ID F7V683_CLOSS Unreviewed; 580 AA.
AC F7V683;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=CXIVA_22950 {ECO:0000313|EMBL:BAK48262.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK48262.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK48262.1; -; Genomic_DNA.
DR RefSeq; WP_013978219.1; NC_015737.1.
DR AlphaFoldDB; F7V683; -.
DR STRING; 1042156.CXIVA_22950; -.
DR KEGG; cls:CXIVA_22950; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR OMA; SWHPQAA; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000008937; 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; NUCLEAR EXPORT MEDIATOR FACTOR 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}; Reference proteome {ECO:0000313|Proteomes:UP000008937};
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 461..553
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 391..425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 580 AA; 66157 MW; 8F492A2D3D87A6E8 CRC64;
MAYDGIAVSN IRHDLAEEFT GGRISKIAQP EKDELLLTLK GTDGQKRLLI SASPSLPVIY
LTEENKKSPM TAPNFCMLLR KHVSGGRIVN ITQPGFERIL IFEIEHLDDL GDLCRKQLIV
ELMGKHSNII FCDASGRILD SIKHISANIS SVREVLPGRQ YFIPRQEGKT SPLDLTDGQA
LIQRLKSRPM PAARAIYSSY TGFSPLAAQE ICYRAGIDGD APVDSVTALQ WDRLAETWIH
FMDAIRNGDF YPNMILDEGR PLEFASYHLT MYRDKETVPY DTVSHLLVDY YAKKAADTRI
HQKSADLRHQ VNVLLERTRK KYYLQQKQKK DTEKRDKYRK YGEMIHAYSY LLKKGMAGFE
NTDYETGKQM QVPLNKDLTP MENAAKYFAR YNKLKRTDEA LTIQLQETKD DLTHLESIAA
SLEIAENEAD LVQIRQELAD AGYLKRPSGK QKKSREVSQP YHYRSSDGFD IYVGKNNIQN
DALTFRFAQG NDWWFHAKGM PGSHVIVRCK TGELPDRTFE EAGRLAGYYS AGRGSEKVEI
DYLQKKNVKK PNKAKPGFVV YYTNYSLTID TDITGIERIE
//