ID A0A4R7KSN0_9CLOT Unreviewed; 578 AA.
AC A0A4R7KSN0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
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=EDD71_1051 {ECO:0000313|EMBL:TDT61825.1};
OS Fonticella tunisiensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Fonticella.
OX NCBI_TaxID=1096341 {ECO:0000313|EMBL:TDT61825.1, ECO:0000313|Proteomes:UP000295325};
RN [1] {ECO:0000313|EMBL:TDT61825.1, ECO:0000313|Proteomes:UP000295325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24455 {ECO:0000313|EMBL:TDT61825.1,
RC ECO:0000313|Proteomes:UP000295325};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TDT61825.1}.
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DR EMBL; SOAZ01000005; TDT61825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R7KSN0; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000295325; 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; 3.40.970.40; fibrinogen binding protein from staphylococcus aureus domain like; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000295325};
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 457..552
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 578 AA; 66718 MW; 9083516F378DBA62 CRC64;
MPFDGIFTSS VVKELSSLVD GKIDKIHQPS KDDIIIFIKK EHKNTKILFS ANPSYPRVHI
TRISTQNPPV PPTFCMILRK HLTGGRITYI RQVDFDRIVE FIIEGKDELG YPVVYRLIIE
IMGKHSNIIL LNNENIIIDS IKHVGSSISR YREVLPGVKY IQPPTQDKIN PLTITKNDLE
EIFNRSGEIP SFKVFINSFF GIGKVFSYQI CGELSVKKIC ELSEQEREML ISNFFYYTSK
IKSGDFDNFI FYRNSDMVDY YAMSLKEYKD LEKIHFESPG ELLDTFYGSR DLRDRLKQKY
NDVFKIVTGL IEKNIKKIQI HRSKLEECKD FEKWKLYGDL IMANQYTIVQ GSDGVMLQNF
YDESLSEVFV PLDKEISPVE NAKKYYKRYS KEKSTVQIVS KQLEESLEEK DYLETILFNL
ENASDIETIE EIINELSEMG YIKKRRNGKN QGKAAPHHFI SSDGFDIYVG KNNKQNDYLT
TKFAISSDIW MHTKNIPGSH VIIKSRAGKV SDTALLEGAI LAAYFSKAKN STNVPVDFTE
RKNVKKPSGA KPGMVIYYTN RTIYVTPDEE KVNRIKKV
//