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Database: UniProt
Entry: A0A1H8AZK6_9BACL
LinkDB: A0A1H8AZK6_9BACL
Original site: A0A1H8AZK6_9BACL 
ID   A0A1H8AZK6_9BACL        Unreviewed;       617 AA.
AC   A0A1H8AZK6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=SAMN05518847_101725 {ECO:0000313|EMBL:SEM76165.1};
OS   Paenibacillus sp. OV219.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1884377 {ECO:0000313|EMBL:SEM76165.1, ECO:0000313|Proteomes:UP000199330};
RN   [1] {ECO:0000313|EMBL:SEM76165.1, ECO:0000313|Proteomes:UP000199330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV219 {ECO:0000313|EMBL:SEM76165.1,
RC   ECO:0000313|Proteomes:UP000199330};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOCJ01000001; SEM76165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8AZK6; -.
DR   STRING; 1884377.SAMN05518847_101725; -.
DR   OrthoDB; 9766163at2; -.
DR   Proteomes; UP000199330; 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; 2.
PE   3: Inferred from homology;
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          496..585
FT                   /note="NFACT RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05670"
SQ   SEQUENCE   617 AA;  68831 MW;  1BD06E2C0876B6C1 CRC64;
     MALDGIVTRA ITHELQACIG ARIYKIHQPG PHDLVLQIRG GGVQGKLLIS ANPTYPRIHF
     TEQSFINPME APMFCMLLRK HCEGAVIEAV RQVGNERIIH LDVRQRDELG DMSFKRIIIE
     LMGKHSNIIL VDAATEMIHD GIHHVTPMIS SYRVIMPGTT YVAPPEQGKD DPLAIADEAT
     FSVALRQTAD ALINPPIPDE DSIHFGSVPK AADPTSITLN QLLVGAFSGL SPLLAKEIIH
     RSTSADESSP LLNGADHINV NAARVWPAFR DMMEQFRSNR YEAQMIAASS SSKPSFSVTE
     LTHLEGAVVT FETVSLCLEA FYGDKAQRDT VKQRANDLIK FLQNERNKNV KKQGKLAETL
     QEAKDADKFR SLGELLTMSL HTIQRGDDFV ETIDYYDEEQ PIIKIALDPL LTPSQNAQRY
     FKRYTKYRNS LTVVAEQMER TSEEMAYLES LLQQLESASL SDIDEIRDEL VEQGYLRSRE
     KRGAKKRKPK QPALLCYTSS EGVPIFVGKN NTQNDFLTNK SSAPNDTWLH TKDIPGSHVV
     IRGTSFGDET LEEAAMLAAH FSQAKSSSSV PVDYTLIRYV KKPSGAKPGY VIYDNQKTLF
     ITPDEPRIKG LPSVIKQ
//
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