ID F0IU80_STRSA Unreviewed; 549 AA.
AC F0IU80;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, 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=fbpA {ECO:0000313|EMBL:EGD38702.1};
GN Synonyms=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN ORFNames=HMPREF9384_1392 {ECO:0000313|EMBL:EGD38702.1};
OS Streptococcus sanguinis SK160.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888812 {ECO:0000313|EMBL:EGD38702.1, ECO:0000313|Proteomes:UP000004562};
RN [1] {ECO:0000313|EMBL:EGD38702.1, ECO:0000313|Proteomes:UP000004562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK160 {ECO:0000313|EMBL:EGD38702.1,
RC ECO:0000313|Proteomes:UP000004562};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-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:EGD38702.1}.
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DR EMBL; AEXZ01000008; EGD38702.1; -; Genomic_DNA.
DR RefSeq; WP_002912195.1; NZ_GL872447.1.
DR AlphaFoldDB; F0IU80; -.
DR PATRIC; fig|888812.3.peg.1375; -.
DR HOGENOM; CLU_022481_2_1_9; -.
DR Proteomes; UP000004562; 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..518
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 268..306
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 549 AA; 62629 MW; 0E26EA0FC716711B CRC64;
MSFDGFFLHH MTEELRRELL GGRIQKINQP FEQELVLQIR SNRQSHKLLL SAHSVFGRVQ
LTDTTFENPA VPNTFIMVMR KYLQGAVIEA IQQVENDRIL EISVSNKNEI GDSVAVTLVI
EIMGKHSNII LLDKASCKII EAIKHVGFSQ NSYRTILPGS TYVAPPQTGS LNPFTVGDEK
LFEILHTEDL EPKRLQQIFQ GLGRDTATEL SDRLAADKLK TFRAFFSSPT QPSLTEKSFS
ALLFSDSKAQ MSTLSELLDT FYKDKAERDR VNQQASELIR RVENELEKNR KKLGKQEEEL
LATENAEEFR QKGELLTTFL HQVPNDQDQV ELDNYYTGEK IIISLDKALT PNQNAQRYFK
RYQKLKEAVK HLTSLIEETR ATILYLESVE TALAQASLTE IAEIREELVQ TGFIRRRQRE
KIQKRQKPEK YLATDGQTII LVGRNNLQND ELTFKIAKKD ELWFHAKDIP GSHVVITGNL
QPSDEVKTDA AELAAYFSKA RLSNLVQVDM IETRKLNKPT GGKPGFVTYT GQKTLRVTPD
EEKIKSMKI
//
