ID A0A1M7RRC5_FERGO Unreviewed; 557 AA.
AC A0A1M7RRC5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN02745226_00021 {ECO:0000313|EMBL:SHN48618.1};
OS Fervidobacterium gondwanense DSM 13020.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=1121883 {ECO:0000313|EMBL:SHN48618.1, ECO:0000313|Proteomes:UP000184207};
RN [1] {ECO:0000313|EMBL:SHN48618.1, ECO:0000313|Proteomes:UP000184207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13020 {ECO:0000313|EMBL:SHN48618.1,
RC ECO:0000313|Proteomes:UP000184207};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; FRDJ01000001; SHN48618.1; -; Genomic_DNA.
DR RefSeq; WP_072757096.1; NZ_FRDJ01000001.1.
DR AlphaFoldDB; A0A1M7RRC5; -.
DR STRING; 1121883.SAMN02745226_00021; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000184207; 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; 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 451..544
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 293..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COILED 376..420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 557 AA; 64772 MW; D7E8949193F35803 CRC64;
MAFDGFVMRI TAGKIEEHIN GLNLRNIYLE DKVLYFSFDA GDLKISLNPN FAHISFTEHI
VKEPEKQTFV DFLRSRIRGA KVSKFSSIGY DRTVVLELKK TDEIGQKHEY KLYIDIMGKH
SNVILVENGV ILDAYKRIET RFRNINPGEK FVLFASNKMN IEEVTADSLS VALEHFPKQK
AISEFIYSTI QGFSRLTAEE LLFRADLDDM ALSQISDEHL NALLEAIASI RRELSENQLY
VYYENDMPID ISVFRLHKYT DFKRCENPVE CVNEYFEFVE KKDKLTQKKN QLLSIVNSKI
EAYEKLIDSI EKEVEECKNA EKYRKFGELL KAYSYQIGHG LEEVTLTDWE TNEEVRIPLE
KHLSAIENSV KYFKMYNKLK KKLEGLSERK EILERELSYL RQLQNTIENA ETLDDLLDIE
EEMVEGELIK KHKGKKNTKV VTHSEPRRYT FNGFTIFVGR NNRQNDELVR KASEHDLWLH
VQGMPGAHVV VKTNGKPIDD ETLQYAAKLA AYYSKGKYST KVPVDYTQVK YVKKPRGFKP
GLVLYSNFKT LFVTPTE
//
