ID A0A348APL8_9FIRM Unreviewed; 589 AA.
AC A0A348APL8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=MAMMFC1_03725 {ECO:0000313|EMBL:BBB93016.1};
OS Methylomusa anaerophila.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Methylomusa.
OX NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB93016.1, ECO:0000313|Proteomes:UP000276437};
RN [1] {ECO:0000313|EMBL:BBB93016.1, ECO:0000313|Proteomes:UP000276437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMFC1 {ECO:0000313|EMBL:BBB93016.1,
RC ECO:0000313|Proteomes:UP000276437};
RX PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT utilizing bacterium isolated from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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}.
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DR EMBL; AP018449; BBB93016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348APL8; -.
DR KEGG; mana:MAMMFC1_03725; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000276437; Chromosome.
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:UP000276437};
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 470..559
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 589 AA; 65292 MW; 1C146A42AEE07F4A CRC64;
MSLDGLSLAP LVAEIHNKLA GGRVEKIFQP EPHSLLLWLR QPGASLRLMI SVNPERSEIH
LTETLPENPA TPPNFCMLLR KHLEDGRVAG VCQHSLDRIV VIAVDVLGER GVIVTKQLVV
ELMGKHSNII LLQDNLIIDS IKRVGFNTSR YRQVLPGREY VYPPGQDRIN LFSTPVNQFV
QHMVQSNSGN SLAKAIMNTA VGLGPLTAKE IAWRAGFSAD IKVNDLDEAD MAALHEAVLS
VIEPMQSGSG MVPNVVMDSG RAIGIAAFLI EHLKQYTTHR FDTMSAAVEF FSRTKGRPVI
ADRDILKKLL TTELTRLTKK QGILTQEIAE AEQSHLLKKY ADILMANLYN IPPGIDTVTL
YDFYNDSPDC ATENAEIVIP LEPSCSPLEN AQNYYHKYNK AKRARETLEI QLGLCRDDIL
YLESIAAALE NAENSAEVSD IRQELISAGY IKEAGKRRLP AAASQPLTVK TTDGFSILIG
KNNRQNDLVT FKHSSPHDIW LHTKDIPGSH VILRTENKQV SDQALSEAAL LAAYYSKARH
SATVPVDYTR RKHVRKPSGA KPGFVYYENQ TTIFVTPDET AVTALINNN
//
