(data stored in SCRATCH zone)

HOGENOM: SAENT6_1_PE1000

ID   SAENT6_1_PE1000                      STANDARD;      PRT;   590 AA.
AC   SAENT6_1_PE1000; A9MND2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Aspartyl-tRNA synthetase; EC=6.1.1 12;AltName:
DE   Full=Aspartate--tRNA ligase; Short=AspRS; (SAENT6_1.PE1000).
GN   Name=aspS; OrderedLocusNames=SARI_01047;
OS   SALMONELLA ENTERICA SUBSP. ARIZONAE SEROVAR 62:Z4,Z23:-- STR. RSK2980.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella; Salmonella enterica subsp. arizonae
OC   serovar 62:z4,z23:--.
OX   NCBI_TaxID=882884;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SAENT6_1.PE1000.
CC       Salmonella enterica subsp. arizonae serovar 62:z4,z23:-- str. RSK2980
CC       chromosome, complete genome.
CC   -!- ANNOTATIONS ORIGIN:SYD_SALAR
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000275159 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A9MND2; -.
DR   EMBL; CP000880; ABX20955.1; -; Genomic_DNA.
DR   RefSeq; YP_001570097.1; NC_010067.1.
DR   ProteinModelPortal; A9MND2; -.
DR   SMR; A9MND2; 1-590.
DR   STRING; A9MND2; -.
DR   GeneID; 5760316; -.
DR   GenomeReviews; CP000880_GR; SARI_01047.
DR   KEGG; ses:SARI_01047; -.
DR   OMA; AFPKTQQ; -.
DR   ProtClustDB; PRK00476; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:EC.
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   HAMAP; MF_00044_B; Asp_tRNA_synth_B; 1; -.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004524; Asp-tRNA-synth_IIb_bac/mt.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:3.30.1360.30; GAD_dom; 1.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   PANTHER; PTHR22594:SF5; AspS_bac; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00459; AspS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   HOGENOMDNA; SAENT6_1.PE1000; -.
KW   aspartyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   590 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD PDRADALKLA
     SELRNEFCIQ VTGTVRARDA KNVNADMATG EIEVLASSLT IINRADSLPL DANHINTEEA
     RLKYRYLDLR RPEMAQRLKT RAKITSLVRR FMDDHGFLDI ETPMLTKATP EGARDYLVPS
     RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT
     APQVREVMEA LVRHLWLEVK DVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELVDVADLLK
     SVEFAVFAGP ANDPKGRVAA LRVPGGAQLS RKQIDDYGNF VKIYGAKGLA YIKVNDRAKG
     LDGITSPVAK FLSTEIVEAI LARTGAQNGD MIFFGADNKK VVADALGALR LKLGKDLSLT
     DEDKWAPLWV IDFPMFEDDG EGGLTAMHHP FTAPRDMTAS ELKAAPENAV ANAYDMVING
     YEVGGGSVRI HNGEMQQTVF GILGINEQEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM
     LLTGTDNIRD VIAFPKTTAA ACLMTEAPSF ANQAALTELG IQVVKKAENN
//

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