ID A0A077JE77_9CYAN Unreviewed; 582 AA.
AC A0A077JE77;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ETSB_1572 {ECO:0000313|EMBL:BAP18299.1};
OS cyanobacterium endosymbiont of Epithemia turgida isolate EtSB Lake Yunoko.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1228987 {ECO:0000313|EMBL:BAP18299.1, ECO:0000313|Proteomes:UP000031625};
RN [1] {ECO:0000313|EMBL:BAP18299.1, ECO:0000313|Proteomes:UP000031625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ETSB Lake Yunoko {ECO:0000313|EMBL:BAP18299.1};
RX PubMed=25049384; DOI=10.1073/pnas.1405222111;
RA Nakayama T., Kamikawa R., Tanifuji G., Kashiyama Y., Ohkouchi N.,
RA Archibald J.M., Inagaki Y.;
RT "Complete genome of a nonphotosynthetic cyanobacterium in a diatom reveals
RT recent adaptations to an intracellular lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11407-11412(2014).
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; AP012549; BAP18299.1; -; Genomic_DNA.
DR RefSeq; WP_044107119.1; NZ_AP012549.1.
DR AlphaFoldDB; A0A077JE77; -.
DR STRING; 1228987.ETSB_1572; -.
DR KEGG; ceo:ETSB_1572; -.
DR HOGENOM; CLU_022481_1_0_3; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000031625; 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 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 458..558
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
SQ SEQUENCE 582 AA; 67651 MW; C21D945C7D38194E CRC64;
MQSFDVTTLT AICRELQISW IPSRLEQVYQ HDRHTISLAL RTLKKRSWLT ISWHSQAARL
CIGDFPPNTP DTFTFSDQLR HQLNGYTLTS LEMIAPWERV VDLQFAKRPG EPPVWHLFLE
IMGKYSNIIL TDAKQQIITV GHQVTANQSS VRTVKTGQPY EFPPILTGTL PKLEEPYERW
QERISLLPKA LKKQMLNSYC GLSPAVAHLM IQTANLDPKQ STDTLRLSDW NRLFDLWQTW
LTILVTADFK PGWTEEGYTV LGWGMVKPAS EIQTLINQYY RDQINYQTFQ QLRHQLLQKL
SSLLKKLRVK ASNFTQKLQQ SIEAGQYRQQ GDLLMAYLHL WQPGMKSICL KTFETEEKVE
INLNPEKNAV QNAQYLYKKH QKLKRACSIV EPLLAKVKGE IDYLEQVEES LNQLDIYDSP
QDLQTIQEIR EELIQQNYLK SPTQSSSSYL DESQPCQYIT PSGLEVWVGR NNRQNDRLTF
CTAGDYDLWF HTQESVGSHV LLRLEPGQKP NEVDLQCAAD WAAYYSRARF SKHVPIVYTE
PKYVYKPKGF KPGMVIYKRE KLLWGQPHKT QTYLKNQGET KN
//
