ID A0A398BH03_9BACI Unreviewed; 571 AA.
AC A0A398BH03;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
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=D1970_03640 {ECO:0000313|EMBL:RID87938.1};
OS Mesobacillus zeae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1917180 {ECO:0000313|EMBL:RID87938.1, ECO:0000313|Proteomes:UP000265816};
RN [1] {ECO:0000313|EMBL:RID87938.1, ECO:0000313|Proteomes:UP000265816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-247 {ECO:0000313|EMBL:RID87938.1,
RC ECO:0000313|Proteomes:UP000265816};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT spacecraft and associated surfaces.";
RL Submitted (AUG-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:RID87938.1}.
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DR EMBL; QWVT01000008; RID87938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A398BH03; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000265816; 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; 3.40.970.40; fibrinogen binding protein from staphylococcus aureus domain like; 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:UP000265816};
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 453..541
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 380..407
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 571 AA; 64785 MW; 803C0F6E1B9EF86B CRC64;
MSFDGLFTRA VTNQLSSLLK GGRINKIHQP YKNEIIMTVR AGGVNHKLLL SAHPSYARVQ
LANGQYDNPD TPPMFCMLLR KHLEGNIIEN IRQYGLDRII IFEIKGRNEL GDLSYKQLIV
EIMGRHSNIV LVDKERNMIL DSIKHVSFAV NTHRAIQPGQ EYILPPAQDK INPFEASQED
VLRKVDFNAG KIDQQLVANF AGLSPLVSRE IVYRAGLANR GTIPNAFTEM MRKLESHEYE
PAFTSSQGKE SFYLVPLTHM EGETRTFSSL GALLDRFYFG KAERDRVKQQ GNDLEKFIVN
ERAKNENKIK KLEQTLSEAR NAGQLQLFGE LLTANLHLAK KGMKALEVIN YYDENGASIT
IPLDPLKTPS ENAQKYFTKY QKAKNAVKIV EEQIEKAKEE AAYFEMLYQQ VESASPKDIA
EIREELAEGG YIRQRQKRGN KRGQPSKITL EKYISSDGTE ILVGKNNKQN DYLTNKAAAR
DDIWLHTKDI PGSHVVIRNS EPSEKTILEA SCLAAYYSKA RQSSSVPVDY TRIRYVKKPA
GSKPGFVIYD NQQTVYITPD EEKVLTMKTD R
//