ID A0A101HBR0_9FIRM Unreviewed; 578 AA.
AC A0A101HBR0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=XD91_0221 {ECO:0000313|EMBL:KUK73981.1};
OS Clostridiales bacterium 38_11.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1641393 {ECO:0000313|EMBL:KUK73981.1, ECO:0000313|Proteomes:UP000053314};
RN [1] {ECO:0000313|Proteomes:UP000053314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK73981.1}.
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DR EMBL; LGGM01000006; KUK73981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101HBR0; -.
DR PATRIC; fig|1641393.3.peg.1753; -.
DR Proteomes; UP000053314; 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; 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; IPR010979; Ribosomal_uS13-like_H2TH.
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; PF18297; NFACT-R_2; 1.
DR Pfam; PF05833; NFACT_N; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844};
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 464..562
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 578 AA; 67002 MW; ED77585E17CA91DE CRC64;
MSLDGFVVRN LVFELNNTII ESKIDKIYQP ENDEIILHLR ASSKNLQLLL SANSTYPRIN
ITSGKYLNPT VPPSFCMFLR KHLTGGIIKK IQQINMDRVI MIEVASKNEL RSETTRRIYI
EIMGKHSNII LTDEKNLVLD CIKRISLSIS SKRQVYPGIK YKMPNFDKKN NLLNINENQI
RLLLNHFNQG VRIGKFLIGS FYGVSPLLSR EVCFLSGIDD SDSIGTLNDI KVSKLIETLM
ALKCSMSQYS FKPMIFINPK SKEYMEFYCF DLKHLPQMER ISYKSINEIL DLFYLEKSKF
ISYKQKTSEL RKRVVSLIDK YEKKLGYLKI ELINAEIREQ YKLFGDLILA NMHKIANKDT
ELIAFDYLAS EEIKIELDPS LNASKNAQKY YKKYNKLKNS EKYLKKQLKI TQESLNYLRN
ILFSLEEAIE LAVVDEIKEE LYKSGYIKKS TQKKKPEKSK PLRIVTKDDF EIYIGKNNEQ
NDFLSFVIAT KNDIWLHAKG VPGSHVIIRS DNREIPDAVL EEAAAYAAYY SRNRGSEKVE
VDYTLKQNLK KPKNAKPGLV IFNENYSLVI EPKKPDLS
//
