ID A7GEM5_CLOBL Unreviewed; 576 AA.
AC A7GEM5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 OrderedLocusNames=CLI_1977 {ECO:0000313|EMBL:ABS42386.1};
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS42386.1, ECO:0000313|Proteomes:UP000002410};
RN [1] {ECO:0000313|Proteomes:UP000002410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F
RC {ECO:0000313|Proteomes:UP000002410};
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000728; ABS42386.1; -; Genomic_DNA.
DR RefSeq; WP_012099937.1; NC_009699.1.
DR AlphaFoldDB; A7GEM5; -.
DR KEGG; cbf:CLI_1977; -.
DR HOGENOM; CLU_022481_2_1_9; -.
DR Proteomes; UP000002410; 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 456..554
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 576 AA; 67180 MW; E0A6A05A7DE0A4B5 CRC64;
MALDGIFLFS MINEMKTKIL NGRVDKVTQP EKDEIVLSIK NNRKTYKLLI SSSAVYPKIH
FTDIPKQNPM QPPMFCMVLR KYLNSSKIIN IRQLDTDRIV LIDFESADEM GFNSIYTLII
EIMGRHSNIT LVRERDNLIM DSIKHVTPEI NSVRNLYPSI EYIYPPASLK LNPFNFSLED
FKDYIKDNNV KLNKTMFSNI FTGVAIPFSK EIFYRLEREN NLEITLENMD EICVIAKNIF
DSIKNKEFYF NCYLEKDTVK DFYCVNLHSL DNFKNIHYEN PSILIESFYF EKDKADRLNS
KSSDLQKLIN LNIERCEKKI KILEGNLKDC DEKEKFQICG EILTANIYAL KKGMDKVNLL
NYYTNEYMDI KLDPNKNPSD NIQKYFKKYN KLKKTEVAAK EQIELTCDEL KYLNSVLTSI
KNADSYDDIE EIKRELIETG YIKFKKKNNK KFKNTKPLHF ISSDGIDIYV GKNNIQNDYL
TLKFASNHDI WMHTKNIPGS HVIVKNFQGN VPEKTLEEAA TLAAFYSKSK DSTKVPVDYT
EVKNVHKPNG AKPGMVIYYT NKTIFIDPKE PNLKQI
//
