSRSETLAV TTSFIECLRY SILINTESVD LCIRLLKEQL MPVIETCMMD
STFMKQCCFV EITHLIRYWS KNRTNEKYKS YVSLMEQFWI ELLLLFEKYM NMLKGITYTA
DEKDSHIEFL LNLKNIPDRT RKKLKVKFSD PSDSVTINTN EPKVKVVDVY ADTVFNAELC
RFVNILFDIT KEIASCSDEQ YDFEKDQNLI LLAFEIPEII NLLINNNGTN EIVSILCDSL
NGRDDICSMQ FIVFITKLMT LMWKHSQTIS SAVQILETLF ELCTREHDAV DTMYNYWKAG
LVESSQILST FEFNDFIKRC GIIIWILDYD ISDISWDKLC LQLEVIRLFA TIVQHIPQKL
KQVYWDVILI FLTKWQQLYN KAKHHHSDIK MTMLIIAFSQ LYYAVETLMN KHKLKPLPEL
PSTLLDEWKN VIVGNIYNGI VRTWTIQLGA YYILKYMVSE LVQHDKILVE SDNFESSNLN
IKKFEEVLLN IQTIVNTMLM EFKLYDTITC TIQPFTDSYT YTLGYLLTWA IVLDICEKSD
SDLRYHYAEI LKIKLFPCLL DNIFKLIPME ALQDNRTVKL LELFTTAPVF CFKESWTEER
LGHIVCWLYT NCLRLLPVLV RQWLSTVDSR VNTTIDKITS HYVSPMLCEK ELFYSRLQLA
NVENMQIKVH STAREVVAAY QMEDTKLELS IVLPPNYPLG KIKIESGQQI DGTAKWKNSL
MQLAKFLTHQ NGSVWDGLLM WKRNLDKKFA GVEECYICFS IFHINTYQVP KFSCHTCRKK
FHTRCLYKWF NTSQKSTCPI CRNVF
//
