(data stored in ACNUC10043 zone)

HOGENOM: IGNAA_1_PE1015

ID   IGNAA_1_PE1015                       STANDARD;      PRT;   477 AA.
AC   IGNAA_1_PE1015; E0SNS2;
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/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B;
DE   Short=Asp/Glu-ADT subunit B; EC=6.3.5 -; (IGNAA_1.PE1015).
GN   Name=gatB; OrderedLocusNames=Igag_1054;
OS   IGNISPHAERA AGGREGANS DSM 17230.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignisphaera.
OX   NCBI_TaxID=583356;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IGNAA_1.PE1015.
CC       Ignisphaera aggregans DSM 17230 chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:E0SNS2_IGNAA
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP
CC       + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the gatB/gatE family. GatB subfamily.
CC   -!- GENE_FAMILY: HOG000223742 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E0SNS2; -.
DR   EMBL; CP002098; ADM27868.1; -; Genomic_DNA.
DR   RefSeq; YP_003859748.1; NC_014471.1.
DR   GeneID; 9716370; -.
DR   GenomeReviews; CP002098_GR; Igag_1054.
DR   KEGG; iag:Igag_1054; -.
DR   OMA; KNYFYAD; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00121; GatB; 1; -.
DR   InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR   InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel.
DR   InterPro; IPR004413; Gln-tRNA_amidoTrfase_bsu.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   PANTHER; PTHR11659; GatB; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF89095; GatB_Yqey; 1.
DR   TIGRFAMs; TIGR00133; GatB; 1.
DR   PROSITE; PS01234; GATB; 1.
DR   HOGENOMDNA; IGNAA_1.PE1015; -.
KW   glutamyl-tRNA(Gln) amidotransferase, B subunit;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   477 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRVVIGLEIH VQMTNLKTKL FCPTPSDYRG KDPNIHVCPV CLGLPGTLPV VNRKAIEYAI
     AVAKALNCEI SRKVIFVRKH YFYPDLPKNY QISQYDGPGF TPIAKNGYIK IFVDGKTKIV
     RIRRINIEED PGKIQYIGDI ERSPYSLIDY NRSGIALLEI VTEPDMESPK EARAFLEKLL
     AILEYIGVTD TALEGAFRVD ANISIEGGGR VEVKNIGSVK DVERALTFEI IRQKRIIEQG
     GVVTRETRHW DEKKGVTIPL RSKEMEEDYR YFPDPDLPPI LLTDEYINKI VSALPELPDA
     RIERFMKQYG LDEYRASVLV LNKSLADFFE ECTKIYSNYK KLADVLITDF LRWVKEYSID
     LRYRSISPEK VVKLLKLLDE GIISIKMLKE LMPKVVRDGI DVEEMVMKTG YTKIEDERYI
     ESIAREVFRE NPKAVRDAIE NPKAINFLIG AIMKKTSGRA DPQKTREIVM RLLEEYK
//

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