(data stored in ACNUC14830 zone)

HOGENOM: DICT6_1_PE1002

ID   DICT6_1_PE1002                       STANDARD;      PRT;   481 AA.
AC   DICT6_1_PE1002; B5YED1;
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 -; (DICT6_1.PE1002).
GN   Name=gatB; OrderedLocusNames=DICTH_1040;
OS   DICTYOGLOMUS THERMOPHILUM H-6-12.
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICT6_1.PE1002.
CC       Dictyoglomus thermophilum H-6-12, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B5YED1_DICT6
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; B5YED1; -.
DR   EMBL; CP001146; ACI20123.1; -; Genomic_DNA.
DR   RefSeq; YP_002250889.1; NC_011297.1.
DR   ProteinModelPortal; B5YED1; -.
DR   STRING; B5YED1; -.
DR   GeneID; 6945541; -.
DR   GenomeReviews; CP001146_GR; DICTH_1040.
DR   KEGG; dth:DICTH_1040; -.
DR   OMA; NIHEGSY; -.
DR   ProtClustDB; CLSK2410140; -.
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; DICT6_1.PE1002; -.
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Transferase.
SQ   SEQUENCE   481 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYKPVIGLEV HAQLSTKTKL FCSCSTEHEN LPPNTNVCPI CMGFPGVLPV VNKKAVEYAI
     KAGLALNCEI SNYSKFDRKN YFYPDLPKGY QISQYDLPLC RNGYIDLYVD GEIKRVRIKR
     IHLEEDAGKL LHIGSGDRLS ESDYSLVDFN RAGIPLIEIV TEPDINSPKE ARLFLQELRL
     ILRYLGISSG DMEKGSLRCD ANISIQTEEG KFGTRTEIKN VNSFFSLEKA LEYEIERQIE
     ILKRGEEVIQ ETRHWDEKKQ KTVSLRSKEE AEDYRYFPEP DLPPLMVTEE MKNKLKSEIP
     ELPAKRRERY LALELSPVDV EILVSDKDLS DFFDKALRIY GNAKNLHSWL SVEILSYLNE
     NKLEFKDLDI DPEKFVKLIE MVDKNEITRP VAKEVLRKYL TQKEDPLVII EKEGLRVVAD
     TSYLQDIIKN VISNNSKAVE DWKKGKKQVI NFLVGQVMKE TRGRASLDVV KNLLEEELNK
     L
//

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