ID A0A0F3RTI2_9LACO Unreviewed; 571 AA.
AC A0A0F3RTI2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-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=VC81_02285 {ECO:0000313|EMBL:KJW13318.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW13318.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW13318.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW13318.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-2015) 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:KJW13318.1}.
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DR EMBL; JZCR01000006; KJW13318.1; -; Genomic_DNA.
DR RefSeq; WP_045806545.1; NZ_JZCR01000006.1.
DR AlphaFoldDB; A0A0F3RTI2; -.
DR STRING; 216463.VC81_02285; -.
DR PATRIC; fig|216463.3.peg.2268; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000033491; 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; 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};
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 452..547
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 431..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 571 AA; 64105 MW; 2CCCBE713EBC8597 CRC64;
MSFDGSFTHA MVHELSQTVA TGRVSKINQP YANEVVLTIR ANGHNHPILL SANPTYARIQ
ETQIPYVNPP VPTNFTMILR KYLQGAILKD VTQAANDRVV HLHFTARNEL GDQQELHLII
EIMARHSNVI LVDQQSGKIL DAIKHVGSDQ NRYRLLLPGA LYITPPKQDL DDPFQGPRED
LTDTIRDYPN RDVLAHALQQ QYQGLGKDTA SALAAALHQP GDAAHHFQAF FAGFDEPQPT
LTISPKGKTS FTAFPYPTDG KTQPATTLSG LLDTYYQDKA ERDRVQQQGS VLIHVVRNEL
KKNRNKLKKL QRTLADTENA DEYRIKGEVL TTYLYQLTRG DTSVTLPNFY DNEKPLKIAL
SNQLSPNQNA QKYFKRYQKA KNAVSYVTEQ IQQTQANVDY FDNIMAQIEL AAPKDLIDIK
LELQEGGYLR DHDHQKKAKK QRKQKISQPD RFTASDGTLI SVGKNNLQND KLTLHTAKRT
DIWLHVKDMP GSHVIVHAAD PSEQTILEAA NLAAYFSKAR ESSTVPVDYV PVKRIHKPNG
AKPGFVIFTG QKTVFVTPES ALVDQLAANN R
//
