ID A0A0F2E0X0_STROR Unreviewed; 551 AA.
AC A0A0F2E0X0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=flpA {ECO:0000313|EMBL:KJQ76862.1};
GN Synonyms=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN ORFNames=TZ95_00709 {ECO:0000313|EMBL:KJQ76862.1};
OS Streptococcus oralis subsp. tigurinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1077464 {ECO:0000313|EMBL:KJQ76862.1, ECO:0000313|Proteomes:UP000033377};
RN [1] {ECO:0000313|EMBL:KJQ76862.1, ECO:0000313|Proteomes:UP000033377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC5873 {ECO:0000313|EMBL:KJQ76862.1,
RC ECO:0000313|Proteomes:UP000033377};
RA Haase E.M.;
RT "Evolution of amylase-binding proteins of oral streptococcal species.";
RL Submitted (FEB-2015) 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:KJQ76862.1}.
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DR EMBL; JYGU01000006; KJQ76862.1; -; Genomic_DNA.
DR RefSeq; WP_045616973.1; NZ_JYGU01000006.1.
DR AlphaFoldDB; A0A0F2E0X0; -.
DR PATRIC; fig|28037.217.peg.681; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000033377; 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..307
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 551 AA; 63368 MW; B301116604A689F1 CRC64;
MSFDGFFLHH MIEELRRELV NGRIQKINQP FEQELVLQIR SNHQSHHLLL SAHPVFGRIQ
LTQTTFENPA QPSTFIMVLR KYLQGAVIES IEQIENDRIV EITVSNKNEI GDHIQATLII
EIMGKHSNIL LVDKSSHKIL EVIKHVGFSQ NSYRTLLPGS SYIAPPSTES LNPFTIKDEK
LFEILQTQEL TAKNLQNLFQ GLGRDTANEL ESLLVSDKLS TFRNFFSQET KPCLTETSFS
PVPFANRIGE PFASLSDLLD TYYKDKAERD RVKQQASELI RRVENELQKN RHKLKKQEKE
LEATENAEEF RQKGELLTTF LHQVPNDQDQ VTLDNYYTNQ PITITLDKAL TPSQNAQRYF
KRYQKLKEAV KYLTELIEET KATILYLESV ETVLNQAGLE EIAEIREELI QTGFIRRRQR
EKIHKRKKPE QYLASDGKTI IYVGRNNLQN EELTFKMARK EELWFHAKDI PGSHVVISGN
LNPSDEVKTD AAELAAYFSK GRLSNLVQVD MIEVKKLNKP TGGKPGFVTY TGQKTLRVTP
DPEKIASMKK S
//