ID A0A151AQ80_9CLOT Unreviewed; 580 AA.
AC A0A151AQ80;
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=CLCOL_04320 {ECO:0000313|EMBL:KYH29794.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH29794.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH29794.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH29794.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-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:KYH29794.1}.
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DR EMBL; LTBB01000002; KYH29794.1; -; Genomic_DNA.
DR RefSeq; WP_061857366.1; NZ_LTBB01000002.1.
DR AlphaFoldDB; A0A151AQ80; -.
DR STRING; 1121305.CLCOL_04320; -.
DR PATRIC; fig|1121305.3.peg.434; -.
DR Proteomes; UP000075374; 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:UP000075374};
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 459..555
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 580 AA; 67646 MW; DB2F6FF11248F7DB CRC64;
MALDGIFLFS LVQELKDVII GGKIDKINQP EKDEIILNIH KGRIKHKLLI SSSSTYPRIH
LTKLNKPNPM KAPMFCMVLR KYLTNAKIAD ISQIDSDRIV IIRFESTDEL GFNSVYLLIT
EIMGRHSNIT LVRERDNMIM DSIKHITSDI NTYRSIFPGV KYIYPPKSSK LNPFNFTYND
VYTYIKDNNI NFNKYMFSNI FTGISKTLST EIYFNLTLNS ISLEPKFLEK ILDYTKMIIN
RILNKDFKYT LYKSSEKDFI DFYCIELNSL NEHTKVPYSS PSDLIEDFYF TKDKFDRLKS
KSSDLQKIIV NNINRCIKKS KILNNTLKQC KDKEKYRLFG ELLTANIYAL KKGMKEIEVD
NYYSENYDKV KIYLDENKTP SENIQSYYKK YNKLKKSEES AYEQLKQNDD ELEYLQSVLT
NIQNVDNYTE IEEIKKELIE TGYIKFKKSY KSSKTKMSKP MHFVSTDGFH IYVGKNNIQN
DYLTLKFAHK NDIWLHTKNI PGSHVIIKSV GIVPETTLKE AANLAAYYSK SQNSSNVPVD
YTQVKNVKKP SGAKPGMVIY YTNQTIYITP EIPKLKQIID
//
