(data stored in ACNUC7421 zone)

HOGENOM: LEXYL1_1_PE101

ID   LEXYL1_1_PE101                       STANDARD;      PRT;   425 AA.
AC   LEXYL1_1_PE101; Q6AHD6;
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   SubName: Full=Aspartyl-tRNA synthetase; (LEXYL1_1.PE101).
GN   Name=aspS; OrderedLocusNames=Lxx01320;
OS   LEIFSONIA XYLI SUBSP. XYLI STR. CTCB07.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=281090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEXYL1_1.PE101.
CC       Leifsonia xyli subsp. xyli str. CTCB07, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:Q6AHD6_LEIXX
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000226032 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6AHD6; -.
DR   EMBL; AE016822; AAT88209.1; -; Genomic_DNA.
DR   RefSeq; YP_061314.1; NC_006087.1.
DR   ProteinModelPortal; Q6AHD6; -.
DR   GeneID; 2938496; -.
DR   GenomeReviews; AE016822_GR; Lxx01320.
DR   KEGG; lxx:Lxx01320; -.
DR   NMPDR; fig|281090.3.peg.1236; -.
DR   OMA; FRAEPHD; -.
DR   ProtClustDB; CLSK821593; -.
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   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
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:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 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   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   HOGENOMDNA; LEXYL1_1.PE101; -.
KW   aspartyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   425 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVAGWVETV RDQKKVQFVV LRDESGAVQL VNPRTVNEDG TVAADEPALT VSGLSQGSFV
     RATGELKHDE RVKLGGIEIK LSALDVETAA IPETPIAADS GIDKRMDWRF LDLREPKHNL
     IFRVQTTFEN ALRHYWVDNG FIEIHTPKLM ASASESRAEL FELPYFETTA YLAQSPQIFK
     QMAQAAGFGK VFEIGPAFRA DPSFTSRHAT EFTSVDTEIS WIESHEDVMK VHEDLLVAGF
     TAVKEKHGAE IEALFGVEIT VPTTPFPRIP LAEAKRIVAE RGYEVPRHDD DMDPEGERQI
     SAYVKETFGH EFVFLTDYAA SIRPYYHMRH SEDRSITKSY DLIFNGVEIS TGAQREHRVE
     TIEQQAREKG LSVEELEDVL AFFRYGVPPH GGFGMGLARV LMLMLHLSNL RETTYLFRGP
     TRLTP
//

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