ID A0A151BF34_9ARCH Unreviewed; 392 AA.
AC A0A151BF34;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Asparaginyl-tRNA synthase {ECO:0000313|EMBL:KYH38535.1};
DE Flags: Fragment;
GN ORFNames=AYL28_003370 {ECO:0000313|EMBL:KYH38535.1};
OS Candidatus Bathyarchaeota archaeon B23.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779367 {ECO:0000313|EMBL:KYH38535.1, ECO:0000313|Proteomes:UP000075353};
RN [1] {ECO:0000313|EMBL:KYH38535.1, ECO:0000313|Proteomes:UP000075353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B23 {ECO:0000313|EMBL:KYH38535.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KYH38535.1}.
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DR EMBL; LUCA01000023; KYH38535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BF34; -.
DR PATRIC; fig|1779367.3.peg.470; -.
DR Proteomes; UP000075353; Unassembled WGS sequence.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 134..392
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 392
FT /evidence="ECO:0000313|EMBL:KYH38535.1"
SQ SEQUENCE 392 AA; 45394 MW; B3F7CDF37A4B0060 CRC64;
MGLVEIASIL DGEHDGEEVS IRGWMYNRRS SGGIHFLMVR DGSGVIQCTL SRDRADEETF
MRVGKLPLES VVELRGLVRV DERAPYGREL SIRGVNNLQE AQPGYPITRK RHGIDFLLDH
RHLYVRDPKM QAILRIRSKV LEAARDWMRE HGYTETHSPS FITAACEGGA TLFSVDYFGR
KDVYLTQSWQ LYAEALIYTL GKIYTIAPSF RAEKSRTRRH LAEYWHLEVE EPWTDLWGIM
EVGDELVTHI CHRVAEEMPR ELRGLGRDPG ELLRLEPPYP RITYDEALEM LRGDGVELEW
GDDFGWREEE PLTKHFDTPF WVTHYPVGVK AFYHKPNPER PEVTLSADML APEGYGEIIG
GGQRIDDFEE LLTRIVEEGL RPEDYSWYLD LR
//
