ID A0A075R7C9_BRELA Unreviewed; 579 AA.
AC A0A075R7C9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BRLA_c034270 {ECO:0000313|EMBL:AIG27739.1};
OS Brevibacillus laterosporus LMG 15441.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG27739.1, ECO:0000313|Proteomes:UP000005850};
RN [1] {ECO:0000313|EMBL:AIG27739.1, ECO:0000313|Proteomes:UP000005850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG27739.1,
RC ECO:0000313|Proteomes:UP000005850};
RX PubMed=21914864; DOI=10.1128/JB.05696-11;
RA Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT invertebrates.";
RL J. Bacteriol. 193:5535-5536(2011).
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; CP007806; AIG27739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075R7C9; -.
DR STRING; 1042163.BRLA_c034270; -.
DR KEGG; blr:BRLA_c034270; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR Proteomes; UP000005850; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005850};
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 456..544
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 383..432
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 579 AA; 65844 MW; EB93C98B55691075 CRC64;
MKNVAFDGLV TRAVVHELSM LVGARITRIH QPHPSDIVMQ VRSNQGTLKL VISANPTYPR
IHLTTEEFMN PKEAPMFCML LRKHCENGVI EAITQDGMER VIYIDLKSRD ELGDTTRKRI
VVEIMGRHSN IILLDVKTDM ILDGIHHVSH GISQYRQVLP GRAYVAPPAQ NKLNPLTASE
QDFVMALQWN EGKLDKQLVE RFSGLSPLIA RELVSRATLP TRDAIWHEFS SFMEQMNLHR
YEPVIETTND KAAFSITSLS HLGVRESETF TSISECLQRF YEHKAMRDVV KQKVQDLLRL
VTNEKHKNEK KIEKLHHSIE DAHEAERYRL YGELILSHMH QVKKGDTELT ATNWYSENAE
TIVIPLDPLK TPSENMQAYY KKYNKAKASL AFIAEQISLA EQEVIYLDGI LVQLAHASLA
EAEEIREELV EQGYLRNRNK RGSKKKKETA PELDTYYSSD GITLLVGKNN KQNEYLTNKL
AASFETWLHT KDIPGSHVVI RSRTVSDQTL FEAAMLAAYF SKAQQGSKVP VDYTLIRHVK
KPSGAKPGYV TYDQQKTLFV TPDATLVAAL RNNSAAEQK
//
