ID A0A4R1Q344_9FIRM Unreviewed; 585 AA.
AC A0A4R1Q344;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=EV210_101105 {ECO:0000313|EMBL:TCL39908.1};
OS Anaerospora hongkongensis.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Anaerospora.
OX NCBI_TaxID=244830 {ECO:0000313|EMBL:TCL39908.1, ECO:0000313|Proteomes:UP000295063};
RN [1] {ECO:0000313|EMBL:TCL39908.1, ECO:0000313|Proteomes:UP000295063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15969 {ECO:0000313|EMBL:TCL39908.1,
RC ECO:0000313|Proteomes:UP000295063};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TCL39908.1}.
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DR EMBL; SLUI01000001; TCL39908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R1Q344; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000295063; 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}; Reference proteome {ECO:0000313|Proteomes:UP000295063};
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 469..555
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 585 AA; 65204 MW; 1ACDAA1E428B846B CRC64;
MSLDGLSLSA LIQELHHQLI GGRIDKIFQP DKNTLLLWIR QPQETIKLLL SVAADYPRIG
ITKHAPDNPA APPTFCMLLR KHLENGRIGQ LTQHGLDRII ILDIDVRAEQ GAITTKRLII
ELMGKHSNII FVHDNTILDS IKRVNVYMSR QRQVLPGRPY SLPPGQEKLN LFHTAASEVV
EQLLMLQQDA LLAKGLIQTV NGLGPVAARE IIWRAGLPEK TAVNDLDSAD KQSLVETIAE
LTSQLAPSAV QPTVAVSEQN ELLAVAAFSL GHLTKARQLT FPTMSLALEF AETLKGPRKL
PAKEVLDKLL HSELTRLQRK KSLLETEWEE ALQADSCRLF ADTLMIHLHD IPANSIQAEL
PDLFSESGNE LLVIPLDPLL SPLANAQNYY SKYNKLQRRQ QMTQQQLEQC IREIDYLESV
LFSLDAAGSA DDINEIQQEL GEAGYLQLKG KPRKQAAPAA GKPTQVVVDG IPILIGRNNR
QNDWLTFKQA RPDDLWLHTK DIPGSHVIIR CKTEDIPEKV LYTAAQCAAW FSKARSSSSV
PVDYTRRRNV KKPSGAKPGF VIYEQQRTLQ VTPDKALLTA LLAVE
//