ID A0A1J6W3Y5_9BACI Unreviewed; 567 AA.
AC A0A1J6W3Y5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=BHE18_06530 {ECO:0000313|EMBL:OIU72282.1};
OS Rossellomorea aquimaris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU72282.1, ECO:0000313|Proteomes:UP000182062};
RN [1] {ECO:0000313|EMBL:OIU72282.1, ECO:0000313|Proteomes:UP000182062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAMM {ECO:0000313|EMBL:OIU72282.1,
RC ECO:0000313|Proteomes:UP000182062};
RA Waghmode S.R., Suryavanshi M.V.;
RT "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT biosurfactant production capacities.";
RL Submitted (SEP-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:OIU72282.1}.
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DR EMBL; MINN01000074; OIU72282.1; -; Genomic_DNA.
DR RefSeq; WP_071617932.1; NZ_MINN01000074.1.
DR AlphaFoldDB; A0A1J6W3Y5; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000182062; 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:UP000182062};
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 451..540
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 379..413
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 567 AA; 64726 MW; 5A7F6893FF49706C CRC64;
MSFDGLFTRA MTKELKDGVM NGRINKIHQP YKNEIIMIVR ANGKNHKLLL SAHPSYSRVQ
ITQEDYENPS VPPMFCMLLR KHLEGYFIED IKQSGLDRMI VFEVKGRNEI GDVSYKQLII
EIMGRHSNII LVDKGRNMIL DSIKHISPSM NTHRTVLPGH EYVMPPKQDK RNPLEATSED
VLRALDFNAG KLDKQIVHSF AGISPLFAKE VTYHAGLGKQ SEIAQSFLDL VRKSKENQVS
PTLIMGEKEI FYWTSLEHVE GEKLAFSSLS ELLDRFFYQK AARDRVKQQG NDLERFIRNE
RDKNVNKIEK LKQTLKDAEQ ADRFQLLGEL LTSNLYAVER GMTEVSVANY YDEDGGSITI
PLNPQKSPSE NAQLYFSRYQ KAKNAIDIVN EQIEKAEEEI IYLERLLQQL ESASTKDVEE
IREELEEEGY LRARKQTKKK KSNGKPVLES YTSSDGIQIL VGKNNKQNDY LTNKSAGRDE
IWLHTKDIPG SHVVIKSNDP SEQTIKEAAN IAAYFSKARE SSSVPVDFTT VRQVKKPKGA
KPGFVIYEGQ QTVYVTPDMD LVRSLKD
//
