ID M0LQU0_9EURY Unreviewed; 697 AA.
AC M0LQU0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=C447_16909 {ECO:0000313|EMBL:EMA35856.1};
OS Halococcus hamelinensis 100A6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA35856.1, ECO:0000313|Proteomes:UP000011566};
RN [1] {ECO:0000313|EMBL:EMA35856.1, ECO:0000313|Proteomes:UP000011566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=100A6 {ECO:0000313|EMBL:EMA35856.1,
RC ECO:0000313|Proteomes:UP000011566};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA35856.1}.
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DR EMBL; AOMB01000043; EMA35856.1; -; Genomic_DNA.
DR RefSeq; WP_007696003.1; NZ_AOMB01000043.1.
DR AlphaFoldDB; M0LQU0; -.
DR PATRIC; fig|1132509.6.peg.3921; -.
DR eggNOG; arCOG01695; Archaea.
DR OrthoDB; 10943at2157; -.
DR Proteomes; UP000011566; 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; NUCLEAR EXPORT MEDIATOR FACTOR 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:UP000011566};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00844};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00844}.
FT DOMAIN 488..604
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 306..340
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
FT COILED 427..454
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 697 AA; 77893 MW; 307F76E8BBCEBA11 CRC64;
MDPKRELTSV DLAALVTELG RYAGAKLDKA YLYGDDLLRL KLRDFDRGRV ELMVEVGETK
RAHVVSPDHV PDAPGRPPDF AKMLRNRLSG ADFAGASQFG FDRVLTFEFE REDRNTRIVA
ELFGEGNVAV LDSTGEVVDC LNTVRLQSRT VAPGAQYEFP SSRFDPLAVD YEGFAARMEE
SNTDLVRTLA TQLNFGGLYA EELCTRAGVE KEQAIEDSGE EEYSALFDAL TRLSERLSDG
DFDPRIYRED DEPVDVTPFP LEENADLDSE GFESFTEALD AYFVDLETTE NEEGGGREKP
DFEEEIERQQ RIIDQQEGAI QGFEEQAEAE RAKAESLYAN YGLVDEILST VRTARERDTP
WEEIEERFEE GKEQGIPAAE AVAGVEASEG TVSVEVDGET ITLDPREGVE QNADRLYREA
KRVVGKKEGA EEAIADTRAE LEALEQRREE WEAGGADATD ADDDSEDIDW LDRRSIPIRT
NEQWYERFRW FHTSDGFLVL GGRNADQNED LVKKYLDRGD RFLHTQARGG PVTVLKATGP
SEPTREIDLP QGTLDEAAKF AVSYSSVWKD GRFAGDVYMA DPDQVSKTPE SGEYLEKGAF
TVRGDRTYFR DTAVGAAVGI TCEPETRVVG GPPSAIEPRT ETSVTLEPGQ YAQNDAAKRL
YRTFRERFRD TSFVRKVASP DLIAEFLPPG GSRVVED
//