ID Q8KWV4_CLODI Unreviewed; 591 AA.
AC Q8KWV4;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=fbp68 {ECO:0000313|EMBL:AAM73699.1};
GN Synonyms=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
OS Clostridioides difficile (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=1496 {ECO:0000313|EMBL:AAM73699.1};
RN [1] {ECO:0000313|EMBL:AAM73699.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14523111; DOI=10.1099/mic.0.26145-0;
RA Hennequin C., Janoir C., Barc M.C., Collignon A., Karjalainen T.;
RT "Identification and characterization of a fibronectin-binding protein from
RT Clostridium difficile.";
RL Microbiology 149:2779-2787(2003).
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; AF394222; AAM73699.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KWV4; -.
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 466..560
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 312..339
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 591 AA; 67679 MW; 89C6C4594FB74185 CRC64;
MAFDGLVIHS IVDELSSKLT GGKIDKIHQP EDDEVIFNIR NNKENFRLVL SASASNPRVY
LTSNYQKENP LKAPMFCMLL RKYIQGGNIV EISQIGFERI IKISVESLDE LKEKTVKNIM
IEIMGRHSNI IITHGEENKI IDSIKRVPFS ISRVRQVLPG HDYSLPPEQN KLNPLDDISK
DLFIKNLEEL EGPIFKSIYS RFLGISPIIA KEICYRAGVN QNAIIKDISD EQFDSLHKVF
CNLFNDINSN KYSPCIIIDK KVDKVVDFSC INLTLFSDLS YINKDSMSRI LEDFYRTKDI
KDRINQRSSD LKKSISVKLD RLYNKLKKQE EELSESENAD IYKIKGELIT SYIYMVEKGM
ESIEVANFYD ENCNDVTIEL NKNLTPSENA QKYFKKYNKM KHAKVEISHQ ISLNKEEIDY
LENIILSIEN CENLAELQDI KEELAKVGYI KTQKKNSKKD TIPSTKPHEF VSSDGFKILV
GKNNKQNDYL TLRLADNDDL WMHTKNIPGS HVIIKCAGKE VPDNTVFEGA MLAAFFSKSK
LSSQVPVDYT KRKNVKKPSG SKPGMVIYET NSTIYVTPEE ETVAKLKVKS E
//
