ID A0A1M4S4Q8_9FIRM Unreviewed; 581 AA.
AC A0A1M4S4Q8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN02746064_00051 {ECO:0000313|EMBL:SHE27202.1};
OS Alkalibacter saccharofermentans DSM 14828.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=1120975 {ECO:0000313|EMBL:SHE27202.1, ECO:0000313|Proteomes:UP000184251};
RN [1] {ECO:0000313|EMBL:SHE27202.1, ECO:0000313|Proteomes:UP000184251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14828 {ECO:0000313|EMBL:SHE27202.1,
RC ECO:0000313|Proteomes:UP000184251};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQTU01000001; SHE27202.1; -; Genomic_DNA.
DR RefSeq; WP_073269062.1; NZ_FQTU01000001.1.
DR AlphaFoldDB; A0A1M4S4Q8; -.
DR STRING; 1120975.SAMN02746064_00051; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000184251; 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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000184251};
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..549
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 581 AA; 66179 MW; D7B9579D3F8122F2 CRC64;
MPLDGFAVHH LQHELSKALV GGKINKIYQP EKDELILNIT NKKSKYELLI SANNNHPRIH
FITATKENPQ SPPMFCMLLR KKLSNGIITA VRQIEFDRIV ELTVTSKDEL FDFSEKKLLV
EIMGRHSNII LLENGIITDS IKRINRFVSS FREVLPGRSY VAPPMNKRDF SSLDDEEFKK
LLLSAPDKKI DKAVMDSFQG ISKLIAREVC NRLDINTEFA ASDIPESLIC KIKNILTVLK
GSPKYCIYKD PDSKEIKDFS TVAITLFDGM EASCYPDVSQ MLEDYYRLKD SHQRIKERTA
SISQIIGNKL ERNYNKLNKL TEDRKNAEDA DKFRLYADML YANLYALKSP VKEVVLDNFT
DGTKITIPLD IRKTPGENAK KYYDRYNKAK RALSYIDEQT QKTKEEIYYL ESILDSISKC
DSIGELREIK DELAENGLIK SYKKSKKNQQ QSLSAPDVFR SSEGYDILVG KNNKQNDMLT
TKTASKDDLW FHVKDQPGSH VVVRCEGKTP GEATIFEAAM LAAYFSKAKM SSNAAVDYTL
IKFVKKPKSA KAGMVIYTDN KTVYVTPSEK KVTDLKNNMT S
//
