ID N2B798_9FIRM Unreviewed; 578 AA.
AC N2B798;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=C823_00668 {ECO:0000313|EMBL:EMZ36301.1};
OS Eubacterium plexicaudatum ASF492.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ36301.1, ECO:0000313|Proteomes:UP000012589};
RN [1] {ECO:0000313|EMBL:EMZ36301.1, ECO:0000313|Proteomes:UP000012589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF492 {ECO:0000313|EMBL:EMZ36301.1,
RC ECO:0000313|Proteomes:UP000012589};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
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:EMZ36301.1}.
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DR EMBL; AQFT01000023; EMZ36301.1; -; Genomic_DNA.
DR AlphaFoldDB; N2B798; -.
DR STRING; 1235802.C823_00668; -.
DR PATRIC; fig|1235802.3.peg.708; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000012589; 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; 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; IPR010979; Ribosomal_uS13-like_H2TH.
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.
DR SUPFAM; SSF46946; S13-like H2TH domain; 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:UP000012589};
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 458..550
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 578 AA; 66385 MW; F2B9AF361902BE69 CRC64;
MAFDGIVIAN LVTELNQTAL HARIYKIAQP EKDALLLTLK GACGQKRLFL SASASLPLIY
LTDTNKPSPL VAPNFCMLLR KHIANGRIVK IWQPDMERII HFEIEHLDDL GDVRKKTLTI
ELMGKHSNLI FTDEENRIID SIKHVSAQVS SVREVLPGRE YFIPTQGKNN PLSADETQFL
TQALSKPLSA AKAIYTSYTG ISPCIANEIC YRAGLDADAP TASFQEEEKT HLCNHFLWMM
QDIKNETFYP NIAVENGRPF EFSSVRLTQY RHLEQQEFTS ISEVLEHFYA ARDTYTRIRQ
KSVDLRKIVA TALERSHKKY QLQLKQLKDT EKRDKYKVYG ELINTYGYGL EEGAKSLEAL
NYYTNETIQI PLDPQLTPME NAKKYFEKYN KLKRTYEALS ELTIETKAEM EHLESISISL
DIALNEDDLV QIKQELIEYG YIRRKGHEKK QKIKSRPFHY RSSDGFDIYI GKNNYQNEEL
TFKLANGGDW WFHAKKMPGS HVIVKTNGQE LPDRTFEEAA MLAGYYSQGR DAQKLEIDYL
QRKNVKKPNG SAPGFVVYYT NYSMTIHPDI AGIELLAD
//
