ID A0A2B2CAJ6_9BACI Unreviewed; 569 AA.
AC A0A2B2CAJ6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=COJ96_09615 {ECO:0000313|EMBL:PFP29927.1};
OS Bacillus sp. AFS073361.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP29927.1, ECO:0000313|Proteomes:UP000223997};
RN [1] {ECO:0000313|EMBL:PFP29927.1, ECO:0000313|Proteomes:UP000223997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS073361 {ECO:0000313|EMBL:PFP29927.1,
RC ECO:0000313|Proteomes:UP000223997};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-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:PFP29927.1}.
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DR EMBL; NUZU01000013; PFP29927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B2CAJ6; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000223997; 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; NUCLEAR EXPORT MEDIATOR FACTOR 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:UP000223997};
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 452..541
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 569 AA; 65050 MW; 79F42FCC424A2F83 CRC64;
MSFDGLFTKA MVDELVRSLK GGRINKVHQP YKNEVILTIR ANGVNQKLLL SAHPSYARVQ
FTEESYDNPS EPPMFCMLLR KHIEGYILED LYQKETDRMI VLEIKGRNEI GDISYKQLII
EIMGRHSNIV LVDKSRNIIL DSIKHVSFAV NSHRAIMPGQ PYVFPPEQHK QDPFHCDQDD
LLRKIDYNAG KIDRQLVEQF AGISPLFAKE VIFQSGLANR ATVPGTFISM VKKVASGDIF
PSIISAGGKD AFYLFPLEHL KGEIKTYPTL SEMLDRFYFG KAERDRVKQQ GNDIERFIHN
EKEKNEKKID KLNVTLKEAE RAEQFQRYGE LLTANLYAAN KGMREIEVLD YYDESGGTII
IPLDPRKTPS ENAQKYFSKY QKAKNAVEIV IEQIEKAQVE VSYFDNLLQQ VQAASPKDIQ
EIREELVEGG YIRERQKKKL KKAQNAKPVL DHFKSSDGTD IIVGKNNKQN DYLTNKLAAR
DEIWLHTKDI PGSHVVIRSK EPSNETIREA AILASYFSKA RNSSSVPVDF TKVRFVKKPS
GAKPGFVIYD NQQTIYVTPD EELVLKLKK
//