ID A0A6A7K9C2_9FIRM Unreviewed; 588 AA.
AC A0A6A7K9C2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, 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=GC105_09500 {ECO:0000313|EMBL:MPW26024.1};
OS Alkalibaculum sporogenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibaculum.
OX NCBI_TaxID=2655001 {ECO:0000313|EMBL:MPW26024.1, ECO:0000313|Proteomes:UP000440004};
RN [1] {ECO:0000313|EMBL:MPW26024.1, ECO:0000313|Proteomes:UP000440004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M08DMB {ECO:0000313|EMBL:MPW26024.1,
RC ECO:0000313|Proteomes:UP000440004};
RA Khomyakova M.A., Merkel A.Y., Bonch-Osmolovskaya E.A., Slobodkin A.I.;
RT "Alkalibaculum tamaniensis sp.nov., a new alkaliphilic acetogen, isolated
RT on methoxylated aromatics from a mud volcano.";
RL Submitted (OCT-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:MPW26024.1}.
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DR EMBL; WHNX01000013; MPW26024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A7K9C2; -.
DR Proteomes; UP000440004; 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; 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; 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:UP000440004};
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 472..565
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 588 AA; 68083 MW; A475D8B7D98D2A39 CRC64;
MPYDGITTFC VVEEIKNKLI QGKINKIYQP ESDEIILNIS NKGNKYSLLL SANNNNPRVY
LTNKTKNNPL APPMFCMLLR KNLQNAVILD ISQVSLDRII EITLNSKNEL GDNVTKKLIV
EIMGRHSNII LINEPENTII DSIKRVGTNI SSYREVLPGK QYVNPPQSKR DPREMDLESF
ISIIDLYKQN KATHKFVMDS FIGVSPPLAH EICHRAKISS DTLVGSLSEE NKLKLFETFT
ALFNNLTHHM KPIMYTNHNK SKIYDFSAIA FTYYELYDIQ NYESISILLE EYYYLKDNLS
RIKNRASSIM QMLNNKLDRN YNKKSKQLDE LQKAHDSEIY RKYGELITSN IYLLKQGQQS
TVLLDYYTGV DIEIPLSIQL SPSQNAQKYF KKYNKGKRAK EYLEEQIAIT EDEIYYLESQ
IDNVNKCSEI NEFNEIKEEL IENGYLKPQG SKNKKKKKED VLSQPLKYVF NNVEIYVGKN
NKQNEYLTMK FASKTDLWLH VKDAPGSHVI IKKDYDKVDE KLVYTAALLA AYYSKLRNSS
NIPVDFTAVK YVKKPKGLKT GMVIYTDQKT VYVTPNEEEI LSLDLIKY
//