CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021898
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B 
Protein Synonyms/Alias
 Asp/Glu-ADT subunit B 
Gene Name
 gatB 
Gene Synonyms/Alias
 TTHA0366 
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
256KTYPMRTKEEEADYRacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841] 
Functional Description
 Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). 
Sequence Annotation
  
Keyword
 3D-structure; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 469 AA 
Protein Sequence
MYEAVIGLEV HLHLKTRTKM FCGCRADYFG AEPNTHTCPV CLGLPGALPV PNRVAVEHGL 60
RLALALGAEV PERLVFHRKN YFYPDLPKNY QISQYDLPLG RGGSLPLGER RVRIKRLHLE 120
EDAGKSLHLE GRTLLDLNRA GSPLIELVTE PDLKTPEEAR LFLQRIQALV QTLGISDASP 180
EEGKLRADVN VSVRRVGEPL GTKVEIKNLN SFKSVQRALE YEIRRQTEIL RRGEKVKQAT 240
MGFEEGSGKT YPMRTKEEEA DYRYFPEPDL PPVAIPRDWL EEVRRSLPEL PWEKEARYRA 300
LGIKEKDAEV LAYTPSLARF LDQALPLGLA SPQALANWLL ADVAGLLHER GLRLEETRLS 360
PEGLARLVGL FERGEVTSRV AKSLLPEVLE GQDPEALVRE RGLKVVADEG ALKALVAEAI 420
AAMPEAAESV RQGKVKALDA LVGQVMRKTR GQARPDLVRR LLLEALGVG 469 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
 GO:0006412; P:translation; IEA:UniProtKB-KW. 
Interpro
 IPR004413; Apn/Gln-ADT_bsu.
 IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
 IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
 IPR018027; Asn/Gln_amidotransferase.
 IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel.
 IPR017958; Gln-tRNA_amidoTrfase_suB_CS. 
Pfam
 PF02934; GatB_N
 PF02637; GatB_Yqey 
SMART
 SM00845; GatB_Yqey 
PROSITE
 PS01234; GATB 
PRINTS