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Database: UniProt
Entry: A1S198_THEPD
LinkDB: A1S198_THEPD
Original site: A1S198_THEPD 
ID   A1S198_THEPD            Unreviewed;       323 AA.
AC   A1S198;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Aspartate-ammonia ligase {ECO:0000313|EMBL:ABL79228.1};
DE            EC=6.3.1.1 {ECO:0000313|EMBL:ABL79228.1};
GN   OrderedLocusNames=Tpen_1833 {ECO:0000313|EMBL:ABL79228.1};
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL79228.1, ECO:0000313|Proteomes:UP000000641};
RN   [1] {ECO:0000313|Proteomes:UP000000641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX   PubMed=18263724; DOI=10.1128/JB.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(2008).
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DR   EMBL; CP000505; ABL79228.1; -; Genomic_DNA.
DR   RefSeq; WP_011753493.1; NC_008698.1.
DR   AlphaFoldDB; A1S198; -.
DR   STRING; 368408.Tpen_1833; -.
DR   EnsemblBacteria; ABL79228; ABL79228; Tpen_1833.
DR   GeneID; 4602070; -.
DR   KEGG; tpe:Tpen_1833; -.
DR   eggNOG; arCOG00409; Archaea.
DR   HOGENOM; CLU_004553_2_2_2; -.
DR   OrthoDB; 131570at2157; -.
DR   Proteomes; UP000000641; Chromosome.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0004071; F:aspartate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   PANTHER; PTHR22594:SF48; ASPARAGINYL-TRNA SYNTHETASE-RELATED PROTEIN (N-TRUNCATION); 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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, ECO:0000313|EMBL:ABL79228.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000641}.
FT   DOMAIN          107..312
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   323 AA;  37545 MW;  EEDDD3473FC51F5D CRC64;
     MEQKTLTLLR DYGVKPLHEL SQEELEVKRS IARITTYTLS FLSRYLVERG FDWVLPVVFS
     KSTDPLWPDP DFSIEKRIEV EIYGETVRST QSMIVHKQVL VSLLSPKIFV FSPNVRIETR
     KRASTGIHAY EFTQLDFEVR GASSSYIRSL VEDMLKSYVS SLKREMEHEL SFLGSELPEI
     MTPFKVVDSK ELEEEYGKEW QTSLRSTLKE PVWVVNIPRE FYDFEDPETG RWDNYDLYVP
     RVGEILSGAR REYEYEKILS KMKRDGVRPE NYRVLLDLAR EGRLLPSAGA GIGVERLLLW
     VTGVRHIGIV QPFPRIPGIV FDL
//
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