ID A0A1H8ZE27_9FIRM Unreviewed; 588 AA.
AC A0A1H8ZE27;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN02910382_00498 {ECO:0000313|EMBL:SEP62664.1};
OS Butyrivibrio sp. TB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520809 {ECO:0000313|EMBL:SEP62664.1, ECO:0000313|Proteomes:UP000198682};
RN [1] {ECO:0000313|EMBL:SEP62664.1, ECO:0000313|Proteomes:UP000198682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TB {ECO:0000313|EMBL:SEP62664.1,
RC ECO:0000313|Proteomes:UP000198682};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOER01000003; SEP62664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8ZE27; -.
DR Proteomes; UP000198682; 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; 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 Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
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 468..561
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 390..434
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 588 AA; 66525 MW; 55008C99FF548482 CRC64;
MAFDGITVAA ITRELSDRCT DGRIYKIAQT EKDEILLTIK PQAERGGGQV RVYLSADASL
PLVYMSDENK PSPQQAPTFC MVLRKHLLNG RIKSIEQPSM ERIIRFNVEH MDEMGDMKTK
TLLIELMGKY SNIIFVDDDN TIIDSIKHVP ASVSSVREVL PGREYFIPDQ HNKLNPKEAT
RESFDKALLE KAGPVFKAIY GSYTGFASTI AQEICFRADV DSQLPASALS SGQMERLYNV
FDLFMTRIKD GEYKPAICYE NGQPKEYAPF HLMTYEKMPG CTLKDYDNMS SLLESYYAEK
NAITRIRQKS ADLRHIVATA LERTVRKYDL QLQQLKDTEK RDKYCVYGEL LNVYGYSAEP
SAKSITVNDY NTGNDLTIPL DPTLTASQNA KKYFERYNKL KRTAENLETL TKEVEAEKNH
LESIQNALDI AQGEEDLVPI RDELVEAGYI HKKGEKKKSS RLQTKSKPLH YKSSDGFDIY
VGKNNYQNDQ LTFKVANGGD WWFHAKGMPG SHVILQTGGK EVPDKAFEEA AALAAFYSKA
KEQEKVEIDY LQRKNVKKPG GAKPGFVVYY TNYSMAIKPD ISALTQAD
//
