ID A0A1I0HKQ7_9BACI Unreviewed; 570 AA.
AC A0A1I0HKQ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN05421676_10954 {ECO:0000313|EMBL:SET84544.1};
OS Salinibacillus kushneri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX NCBI_TaxID=237682 {ECO:0000313|EMBL:SET84544.1, ECO:0000313|Proteomes:UP000199095};
RN [1] {ECO:0000313|EMBL:SET84544.1, ECO:0000313|Proteomes:UP000199095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SET84544.1,
RC ECO:0000313|Proteomes:UP000199095};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOHJ01000009; SET84544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0HKQ7; -.
DR STRING; 237682.SAMN05421676_10954; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000199095; 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; 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 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 451..543
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 294..321
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COILED 379..428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 570 AA; 66519 MW; A236FC301D5CF4EA CRC64;
MSFDGVVTRA VVNELSTKLT TGRILKIYQP TNSELVITVR SHGENHKLLL SVHPSYARLH
LTNESLTNPK EPPMFCMLLR KYLSGGFIEK VEQKDMERMI RFRIYTKDEI GDITSKSLIV
EIMGKHSNIM LVDEEKNVIL DSMKHIPPTQ NRHRTILPGQ PYVFPPEQNK LHPLEIDGER
FVQKLDFNGG KLDQQMVQTL MGLSPLMARE LEHRAHLGSA RKYKDVFEDF QKDLKEHNYT
PTIYQGNKEQ FYVFYLDSLP NERITYASIS EMLDTYYRGK AERDRVKQQM GDIYRLLKNE
RDKNKRKIKK HQQTLKKAEK AEVYQKLGEL LTANMHLIKT GDSSVKVIDY YDPEQAEIEI
ELNPNKTPSE NAQSLFQTYH KLKKSKEVVT KEIDKANEEI QYLEQLMQQL ESAREQDLEE
IREELQEQGF IKKKRNKQKK KKNQKPQLDE YQASDGTLIL VGRNNKQNEY LTNRLANKEE
IWLHAKDIPG SHVLIRDTRP NEETIQEAAQ LAAFYSKSKM SSTVPIDYTK VKHVHKPNGA
KPGYVIYENQ KTVFVTPTEK KIHEMKKDRS
//
