ID W8Y7E7_BACTU Unreviewed; 569 AA.
AC W8Y7E7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BTDB27_003730 {ECO:0000313|EMBL:CDN37388.1};
OS Bacillus thuringiensis DB27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1431339 {ECO:0000313|EMBL:CDN37388.1};
RN [1] {ECO:0000313|EMBL:CDN37388.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB27 {ECO:0000313|EMBL:CDN37388.1};
RA Iatsenko I., Pickard D., Corton C., Dougan G., Sommer R.J.;
RT "Draft genome sequence of highly nematicidal Bacillus thuringiensis DB27.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDN37388.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB27 {ECO:0000313|EMBL:CDN37388.1};
RA Aslett M.;
RL Submitted (JAN-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}.
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DR EMBL; HG810018; CDN37388.1; -; Genomic_DNA.
DR RefSeq; WP_030027587.1; NZ_HG810018.1.
DR AlphaFoldDB; W8Y7E7; -.
DR HOGENOM; CLU_022481_2_1_9; -.
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};
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 453..540
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 569 AA; 64914 MW; 14C731C3943F4EA6 CRC64;
MAFDGLFTRA ITHEIENSLY TGRISKIYQP SKYEILLHIR ANGKNQKLLL SSHPTYARMH
LTNQNYDSPA IPPMFCMLLR KHLEGGFIEK IEQIDLERII QITVRSRNEI GDESLKTLVI
EIMGRHSNII LLDTKTNVIL DSLKHVSLAV NRHRTVYAGA EYVAPPAQHK INPLQIETAD
DFIRPLDFLS GNMDKQLVGA FMGISPLFAK EIVKKAGMVN EKALSEAFFS IQTPLLSHAY
TPTMITANGK EFFYLFPLTH LQGEEKTFSS VSELLDRFFF GKAERDRVKQ QAHDLERFMQ
NEKNKNEKKL IKLQKTLQDA GKADKYQLFG ELLTANMYAL KKGDKDIEVV NYYDENGGTV
KITLDPLKTP SENAQRYFQK YQKAKNSVVV VEEQIEKTNE EILYFDSLLQ QMEAASSKDI
EEIREELAEE GYVRNRKTKN AKKKPTKPVL DKYVASDGTE IFVGKNNKQN DYLTTKFARR
DEIWLHTKDI PGSHVVIRSL EPAEETLLEA AKIAAYYSKA KESSSVPVDF TKIRHVKKPS
GAKLGFVTYD NQQTVYVTPD ADIVMKLKA
//
