ID A0A369XX94_9FUSO Unreviewed; 536 AA.
AC A0A369XX94;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=DV867_11535 {ECO:0000313|EMBL:RDE60168.1};
OS Psychrilyobacter sp. S5.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Psychrilyobacter.
OX NCBI_TaxID=2283384 {ECO:0000313|EMBL:RDE60168.1, ECO:0000313|Proteomes:UP000253914};
RN [1] {ECO:0000313|EMBL:RDE60168.1, ECO:0000313|Proteomes:UP000253914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5 {ECO:0000313|EMBL:RDE60168.1,
RC ECO:0000313|Proteomes:UP000253914};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Psychrilyobacter sp. strain S5.";
RL Submitted (JUL-2018) 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:RDE60168.1}.
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DR EMBL; QQOU01000021; RDE60168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369XX94; -.
DR Proteomes; UP000253914; 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; 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:UP000253914};
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 430..517
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 536 AA; 61631 MW; 5492D501DDAA8849 CRC64;
MLYIDGISLS KLKDELDETL KGRKVTKIFQ YSPLSLSVFL GKLNLYVSAT PNLPICYIAT
KKEVAPDKPM SFSLSLRKYL VGAILTGVEQ YKNDRILLLS FEKVNELGVK QKVKLIVEIM
GKHSNIILVD DDWMILDLLK KFSIEENKLR LLMGGARYQF PIITEKTSPE DVSKEEFDNY
LAENTLIQNI DGMGKLTAKY MTDYSKFYEL INESASPTLY KENGIIKYGT IVNLPLAGYE
EVKFESINGM IDTYILETLN SEQFNNQKRT LAKVAEKELK KNKKTIKNIN RDIEKYSTYE
KYKKIGDILA ANLYSLKGYE KSVTLYDFYE NCNIEIALNP QKSSNENLDN YYNLYNKHKR
GYQHSVERLE TIKSEIIYLE SILSFINHAQ DKKTLEGIEE ELIANKYLKK IIKTKKKKKI
AKITPPTAEI DGFTVYYGRN NIENEYVTFK IGDRHDLWFH AKDVPGSHLI VKTNGEEISE
ETLYKVGELA SQHSKVGQGE TIRIDYCLKK YVKKIKGAKP GLVIYSNEKS VFVKKG
//
