ID Q0SRX7_CLOPS Unreviewed; 575 AA.
AC Q0SRX7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=fbpA {ECO:0000313|EMBL:ABG87850.1};
GN Synonyms=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN OrderedLocusNames=CPR_1815 {ECO:0000313|EMBL:ABG87850.1};
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380 {ECO:0000313|EMBL:ABG87850.1, ECO:0000313|Proteomes:UP000001824};
RN [1] {ECO:0000313|EMBL:ABG87850.1, ECO:0000313|Proteomes:UP000001824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A {ECO:0000313|Proteomes:UP000001824};
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., Deboy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000312; ABG87850.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0SRX7; -.
DR SMR; Q0SRX7; -.
DR KEGG; cpr:CPR_1815; -.
DR Proteomes; UP000001824; 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; 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; PF18297; NFACT-R_2; 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};
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 455..547
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 575 AA; 66405 MW; CCA36E9D4F82A2B3 CRC64;
MALDGIYLYN LINELKDSLI NSRIDKINQP EKDEIIINVR GKENKKLLIS SSSKYPRLHF
TTISKNNPLQ PPVFCMVLRK YLTGGRIIDI YQQSTDRIVS IDIANKDEMG FHSVYTLVVE
IMARHSNISL VRKRDNKIME SIKHITANKN SFRVLYPGVS YVFPPASEKL NPFDFSKEDL
KIELSKNNNE LDEKIFSKLL TGVGKNLSLE MYSLFKSQFG DSYVFDDIFN FICNYFTNIF
KDIQNIIFYK NEKIIDFYFK DLSILDNCTK EVYDNSSELL DAFFANKDKQ DRLHAKSADI
QKLVNTNIDR CLKKIKVLEK TLEECSKKEE FKIKGELLTS YIYSIKKGDK SVDLLNYYSE
DEEYLTISLD ENKTPSENIQ FYFKKYNKLK KAEESALEQL AINEDELKYL NSVSSSIQVA
DNYEDIDAIK NELIETGYIR FRRNNNGKKK EKQSKPYHYV SSDGIDIYVG KNNIQNDYLT
LKFADKNDTW LHTKDIPGSH VIVKSSNIPD KTLEEAANLA VFYSKGKGGT KIPVDYTLVK
NVKKPSGSKP GMVIYSTNKT VYMDSPKEIT LEKLK
//
