ID A0A139C6M2_9FIRM Unreviewed; 589 AA.
AC A0A139C6M2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=AWU54_2364 {ECO:0000313|EMBL:KXS36887.1};
OS Candidatus Frackibacter sp. T328-2.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Frackibacter.
OX NCBI_TaxID=1785949 {ECO:0000313|EMBL:KXS36887.1, ECO:0000313|Proteomes:UP000070439};
RN [1] {ECO:0000313|EMBL:KXS36887.1, ECO:0000313|Proteomes:UP000070439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T328-2 {ECO:0000313|EMBL:KXS36887.1};
RA Wolfe R., Daly R., Wrighton K.;
RT "Candidatus Frackibacter-2 T328 Annotated.";
RL Submitted (JAN-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}.
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:KXS36887.1}.
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DR EMBL; LSBO01000194; KXS36887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139C6M2; -.
DR PATRIC; fig|1785949.3.peg.423; -.
DR Proteomes; UP000070439; 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; 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};
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 469..560
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 589 AA; 68827 MW; 50018DE6F5772656 CRC64;
MALDGLVLNA IKYELEERLI GGRLDKIYQP EDELLTLRFR QPGENIELLL SAHPQDPRVH
ITEEDRENPL RPPTFCMLLR KHLEHGRLRK IEQPEFERII KFYIDSKNND GEIETKILLI
EIMGRHSNII LLQEDGQILD SIKRVTSNMS RHREILPGKE YQQPPKQDKI NPLIITKEEF
LQRITDNIDK SSYRAIMENI RGVSPLVAKE LAYRAGIGRE EKIRKINSLA LDELWTEFQK
VIKLIEDNNF YPNLVFDKDG NLKEYSVIDL TQFPNLKKKE FASTNQLLDY YFTTQIKSRK
LNSLKGSLTK ITSDNIEKAM KKYRRVKGQL KGARNAEKYR IKGELIKANI HQIEPGQDKL
KTINYYSEDQ EEITIQLDQD LSPVENSQKY FQKYNKAKRS VDYLENELRK AKNEINYLKQ
VEVSMNQAED VTDLEEIKEE LADEGYIKKQ KSNKDKRRNQ KKKSEPLKFK SSDGFDIRVG
RNNRQNDKLT KYVANNHDLW LHVKDLPGSH VIIRNHTRDE IPENTIEEAA HLAAYYSKGK
ESSNVPVDYT LVKNVNKPKG AKPGMVYYEE QQTLFVTPDE ELIEELAQN
//
