ID A0A1V2YBE1_9FIRM Unreviewed; 587 AA.
AC A0A1V2YBE1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN ORFNames=BEN19_03440 {ECO:0000313|EMBL:OOB76908.1};
OS Epulopiscium sp. Nuni2H_MBin003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884657 {ECO:0000313|EMBL:OOB76908.1, ECO:0000313|Proteomes:UP000189211};
RN [1] {ECO:0000313|EMBL:OOB76908.1, ECO:0000313|Proteomes:UP000189211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nuni2H_MBin003 {ECO:0000313|EMBL:OOB76908.1};
RA Ngugi D.K., Miyake S., Stingl U.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ribosome quality control system (RQC). Recruits
CC Ala-charged tRNA and directs the elongation of stalled nascent chains
CC on 50S ribosomal subunits, leading to non-templated C-terminal Ala
CC extensions (Ala tail). The Ala tail promotes nascent chain degradation.
CC May add between 1 and at least 8 Ala residues. Binds to stalled 50S
CC ribosomal subunits. {ECO:0000256|HAMAP-Rule:MF_00844}.
CC -!- SUBUNIT: Associates with stalled 50S ribosomal subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00844}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000256|HAMAP-
CC Rule:MF_00844}.
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:OOB76908.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDJN01000203; OOB76908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2YBE1; -.
DR STRING; 1884657.BEN19_03440; -.
DR Proteomes; UP000189211; Unassembled WGS sequence.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR HAMAP; MF_00844_B; RqcH_B; 1.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR InterPro; IPR043682; RqcH_bacterial.
DR PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
DR Pfam; PF05833; NFACT_N; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000189211};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00844};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00844}.
FT DOMAIN 462..559
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 587 AA; 67428 MW; 30CEE592773A4957 CRC64;
MALDGIVLSN IIHELKQKII GGKIDKIYQL EQAELLLTIR NNKTNYKLLL NAGSQYPRIN
FSTLSKNETN TPPMFCMFLR KHIGGGKIID IIQPNFERIV KICIEAKDEL GDITNKILIL
EIMGRHSNII LIKEDNLILD SIKHISYDKS KVRPILPNYI YNYPPNQDKL NPLLVNKLTF
IEAISSLDNE IYKRLYQTFS GLSPLISRQI CLDAKLDSHA KDISENGLLA LYNAFNNIIT
YVKSANFTPT LYETQDGDLV DYYSFDLPII EADKKTHNQS INDILEQFTH TKNHRYNISQ
KTADIKKLII TFIDRTTRKE ALLQQAVKTS TDNELFKIYG ELITAYSYNI TPGDNNFTTL
NYYDTNPQEI VIPLDTNKSA IENAQAYFKK YSKLKRAHSA ALEQLDIIKD DLKYLQSVLV
CLDMLENETD IMELRQELID MGYLKRKLKD SKKKTKNKQP YLHFKTSSNL DIYVGKNNYQ
NDELTMKFAK AHDMWLHLKN GAGSHVIIKS QNGYEFTNQD LYEGAILAAY HSSARLSSNV
QIDYTLRKNI KKIPSQKPGM VIYNNFKTLS VTPTENEVNM LLAVTNK
//
