ID A0A101VNG2_9FIRM Unreviewed; 618 AA.
AC A0A101VNG2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=APF84_16285 {ECO:0000313|EMBL:KUO57947.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO57947.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO57947.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO57947.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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:KUO57947.1}.
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DR EMBL; LOEZ01000097; KUO57947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VNG2; -.
DR STRING; 1734398.APF84_16285; -.
DR Proteomes; UP000053404; 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; 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; 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 486..584
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 457..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 70563 MW; E12880E5F0BFE08E CRC64;
MALDSITLYH LLNELRPELI GTRIDRIVQP EKEEIHLILR SKKRSLLRLL LNAGSTSARI
HFTDEHKKNP TTAPMFCMIL RKHLESGKIL DIQQEGLERI VTIYVENYND RGDLQYYYLH
LEIMGKHSNL ILVDPQTNTI LDGLRRYSHL LSRYREVLPG RQYLAPPNQN KSDLVTDEEN
WMTLFLHHKL DTKVSDALVE IINGISPELA KELILRAGLD QDTILDNCGE IDFSRLYQAY
SSFILERKNA LLDPCVYFQS DLKRDIPSAF SFIPYLQYSD LSEQKVSTLN GAVSLYYTKK
INSNITEAKR GSLRKVVQSL YSHLNKKLGI HENTISKSEK GLRYQKLGEL LTANLYMLSP
GMSEITVDDY TDPEYKPMSI SLDPALSGID NAQRYYKLYN KSKVTIQKTQ PLLHAAQEEM
EYLQSLALSI EQAETNEELA EIHQELIDQG YISSKPANKS SYSKSISSKK KTSQKKKEPD
SESFPHVYLS QAGKTIIVGR NNRQNDKMTW REAKPSDMWL HVKKIPGSHV IVPLEENEEF
PDDATLLDAA ALAVYFSQAR GSSQVSVDYT HVKQIKKPKG AKPGMVVYEQ NWSLLITPKE
EDINRLLATE AVESKPIV
//
