ID A0A317L027_9BACI Unreviewed; 569 AA.
AC A0A317L027;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=DLJ74_10950 {ECO:0000313|EMBL:PWU68923.1};
OS Gracilibacillus dipsosauri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=178340 {ECO:0000313|EMBL:PWU68923.1, ECO:0000313|Proteomes:UP000245624};
RN [1] {ECO:0000313|EMBL:PWU68923.1, ECO:0000313|Proteomes:UP000245624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD1 {ECO:0000313|EMBL:PWU68923.1,
RC ECO:0000313|Proteomes:UP000245624};
RA Deutch C.E., Yang S.;
RT "Genomic analysis of Gracilibacillus dipsosauri DD1 reveals novel features
RT of a salt-tolerant amylase.";
RL Submitted (MAY-2018) 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:PWU68923.1}.
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DR EMBL; QGTD01000008; PWU68923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317L027; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000245624; 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 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:UP000245624};
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..540
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 431..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 294..321
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COILED 379..427
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 569 AA; 65774 MW; 6765997FACB79234 CRC64;
MVFDGVVTRA IAHELDRKLS SGRVLKIYQP TETELLFTIR QYGENKQLLL SAHPSYARIH
VTEDQYDNPR EPTMFCMMLR KHLGGSFIES VEQIENERIL HIHFQTKNEI GDLSVKKLVV
ELMGKHSNII LVDQDRQLIL DSIKHISGAQ NRHRSILPGN EYISPPSQNK VNPINVDEEM
FIRKLDFNAG KLDQQIVQTF MGISPLLANE IIYQARLGNL DDYKQAFKKI ISPIRENEYV
PQILHDNKSR FYVLDLESYS GEKKRFNSVS EMLDTYYSGK AERDRVKQKA GDLIRFLTNE
VKKNQRKLLK LDKTLEEAEH ADRYQRDGEL LTAHMHLVRK GDKQVEVTDY YDPNQVTRTI
KLNEHKTPSE NAQAFFKKYH KLKKSKQMVE EEKKKANEEI VYLEEIIEQI NSAREQDIEE
IREELQEQGY LKKKSGKGKP KKKTTKPEPE TFYASDGTII LVGKNNKQNE YLTNRIARKN
EIWLHTKDIP GSHVVIRSTD PSAGTLHEAA QLAANFSKSK NSSSVPVDYT LIRHVKKPNG
AKPGFVIYEN QKTLFVTPDK AFISKLKNK
//