ID F4HNJ3_PYRSN Unreviewed; 650 AA.
AC F4HNJ3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Archaeal Rqc2 homolog aRqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=aRqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN OrderedLocusNames=PNA2_0051 {ECO:0000313|EMBL:AEC50969.1};
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC50969.1, ECO:0000313|Proteomes:UP000008293};
RN [1] {ECO:0000313|EMBL:AEC50969.1, ECO:0000313|Proteomes:UP000008293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:AEC50969.1,
RC ECO:0000313|Proteomes:UP000008293};
RX PubMed=21602357; DOI=10.1128/JB.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
CC -!- FUNCTION: Probably part of the ribosome quality control system (RQC).
CC May mediate the addition of alanine residues (Ala tailing) to
CC incompletely synthesized nascent chains from stalled ribosomes, leading
CC to their degradation. {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; CP002670; AEC50969.1; -; Genomic_DNA.
DR RefSeq; WP_013747528.1; NC_015474.1.
DR AlphaFoldDB; F4HNJ3; -.
DR STRING; 342949.PNA2_0051; -.
DR GeneID; 10553503; -.
DR KEGG; pyn:PNA2_0051; -.
DR PATRIC; fig|342949.8.peg.51; -.
DR eggNOG; arCOG01695; Archaea.
DR HOGENOM; CLU_003612_2_1_2; -.
DR OrthoDB; 10943at2157; -.
DR Proteomes; UP000008293; 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; 1.10.8.50; -; 1.
DR Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR HAMAP; MF_00844_A; RqcH_A; 1.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR InterPro; IPR043681; RqcH_archaeal.
DR NCBIfam; NF041120; RqcH_arch; 1.
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.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00844};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00844};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00844}.
FT DOMAIN 452..561
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 271..316
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COILED 399..443
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 650 AA; 76084 MW; 269212015FC1F354 CRC64;
MKEEMSSVDI RYIVQELKEE LKGARIDKVY HEGDEVRIKL HKTGEGRRDL IIEAGKRLHL
TTYIKESSSS PSSFAMLLRK YLSGAFVDEI EQHDFDRIVK IRVGKFTIIA ELFRRGNVIL
VDENNVILGA IRYEEFKDRS IKPKHEYKFP PARENPLEVS FDKFVELIKG EDTEIVRALA
RKLNMGGLYA EEILLRAEVN KKKRTSELSE EELKRIYEKM KEVFNAPKKP NIVYKDGRMV
DVVPIDLRWY DGYEKVYFDT FSKALDEYFG KLTIEKAREE KTKKLEEKKK QLIATLKRQE
NMIKGFKEEM RRNQEIADLI YANYQLVDNL LKELSKAVER LGWEELIRRV EEGKKKGNRI
AMMIKSINPQ ENSVTIEIED KKVRLYIDRD INENAEIYYE KAKKAKHKLE GAKKAYEELK
KKLEQVEKEI EEEEKKVQVK KIERRKKKWF EKFRWFISSE GFLVIGGKDA TTNEIVVRKY
MGENDIYCHA DIWGAPHVII KDGRRASEKT IFEACQFAVS MSRAWSEGLY SADAYWVYPE
QVKKQAPSGE FLPKGAFMVY GKRNWMHGIP LKLAVGIIRY EGEDLVMCGP VDAVRKHAKR
YVVIRPGDTK KSELVKRIKK IFEKWGYKVP EEDIMSVLPP GEGDIIEVVE
//
