ID A0A430AZK3_9ENTE Unreviewed; 564 AA.
AC A0A430AZK3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=CBF29_04470 {ECO:0000313|EMBL:RSU13513.1};
OS Vagococcus elongatus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=180344 {ECO:0000313|EMBL:RSU13513.1, ECO:0000313|Proteomes:UP000287605};
RN [1] {ECO:0000313|EMBL:RSU13513.1, ECO:0000313|Proteomes:UP000287605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 51432 {ECO:0000313|EMBL:RSU13513.1,
RC ECO:0000313|Proteomes:UP000287605};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:RSU13513.1}.
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DR EMBL; NGKA01000005; RSU13513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430AZK3; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000287605; 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}; Reference proteome {ECO:0000313|Proteomes:UP000287605};
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 444..537
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 293..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 564 AA; 64747 MW; 85DE5001DE6BE1DD CRC64;
MSFDGYFTHG MVQELNQILS GGRIAKIHQP FENEVILVIR NQRKNFKLLL SAHPSYARMQ
ITEVDYSNPD NPPNFCMMLR KYLDSAILEK IEQIENDRII HYSFSRRNEL GDLEDIVLVV
ELMGRHSAII LVNKETGKIL DCLKHVGPSQ NSYRLLLPGT NYIEPPKNEN QSDPFFVDEK
KLFHLLSTAE ELTPHYLQQH FQGLGFDTAN ELCFRLTQRS QEKLKIWRNF FTPQQELVPS
IYEKDAKEYF SSVPFTNLGH PAATFSSLSQ LLDVFYEGKA EKDRVRQQAG SLIKKIETEF
KKNQKKIKKL EKSLADTESA DTYQLRGELL TTYLYLINPG DHEVTVENYY DNNQPLKIAL
QPELSPSKNA QRYFKRYNKL KTGAKMIREQ LEKARQEENY LASVLSQLEI AAPSDIPVIR
EELIASGYVR ERLKGKKKAK ASKPQVFYSS DGDQILVGKN NLQNDQLTLR TAKKTDIWLH
AKNIPGSHVI IKNDAPSEQT IAEAANLAGY FSKYRLSSQV PIDYVPVKHV RKPSGAKPGY
VIYENQQTIY VTPDKHLVEK LKSS
//
