ID A0A0C1R0G5_9CLOT Unreviewed; 582 AA.
AC A0A0C1R0G5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=U732_1555 {ECO:0000313|EMBL:KIE46887.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46887.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE46887.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46887.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(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:KIE46887.1}.
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DR EMBL; AYSO01000015; KIE46887.1; -; Genomic_DNA.
DR RefSeq; WP_039632626.1; NZ_AYSO01000015.1.
DR AlphaFoldDB; A0A0C1R0G5; -.
DR STRING; 29341.RSJ17_12470; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000031366; 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; 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:UP000031366};
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 462..559
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 582 AA; 67697 MW; 481B067935F7FEF1 CRC64;
MALDGIYLHS ILHELKVEFI NARVEKINQP EKDEITLTFK KSRKAQKLLI SSSSNYPRIQ
ITNNSKENPL KAPMFCMVLR KYLNTAVLVD IRQIESDRIV IVDFESTDEL GFNSIYSLIV
EIMGRHSNIS LVRQRDNIVM DSIKHITPDI NTYRILYSGV EYKYPPASTK LNAFDFTKEQ
FIDKVKENYI NKDFDKKFFT NIFTGVSPAL SSEMIYRLKE NNIEFTINNL EEIYKYILVF
FNYIETNTYS LGSYDMDGVL KDFHCITFKE LLNNGFNLNE YESPSRLIEN FYFEKDKIDR
LNARSYNLQK IVNNNLDRVG KKINILNETL ENCKEKQQLN LYGELLTANI YAIKKGDKFI
NVLNYYSEDN EYINIELDEH KTPSENIQNY FKKYNKLKKS EENAKIQIKL ALEEQEYLQS
VLSHIHNADN YTEIEDIKNE LVETGYIAFK KSHKGKKSKI SKPMHFISSD NVDIYIGKNN
MQNDYLTLKF ANKNDIWLHT KNIPGSHVII KNNGNITETT LLEAATLAAL YSKAKNSSNV
PVDYTEVKNV KKISGAKPGM VIYYTNKTLY VTPKQLNLKS ME
//
