ID A0A143Y6T4_9LACT Unreviewed; 567 AA.
AC A0A143Y6T4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=TR210_89 {ECO:0000313|EMBL:CZQ80865.1};
OS Trichococcus ilyis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ80865.1, ECO:0000313|Proteomes:UP000076878};
RN [1] {ECO:0000313|EMBL:CZQ80865.1, ECO:0000313|Proteomes:UP000076878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ80865.1};
RA Wen L., He K., Yang H.;
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}.
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DR EMBL; FJNB01000001; CZQ80865.1; -; Genomic_DNA.
DR RefSeq; WP_068620453.1; NZ_FNYT01000001.1.
DR AlphaFoldDB; A0A143Y6T4; -.
DR STRING; 640938.TR210_89; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000076878; 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 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 446..539
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 432..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 64318 MW; 5665ADA6479DA882 CRC64;
MSFDGVFTRA MVSELNRELE NGRIGKVHQP FQHEIILTVR ANRKNKRVLL SAHPSYARLQ
VIEDSLSNPD SAPNFCMVLR KKLEGAIIEE IRQLGNDRIV IFSFRNFDEL GDQQQLELIV
ELMGRHSNIF LIDKASRIII DCLKHVPFYQ NSFRPLHPGV AYQLPPHQDR SDLFALEPAE
IEKLVAQFDP EVPLRNALQQ TFQGLGSDSA QEIAHYAADD GLAPAAAIQL FKERVASVSP
TLTNESERKQ HFTPFPYTSL PGDKQAFATL SQLLDAYYAE KATRDRIHQV ASDLLQIVST
ELKKNQLKLQ KLDQTLLETE KADVFRIKGE LLTAYLHQFE KGQQEVVLNN FYDDEKPVAI
SLNPSLTPSQ NAQKYFSKYQ KLTTAVNHVN EQIRQTHAEN EYLETIETQI QLSDPQDLEE
IKDELSESGY LKRKQSLKNK KKKTSKPHRF RSADGTSILV GKNNLQNDQL TLKTAKKTDI
WLHAKNIPGS HVIIESNNPS EETVFEAANI AAYYSKFQNS ANVPVDYVAV KQIRKPNGAK
PGFVIYEGQK TVYVTPDKDL IKALKAD
//
