ID C8W090_DESAS Unreviewed; 595 AA.
AC C8W090;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=Dtox_2332 {ECO:0000313|EMBL:ACV63145.1};
OS Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV63145.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV63145.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV63145.1; -; Genomic_DNA.
DR RefSeq; WP_015757846.1; NC_013216.1.
DR AlphaFoldDB; C8W090; -.
DR STRING; 485916.Dtox_2332; -.
DR KEGG; dae:Dtox_2332; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_9; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000002217; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002217};
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 472..563
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 452..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 309..336
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 595 AA; 67364 MW; B3DE17D76EC34DA4 CRC64;
MPFDGLVLAA VKQELDVLTG GRIERIYQPS KDEVVLSIHR PGSKQRLVLS AHAYKTRIHT
TSHTKENPLN APLFCMVLRK HLEGGRICGF SQPGLDRVLI IDIEARDELG QMTSKHLICE
IMGKHSNIIL VDKERNTIID GIKRYSHNVS RYREVLPGRV YLPPPEQNKQ NPLLLNEDSF
RKYLLAGSLE AKVTNILQKS FDGLSPLICR EIIYRSGLDA DLILDHCGEH ELRLLWQSLA
AITENARKGV YYPVILFDRS GLPVDYAAFD ISHLEGLSKQ TSAMCSILDQ YYTAVYSLDL
VNGQKQALNQ IVNKEMKRLQ KKIDIYQQNL VDAEEAEIYK LYGELLTANL YRVSSKDTDV
ELENFYRPGE TVVVKLDSRL SPSENAQSYF KKYLKSKNTK LSAEELSKQA HSDLAYLESV
ETAIAQAVTT AEMAEIKLEL VEEGLLKETS RRINHKKVKK DKKDRNKPRP MSFCSTDGIQ
ILVGKNNKQN DYLTMKIASE KDIWLHTKDI PGSHVIIRTE GKEVSENTLL EAASLAAYFS
KARNLAKVPV DYTARKFVHK PNGAKPGYVI YDKQKTLLVA PNEELLENLT AQKPL
//
