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Database: UniProt
Entry: A0A017RYA0_9CLOT
LinkDB: A0A017RYA0_9CLOT
Original site: A0A017RYA0_9CLOT 
ID   A0A017RYA0_9CLOT        Unreviewed;       594 AA.
AC   A0A017RYA0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Aspartate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00044};
DE            EC=6.1.1.12 {ECO:0000256|HAMAP-Rule:MF_00044};
DE   AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE            Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
GN   Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044};
GN   ORFNames=Q428_01050 {ECO:0000313|EMBL:EYE89637.1};
OS   Fervidicella metallireducens AeB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Fervidicella.
OX   NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE89637.1, ECO:0000313|Proteomes:UP000019681};
RN   [1] {ECO:0000313|EMBL:EYE89637.1, ECO:0000313|Proteomes:UP000019681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AeB {ECO:0000313|EMBL:EYE89637.1,
RC   ECO:0000313|Proteomes:UP000019681};
RX   PubMed=24786951;
RA   Patel B.K.;
RT   "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT   Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL   Genome Announc. 2:e00345-14(2014).
CC   -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC       two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC       AMP and then transferred to the acceptor end of tRNA(Asp).
CC       {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC         Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.12; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00044};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303, ECO:0000256|HAMAP-
CC       Rule:MF_00044}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
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:EYE89637.1}.
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DR   EMBL; AZQP01000002; EYE89637.1; -; Genomic_DNA.
DR   RefSeq; WP_035377363.1; NZ_AZQP01000002.1.
DR   AlphaFoldDB; A0A017RYA0; -.
DR   STRING; 1403537.Q428_01050; -.
DR   OrthoDB; 9802326at2; -.
DR   Proteomes; UP000019681; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00777; AspRS_core; 1.
DR   CDD; cd04317; EcAspRS_like_N; 1.
DR   Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR047090; AspRS_core.
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   ECO:0000256|HAMAP-Rule:MF_00044};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00044};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00044};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00044};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00044};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00044}; Reference proteome {ECO:0000313|Proteomes:UP000019681}.
FT   DOMAIN          155..562
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          204..207
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         180
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         226..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         226
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         455
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         496
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT   BINDING         541..544
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   594 AA;  67890 MW;  767880F7189EFBF0 CRC64;
     MGESIKGLKR SCMCGQLNES NVGNTVTLMG WVQRRRDLGS LIFVDLRDRT GIVQVVFGEE
     IDKNAFHKAE AIRSEYVLAV TGNVVLRESP NPNMPTGMIE IKATDLRILS ESETPPIYIK
     EELDAAEQIR LKYRYLDLRR PDMQRRLMVR HRAAKIVRDF MDENGFLEME TPMLTKSTPE
     GARDYLVPSR NFPGMFYALP QSPQLFKQLL MVSGFDRYFQ IVRCFRDEDL RANRQPEFTQ
     IDIEMSFVDV DDVIEMNERL IQRLFKEILN VDVKLPIMRM PYKEAMERYG SDKPDIRFGL
     ELVNLTDVVR NSSFKVFQDA IANNGDVRAI NAKGCADFGR KEIDRLGEYV KTYGAKGLAW
     IAIKEDEIKS PIGKFFSEDE MKAIIDRVNG EVGDLILIVA DKPDTVFASL GALRLELGRK
     LNLIGPENKE FKFLWVTEFP LFEYDEEENR YVAKHHPFTM PMEEDLEFLE TEPGKVRAKA
     YDIVLNGEEI GGGSIRIHDT KIQERMFKAL GFTMESAWEK FGFLLEAFKF GPPPHGGLAY
     GFDRLVMFLT GTENIKDVIA FPKNQNAACP LTNAPNVVDS KQLTELGIST INKE
//
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