ID A0A1G6L912_9BACI Unreviewed; 568 AA.
AC A0A1G6L912;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN05421737_10823 {ECO:0000313|EMBL:SDC39026.1};
OS Shouchella lonarensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1464122 {ECO:0000313|EMBL:SDC39026.1, ECO:0000313|Proteomes:UP000242662};
RN [1] {ECO:0000313|Proteomes:UP000242662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25nlg {ECO:0000313|Proteomes:UP000242662};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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; FMYM01000008; SDC39026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6L912; -.
DR STRING; 1464122.SAMN05421737_10823; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000242662; 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:UP000242662};
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 427..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64920 MW; 67F723A51FCBEACF CRC64;
MSFDGFVTRA VTHELQSLLG GRMNKVFQPS KTELVCAIRA HGKNHFLLLS ANATFARVHM
TKEKYENPNE PPMFCMLLRK HLEGGIIRAI TQYQTDRIIT FTIEKRDELG DTKTKQLIVE
IMGRHSNIIL VDPTTNMVID SIKHVRFDQS RYRTVGPGQL YKHPPAQEKQ DVLTVTEKDV
LKSLDFNAGK LSAQLVHSFH GLSPLVANEI VHRAGLANQT TLPKAFFDVI EPLKTHCYTP
EIVGGKKAFF SVVHLAHKNG DRTHFSTTND MLDRYYYKKA ERDRVKQQAF DVERLLKQTY
EKNKRKQAKL TETLTRTNEA NLHQHYGELL TAHLHLVKKG ASSIDVVDYY DPEGRCVTIA
LDPTKTAAEN AQAYFKRYQK AKTARLEVTD QIQKTRIELD YLANLLQQLD VASPKDIEEI
REELRDGGYM RSRSSHKKKK KSQSSHPQLE SYVSSTGVPF FVGKNNRQND YLTRHFSRQD
EIWLHTKDIP GAHVLIRSTA PDEATLKEAA IVAAYFSKAR HSASVPVDYT KIRYVKKPSG
AKPGYVTYEK QTTLFVTPEE EKVLQLRR
//
