ID A0A167C7P7_9BACL Unreviewed; 587 AA.
AC A0A167C7P7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=PNBC_15770 {ECO:0000313|EMBL:OAB72884.1};
OS Paenibacillus crassostreae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB72884.1, ECO:0000313|Proteomes:UP000077134};
RN [1] {ECO:0000313|EMBL:OAB72884.1, ECO:0000313|Proteomes:UP000077134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB72884.1,
RC ECO:0000313|Proteomes:UP000077134};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-2016) 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:OAB72884.1}.
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DR EMBL; LSFN01000032; OAB72884.1; -; Genomic_DNA.
DR RefSeq; WP_068659799.1; NZ_LSFN01000032.1.
DR AlphaFoldDB; A0A167C7P7; -.
DR STRING; 1763538.LPB68_04480; -.
DR KEGG; pcx:LPB68_04480; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000077134; 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; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000077134};
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 465..553
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 587 AA; 67131 MW; D4BBA4488DFCEA4B CRC64;
MALDGIVTRA IVQELQVYKG ARISKIYQPN NHDILFNLRS REGNSKLLLS VNPTYPRVHL
TDKSFLNPQE APMFCMLMRK HCESGTIEDI QQVGMERIIH ISIRQRDELG DVSLKKIIIE
LMGRHSNIIL MDASSGIILD GIHHVTPAIS SFRIVMPGVA YTEPPEQHKL NPLEVDQDSF
IKAYTETEQE PISWIVDSFS GLSPLIAQEV VYRANQEQDS VLSDENRISA TLLWRAFSQV
MVAVSKHDYQ PTIGANVKGK MVFSAISLSM LHSDVTTYNS ISECLEEYYG DKAERDTVKQ
KVSDLLRFLH NERAKNLKKL DHLQEDILEA GDADQYRIWG ELIFASLHMI NKGDKSVELT
NFYDDEQATM TVPLDPLLSP TENAKRYFKK YNKYKNSLVV IDQQLIKTHE EIRYMDDLLQ
QLSHASMNDI EEIREELIQQ QYLRDRSKKT RKKKVKKKND RPTLHVFTSS EGIEIYVGKN
NLQNEYVTNR LASPNDTWLH TKDIPGSHVV IRSDSFGEAT LEEAAQLAAY FSQAKESSSV
PVDSTLIRHV RKPSGSKPGF VIYDHQKTLF VTPDERRIKE LPSTIKN
//
