ID A0A0W1R4Q1_9EURY Unreviewed; 708 AA.
AC A0A0W1R4Q1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AUR64_18990 {ECO:0000313|EMBL:KTG08324.1};
OS Haloprofundus marisrubri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloprofundus.
OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG08324.1, ECO:0000313|Proteomes:UP000054387};
RN [1] {ECO:0000313|EMBL:KTG08324.1, ECO:0000313|Proteomes:UP000054387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB9 {ECO:0000313|EMBL:KTG08324.1,
RC ECO:0000313|Proteomes:UP000054387};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT archaeon isolated from the Discovery deep brine-seawater interface in the
RT Red Sea.";
RL Submitted (DEC-2015) 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}.
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:KTG08324.1}.
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DR EMBL; LOPU01000031; KTG08324.1; -; Genomic_DNA.
DR RefSeq; WP_058583044.1; NZ_LOPU01000031.1.
DR AlphaFoldDB; A0A0W1R4Q1; -.
DR STRING; 1514971.AUR64_18990; -.
DR OrthoDB; 10943at2157; -.
DR Proteomes; UP000054387; 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; 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 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 500..616
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT REGION 288..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..478
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 79762 MW; 791E94B0832EFA8D CRC64;
MDPKRELSSI DLAALVTELR RYEGAKVDKA YLYGDDLLRL KMRDFDRGRV ELFVEVGDVK
RAHVAAAEHV PDAPGRPPNF AKMLRNRLSG ADFAGVEQFE FDRILVFKFE RGDSDTELVA
ELFGQGNIAV LDENREVVSS LSTVRLKSRT VAPGSQYEFP SSRLNPLDVR YEAFAHKMDD
SDTDVVRTLA TQLNLGGLYA EEVCTRAGVE KTMDIADAGD EEYEKLYDAL GRLRDQLAKG
EFDPRVYLED DAVVDVTPFP LEEHESEGLD AEAYDSFNGA LDEYFHRLDR SDDDGGSSGG
GAAADTGRPD FQEEIEKKQR IIEQQEGAIS GFDEQAQEER ERAEQVYARY DLVNEILTTI
RGAREQGVPW DDIGTKFEEG KEQGIDAAEA VRGVDGANGT VTVSLDDTTV TLDVSMGVEK
NADQLYKEAK RVEEKKEGAL DAIEDTREDL EALKKRREEW ERGDEDEDEE DEEDDDHEEI
NWLSRQSVPI RQQDHWFERF RWFRTSDDFL VIGGRNADQN EELVKKYLGK GDLFFHTQAR
GGPVTILKAT GPSEPARDVE IPEQSREEAA QFAVSYASVW KEGRFAEDAY MVTHDQVSKT
PESGEYVEKG SFVIRGDRTY YRDVKAEVAV GIACEPETRV VGGPPSAIEP QAETSIRVRP
GRYAQNDMAQ MCYRQLRKRF ADQSFVRKVA SADKIQEFLP PGGSEMVE
//
