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Aspartate--tRNA ligase (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS)

 A0A126SRW4_MYCMY        Unreviewed;       574 AA.
A0A126SRW4;
11-MAY-2016, integrated into UniProtKB/TrEMBL.
11-MAY-2016, sequence version 1.
25-OCT-2017, entry version 13.
RecName: Full=Aspartate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00044};
EC=6.1.1.12 {ECO:0000256|HAMAP-Rule:MF_00044};
AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
Name=aspS_3 {ECO:0000313|EMBL:AMK56798.1};
Synonyms=aspS {ECO:0000256|HAMAP-Rule:MF_00044};
ORFNames=MSCT144_09060 {ECO:0000313|EMBL:AMK56798.1};
Mycoplasma mycoides subsp. mycoides.
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=2103 {ECO:0000313|EMBL:AMK56798.1};
[1] {ECO:0000313|Proteomes:UP000069590}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=T1/44 {ECO:0000313|Proteomes:UP000069590};
Gourgues G., Barre A., Beaudoing E., Weber J., Magdelenat G.,
Barbe V., Schieck E., Jores J., Vashee S., Blanchard A., Lartigue C.,
Sirand-Pugnet P.;
"Complete Genome sequence of Mycoplasma mycoides subsp. mycoides
T1/44, vaccine strain against contagious bovine pleuropneumoniae.";
Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in
a two-step reaction: L-aspartate is first activated by ATP to form
Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
{ECO:0000256|HAMAP-Rule:MF_00044}.
-!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
diphosphate + L-aspartyl-tRNA(Asp). {ECO:0000256|HAMAP-
Rule:MF_00044}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651735}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651743}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00667367}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
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EMBL; CP014346; AMK56798.1; -; Genomic_DNA.
RefSeq; WP_061104453.1; NZ_CP014346.1.
EnsemblBacteria; AMK56798; AMK56798; MSCT144_09060.
PATRIC; fig|2103.21.peg.882; -.
Proteomes; UP000069590; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
InterPro; IPR004364; aa-tRNA-synt_II.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004524; Asp-tRNA-ligase_1.
InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
InterPro; IPR004115; GAD-like.
InterPro; IPR029351; GAD_dom.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
Pfam; PF02938; GAD; 1.
Pfam; PF00152; tRNA-synt_2; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
PRINTS; PR01042; TRNASYNTHASP.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF55261; SSF55261; 1.
TIGRFAMs; TIGR00459; aspS_bact; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
3: Inferred from homology;
Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651728};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Complete proteome {ECO:0000313|Proteomes:UP000069590};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651756};
Ligase {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651728};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651746};
Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00044,
ECO:0000256|SAAS:SAAS00651732}.
DOMAIN 138 544 AA_TRNA_LIGASE_II.
{ECO:0000259|PROSITE:PS50862}.
NP_BIND 215 217 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
NP_BIND 523 526 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
REGION 193 196 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 169 169 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 215 215 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 224 224 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 437 437 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
BINDING 471 471 ATP. {ECO:0000256|HAMAP-Rule:MF_00044}.
BINDING 478 478 Aspartate. {ECO:0000256|HAMAP-
Rule:MF_00044}.
SEQUENCE 574 AA; 66670 MW; 884BF38212A962E4 CRC64;
MKRTHTCGEL TINNIDQEVI LQGWVKKIRK LGAMVFIDLK DRYGITQLVV DQQHIDLINN
VKNEYVIEIK GNVVKRKSIN KELVTGDIEV IVKELFIINK SELTPFVLEN DVNVNEDTRL
TYRYLDLRRP VMQNNLIIRA KINHIIRNFL TDSNFLEVET PYFAKSTPEG ARDFLVPSRL
NKNKFYALPQ SPQLFKQLLM ISGIDRYYQI VRCFRDEDLR IDRQPEFTQL DLEMSFATSE
DVMQISESLI KKILKEVKNF EIKEPLLRLS YKDAIDLYGS DKPDLRYDLK IHTLNDIFKN
TNIKFLNNPD LFIRAICIDK LLSKKQLEDL NQQAKQFHFN SIAFIKFENN NWSGSLASQL
TENEKELLIK EFDIKNKATI VLNIGKYEQI SQLMGAIRIS LAKMFNLETK DDFKLLWVVD
FPLFEFSEQE NRYVAAHHPF TSPKEECLTD FDTNKKDALT CAYDLVMNGF EIGGGSQRIT
NPEIQQRMFD AVELTTQQVE TNFGWFMNAY KYGAPYHAGI AWGLDRISMI VTDSNSIRDV
IAFPKNSLGI DMMSNAPDLV SEKQLEELNI KIVK


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