ID A0A1X7HK08_9BACL Unreviewed; 586 AA.
AC A0A1X7HK08;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN05661091_4031 {ECO:0000313|EMBL:SMF87956.1};
OS Paenibacillus uliginis N3/975.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1313296 {ECO:0000313|EMBL:SMF87956.1, ECO:0000313|Proteomes:UP000192940};
RN [1] {ECO:0000313|EMBL:SMF87956.1, ECO:0000313|Proteomes:UP000192940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N3/975 {ECO:0000313|EMBL:SMF87956.1,
RC ECO:0000313|Proteomes:UP000192940};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT840184; SMF87956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7HK08; -.
DR STRING; 1313296.SAMN05661091_4031; -.
DR Proteomes; UP000192940; Chromosome i.
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; 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:UP000192940};
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..550
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 586 AA; 66435 MW; F23570B3D7ABF2E0 CRC64;
MALDGIVTRA IVHELTACRG ARISKIYQPN ERDIVLHIRS QNGNAKILLS ANPTYPRVHL
TEESFLNPPE APMFCMLMRK HCESGIIEEI KQIGMERIIH IRVRQRDELG DVSSKTIIIE
LMGRHSNIIL LDHSTGTILD GIHHVTPAIS SYRIIMPGVA YTEPPQQNKL NPLETVQEQF
RESCLLSSDD PIACLVDSFS GMSPLAAQEI AHRAGYTTGG DPSSAEKDCG GLWNAFSEIM
TEVENHRYTP VSGVNVKGKM VFSVIPLTML PGQTEHYDSP SKCLEDYYGD KAQRDTVKQK
VSDLLRFLQN ERSKNIKKLD KLHEDLEEAG DADRYRISGE LLFASLHSIQ KGDKQAELLN
YYDEDQQMIT IPLDPLLSPS DNAQRYFKKY NKYKNSLAVI DEQLIKTREE ISYIENLLQQ
LAHASLNDID EIREELIQQG YLRDRSRKTR KKKKNDKPTL HMYTSSEGIE LYVGKNNLQN
EYVTNRLASS NDTWLHTKDI PGSHVVIRSD SFGENTLQEA AQLAAYYSQA KESSSVPVDY
TLIRHVRKPS GSKPGFVIYD HQKTLFVTPD AQLIKSLPNV IKNQRK
//
