ID A0A1A5YH20_9BACL Unreviewed; 583 AA.
AC A0A1A5YH20;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=A7K91_04690 {ECO:0000313|EMBL:OBR64882.1};
OS Paenibacillus oryzae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1844972 {ECO:0000313|EMBL:OBR64882.1, ECO:0000313|Proteomes:UP000092024};
RN [1] {ECO:0000313|EMBL:OBR64882.1, ECO:0000313|Proteomes:UP000092024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1DrF-4 {ECO:0000313|EMBL:OBR64882.1,
RC ECO:0000313|Proteomes:UP000092024};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-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:OBR64882.1}.
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DR EMBL; LYPA01000064; OBR64882.1; -; Genomic_DNA.
DR RefSeq; WP_068684019.1; NZ_LYPA01000064.1.
DR AlphaFoldDB; A0A1A5YH20; -.
DR STRING; 1844972.A7K91_04690; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000092024; 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:UP000092024};
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 462..551
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 390..424
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 583 AA; 64655 MW; DAD0EBDE8849EDB6 CRC64;
MSLDGIVTAA IAHELQRCVG ARIHKIHQPT SHELVLSIRG GGFGGKLLLS ANPTYPRVHF
TNAAYSNPLE APMFCMLLRK HCEGGVITAV SQVGRERILH IGVRHRDELG DTSHKTIIVE
IMGRHSNIIL TDTGSGMIHD GIHHVTPAIS SHRIILPGSL YTPPPHQGKT DPLTVVSEAA
FLECLTAQED SDAPMHKALV DAFSGISPLL AKEMVHRASK GGNQPEPSSL WSSFNDLMEV
ARNHVFTPVI ATQRSSGKAF FSITELTHIE DAEVQSFPSA SECLEDFYGD KAERDTVKQR
AADLIRFVQN ERAKNGLKIK KLQDTLQEAK DAEKYRVLGE LLTAYMHNFN RGDSEITVIN
FYDENGAEVT IPLDPQLSPS ENAQKYFRRY TKHRNSVSIV KEQMEMAENE ITYFESLLQQ
LENASLGDIE EIRDELVQQG YMRERHKRGP KRKKTGKPSL LCYTSSEGIS VYVGKNNTQN
EYLTNRLAAA SDTWLHTKDI PGSHVVIRGT GFGDATLEEA AMLAAHYSQA KASSLVPVDY
TQIRHVRKPS GAKPGFVIYD NQKTLFITPD EGRIKGLASE IKA
//
