ID A0A095XK99_9FIRM Unreviewed; 581 AA.
AC A0A095XK99;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=HMPREF1635_00775 {ECO:0000313|EMBL:KGF10151.1};
OS Clostridiales bacterium S5-A14a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=1230734 {ECO:0000313|EMBL:KGF10151.1, ECO:0000313|Proteomes:UP000029601};
RN [1] {ECO:0000313|EMBL:KGF10151.1, ECO:0000313|Proteomes:UP000029601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5-A14a {ECO:0000313|EMBL:KGF10151.1,
RC ECO:0000313|Proteomes:UP000029601};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF10151.1}.
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DR EMBL; JRNA01000003; KGF10151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095XK99; -.
DR STRING; 1230734.HMPREF1635_00775; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000029601; 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; 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 Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000029601};
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 464..567
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 292..319
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 581 AA; 65454 MW; 55E72283FD2AB7CC CRC64;
MAFDGIMTWA ISEELSQKLT LGKIGKIYQP ESESLVFVIH TKDGRFRLYA SASGNAPHIC
LTQREFENPQ QPPIFCMILR KHIQGGRISR IAQNSSERII EIDFQVLDEL GFTVSKRLIF
EIMGKHSNII LVNLNDGRII DSIKRVSIDV NRARQILPGL IYNYPPSQGK TGFKELLGMS
DLNEENGHLV SVNWQDSNDI MDKVGGISPR VADSIALLGY DVFKDIIAKI KDLNSQTKIY
SNGKKLIDFH IVPMDGILSE IKSFDSPSAG VDYFFEHKKE TNLMQQAESN LLKKINSVRE
KLGLKLQRME EDVLKAKRSE HLRLYGELLT ANLHNIKKGE LMAHIVNYYD GSTVDIRLDP
KLSPSENAQN YYKKYGKAMN TIKEKQPMIE SVKAEIAYVD TVIDHLSRAT EIKEIDYIRD
ELIDEGYLKG RIFGKNGRSK NKSKSVKSSV SNGKINNPLV FALPTGRKII VGRNNKENDV
LTLRMASKSD IWFHTKDIPG SHVILQTGGI DLSSMEENFP EEIKTAAGVA AYHSKGKSSE
NVPVDYTEVR YVKKPSGAKP GMVIFKNNKT IWITPKIPSR P
//