ID A0A1Q7ABX9_9CHLR Unreviewed; 438 AA.
AC A0A1Q7ABX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Aspartate--tRNA ligase {ECO:0000313|EMBL:OLB59615.1};
DE Flags: Fragment;
GN ORFNames=AUH94_09410 {ECO:0000313|EMBL:OLB59615.1};
OS Ktedonobacter sp. 13_2_20CM_2_54_8.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805234 {ECO:0000313|EMBL:OLB59615.1, ECO:0000313|Proteomes:UP000186751};
RN [1] {ECO:0000313|EMBL:OLB59615.1, ECO:0000313|Proteomes:UP000186751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303}.
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:OLB59615.1}.
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DR EMBL; MNDO01000612; OLB59615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7ABX9; -.
DR Proteomes; UP000186751; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 CDD; cd04317; EcAspRS_like_N; 1.
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; IPR004524; Asp-tRNA-ligase_1.
DR InterPro; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR029351; GAD_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02938; GAD; 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; SSF55261; GAD domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OLB59615.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 149..301
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT NON_TER 438
FT /evidence="ECO:0000313|EMBL:OLB59615.1"
SQ SEQUENCE 438 AA; 49645 MW; CDD1EFFAF301B1B2 CRC64;
MAYAVHYRTH TCGDLNKDAI GQQVTLAGWV NRRRDHGGLV FLDIRDRYGI TQVICDPERS
AEAHRVASEV RSEYVVQVSG KVVPRLAGAE NPNLSTGAIE VAAEHIEILS PSRTTPFPIR
DDIQVDESLR LKYRYLDLRR PSMRDNMILR HRVVKAMRDY LDERGFLEIE TPILMKSTPE
GARDYLVPSR LYPGEFYALP QSPQQLKQLL MVAGLDRYFQ IARCFRDEDQ RSDRQPEFTQ
LDVEMSFVDE EDVMNLIEGL LIFLIEETTQ KRIKLVPFPR LSFSEVMDRY GTDHPDLRFD
LPLVEISDLA RAGNFGVFQS ALAANGMVKG IRVPGAGGYS RKEIEELTEF ARMLGAKGLV
SLAIGPTGEV KSPLIKFMSR EEVQAIIDRL QGEPGDLLLF VADSAKVCND VLYRLRGKLA
ERLNLIDPNE MALCWVVD
//
