ID S0EXN2_CHTCT Unreviewed; 575 AA.
AC S0EXN2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=CCALI_02453 {ECO:0000313|EMBL:CCW36252.1};
OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC Chthonomonadaceae; Chthonomonas.
OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW36252.1, ECO:0000313|Proteomes:UP000014227};
RN [1] {ECO:0000313|Proteomes:UP000014227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23976 / ICMP 18418 / T49
RC {ECO:0000313|Proteomes:UP000014227};
RA Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT from the Armatimonadetes phylum (formally candidate division OP10).";
RL Submitted (MAR-2013) 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; HF951689; CCW36252.1; -; Genomic_DNA.
DR RefSeq; WP_016483764.1; NC_021487.1.
DR AlphaFoldDB; S0EXN2; -.
DR STRING; 454171.CP488_01636; -.
DR KEGG; ccz:CCALI_02453; -.
DR PATRIC; fig|1303518.3.peg.2550; -.
DR eggNOG; COG1293; Bacteria.
DR HOGENOM; CLU_022481_2_1_0; -.
DR InParanoid; S0EXN2; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000014227; Chromosome.
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; 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:UP000014227};
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 461..551
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 389..423
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 575 AA; 65191 MW; 0EE52305A11B0242 CRC64;
MKTFDSLTLH ACIDELNSAL VGGQIQEVRQ PDEREILLGI RNRGANHLLL LSAHPQFARA
HLTLKRPPNP PTPPTFCMAL RKHVEGLHLL KVRQLDFDRV VFLEIGLPAN GLPSATLIGE
FMGKHSNLVL VTPEGTILDA VHRVSHRINR VRQLLPGQPY QLPPPQPDRV NPFTPHAIDK
ILRELESIPS NDVESLASAL MQIYAGISPF LAREIAMRAL HYEDRAEGLR VAWASLFDAA
ARQDYQPTLF LSDAGTPVGA YPFPSVQWPD HQQKPMESLQ LALDQAYTFL VEQSERESLR
ANLRARIERA IATWQKRHEG AKKALEEAEK ADFYRQNGEL ILANLWRIQP NMSHVIVEDF
YDPDLKPRTI PLDPHRTPQE NAESWFQRYR KAKVAREQEA QRLAQAESAL RRLEAALVEL
TQLGTCEAIR ELGEELTLQG LLPKESSERG RTEEPEFEGH KIRRYFSPEG YEILVGETAT
ANDYLTTRVA HPNDIWLHVR AGVSAHVIIR THGQPERVPR SVIEFAARLC AQHSKQKHAA
LVPVDYTLRK YVRRPRGAPP GAADYWNERT IEVTP
//
