ID A0A1I0MDR3_9EURY Unreviewed; 726 AA.
AC A0A1I0MDR3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=SAMN05216285_0817 {ECO:0000313|EMBL:SEV86268.1};
OS Natrinema salifodinae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEV86268.1, ECO:0000313|Proteomes:UP000183275};
RN [1] {ECO:0000313|Proteomes:UP000183275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOIS01000001; SEV86268.1; -; Genomic_DNA.
DR RefSeq; WP_049989326.1; NZ_JROF01000005.1.
DR AlphaFoldDB; A0A1I0MDR3; -.
DR STRING; 1202768.SAMN05216285_0817; -.
DR eggNOG; arCOG01695; Archaea.
DR OrthoDB; 10943at2157; -.
DR Proteomes; UP000183275; 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_A; RqcH_A; 1.
DR InterPro; IPR008532; NFACT_RNA-bd.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00844};
KW Reference proteome {ECO:0000313|Proteomes:UP000183275};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00844};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00844}.
FT DOMAIN 516..633
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 246..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 328..362
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COMPBIAS 253..271
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 81773 MW; 8BAA751347CDE6B7 CRC64;
MDPKRELTSV DLAALVGELG AYEGAKVDKA YLYGDDLVRL KMRDFDRGRV ELIFEVGEVK
RAHTVAPERV PDAPGRPPQF AMMLRNRLSG ADFVGVEQYE FDRILEFTFE RDDGITRIIV
ELFGQGNVAV TDGEYEVIDC LETVRLKSRT VVPGSRYEFP ESRTNPLTVS REAFDREMDD
SDTDVVRTLA TQLNFGGLYA EEICTRAGVE KAMDIDDADE AVYDRVYQAI ERLALDIRNG
NFDPRLYLES DDEGSDGGDE AEGDDDTDAD EGRVVDVTPF PLEERSDLAA DPYDSFLAAL
DDYFFRLVLD DEEEQEPTER RPDFESEIAK HERIIEQQQG AIEGFEQEAE SLREQAELLY
AQYGLVDEIL STIQEARDQD RSWDEIEERF AEGAERGIEA AEAVADVDGS EGTVTVELDG
ERIDLNANRG VEQNADRLYT EAKRVEEKKE GALAAIEDTR EDLEAVKRRR NEWEADESGS
ADADEDEGDE DEDAKRDWLS EPSVPIRENE PWFDRFRWFH TSDDYLVIGG RNADQNEELV
KKYLEPGDKV LHTQAHGGPV TVLKATDPSE SSSSDIELPE SSIEEAAQFA VTYASVWKDG
RYAGDVYAVD ADQVSKTPES GEYLEKGGFA IRGDRTYYRD TPVGAAVGIQ CEPYTRVIGG
PPSAIEDRAV TTIELEPGRY AQADAAKRMY RRFRERFADE SFVRKIASPD RIQHFMPPGG
SRIKED
//
