ID A0A0B0D5W6_9BACI Unreviewed; 577 AA.
AC A0A0B0D5W6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LD39_09400 {ECO:0000313|EMBL:KHE71517.1};
OS Halobacillus sp. BBL2006.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1543706 {ECO:0000313|EMBL:KHE71517.1, ECO:0000313|Proteomes:UP000030879};
RN [1] {ECO:0000313|EMBL:KHE71517.1, ECO:0000313|Proteomes:UP000030879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBL2006 {ECO:0000313|EMBL:KHE71517.1,
RC ECO:0000313|Proteomes:UP000030879};
RA Kirchner G., Treves D., Francis J.III.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BBL2006.";
RL Submitted (SEP-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}.
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:KHE71517.1}.
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DR EMBL; JRNX01000285; KHE71517.1; -; Genomic_DNA.
DR RefSeq; WP_035545531.1; NZ_JRNX01000285.1.
DR AlphaFoldDB; A0A0B0D5W6; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000030879; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000030879};
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 452..540
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 426..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 66590 MW; 8D2EF9DCDB7DF204 CRC64;
MSFDGIVTRA ITNELNEKIQ SGRIMKIYQP TDTELIFTVR AQRKNHTLLL SAHSSYARFH
LTEDQYSNPK EPPMLCMLLR KHLVGGFVEN IEQEDMERIV KFRVRTRNEI GDETVKTLII
EVMGKHSNIL LIDENQGHIL DSIKHLPPSQ NRHRTIMPGQ PYKLPPEQGK ISPLDLEPDD
LIRKLDFNAG KMDKQILGVV MGFSPMITKE IAYQAKLGGP DAYKEAYAQV RERVVNHDYE
PQVNLGEREQ FYVLPLHTFS EDTEQFTSIS EMLDAYYSGK AERDRVKQQA GDLYRFLKNE
RDKNVRKIKK HHHTLKKSES AEEYQRLGEL LTAHMHMVKN GDAQVTVVDY YDPDQAERTI
ELNPNKSPSE NAQNYFQTYQ KLKKSKQVVQ QEIKKAEDEI QYFERLIQQV ESAREQDIEE
IREELREQGY MKKKPSAGKK KNKPAKPAPE SFISSDGTQI YVGRNNKQNE YLTNRIANKS
DIWLHAKDIP GSHVVIRDEN PTEDTLFEAA QLAANFSKSS KSSTVPVDYT QIKHVKKPSG
AKPGYVIYDH QQTLFVTPET SFVKKLRKLA KEKSRDS
//
