ID F5VVD7_STROR Unreviewed; 551 AA.
AC F5VVD7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=HMPREF9968_1853 {ECO:0000313|EMBL:EGL88525.1};
OS Streptococcus oralis SK255.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1005704 {ECO:0000313|EMBL:EGL88525.1, ECO:0000313|Proteomes:UP000003695};
RN [1] {ECO:0000313|EMBL:EGL88525.1, ECO:0000313|Proteomes:UP000003695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK255 {ECO:0000313|EMBL:EGL88525.1,
RC ECO:0000313|Proteomes:UP000003695};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (APR-2011) 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:EGL88525.1}.
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DR EMBL; AFNM01000033; EGL88525.1; -; Genomic_DNA.
DR AlphaFoldDB; F5VVD7; -.
DR PATRIC; fig|1005704.3.peg.1182; -.
DR eggNOG; COG1293; Bacteria.
DR Proteomes; UP000003695; 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; 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 434..519
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 269..304
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 551 AA; 63357 MW; 96F9853B656F4742 CRC64;
MSFDGFFLHH MVEELRSELV NGRIQKINQP FEQELVLQIR SNRQSHRLLL SAHPVFGRIQ
LTQTTFENPA QPSTFIMVLR KYLQGAVIES IEQVENDRIV EITVSNKNEI GDHIQATLII
EIMGKHSNIL LVDKSSHKIL EVIKHVGFSQ NSYRTLLPGS TYIAPPSTES LNPFTVKDEK
LFEILQTQEL TAKNLQSLFQ GLGRDTANEL ERLLVSDKLS TFRNFFDQKT KPYLTETSFS
PVPFANRVGD PFSSLSDLLD TYYKDKAERD RVKQQASELI RRVENELQKN RHKLKKQEKE
LLATDNAEEF RQKGELLTTF LHQVPNDQDQ VTLVNYYTNQ PITIALDKAL TPSQNAQRYF
KRYQKLKEAV KYLTELIEET KSTILYLESV ETVLNQAGLE EIAEIREELI QTGFIRRRQR
EKIQKRKKPE QYLASDGKTI IYVGRNNLQN EELTFKMARK EELWFHAKDI PGSHVVISGN
LNPSDEVKTD AAELAAYFSK GRLSNLVQVD MIEVKKLNKP TGGKPGFVTY TGQKTLRVTP
DPEKIASMKK S
//
