(data stored in ACNUC7421 zone)

HOGENOM: ECOL6_1_PE1004

ID   ECOL6_1_PE1004                       STANDARD;      PRT;   430 AA.
AC   ECOL6_1_PE1004; P0A8L2; P09156;
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=Seryl-tRNA synthetase; EC=6.1.1 11;AltName:
DE   Full=Serine--tRNA ligase; Short=SerRS;AltName: Full=Seryl-tRNA(Ser/Sec)
DE   synthetase; (ECOL6_1.PE1004).
GN   Name=serS; OrderedLocusNames=c1030;
OS   ESCHERICHIA COLI O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOL6_1.PE1004.
CC       Escherichia coli O6 (strain UPEC / O6:H1 / ATCC 700928 / CFT073)
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:SYS_ECOL6
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
CC       able to aminoacylate tRNA(Sec) with serine, to form the
CC       misacylated tRNA L-seryl-tRNA(Sec), which will be further
CC       converted into selenocysteinyl-tRNA(Sec) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate
CC       + L-seryl-tRNA(Ser).
CC   -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate
CC       + L-seryl-tRNA(Sec).
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
CC       1/1.
CC   -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a
CC       N-terminal extension that is involved in tRNA binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Type-1 seryl-tRNA synthetase subfamily.
CC   -!- GENE_FAMILY: HOG000035938 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P0A8L2; P09156; -.
DR   EMBL; AE014075; AAN79502.1; -; Genomic_DNA.
DR   RefSeq; NP_752959.1; NC_004431.1.
DR   ProteinModelPortal; P0A8L2; -.
DR   SMR; P0A8L2; 1-430.
DR   EnsemblBacteria; EBESCT00000044015; EBESCP00000042364; EBESCG00000043065.
DR   GeneID; 1036773; -.
DR   GenomeReviews; AE014075_GR; c1030.
DR   KEGG; ecc:c1030; -.
DR   GeneTree; EBGT00050000009989; -.
DR   OMA; HTKPLEE; -.
DR   ProtClustDB; PRK05431; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00176; Ser_tRNA_synth_type1; 1; -.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002317; Ser-tRNA-synth_IIa.
DR   InterPro; IPR015866; Ser-tRNA-synth_IIa_N.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   Gene3D; G3DSA:1.10.287.40; Ser-tRNA-synth_IIa_N; 1.
DR   PANTHER; PTHR11778; tRNA-synt_ser; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF46589; tRNA_binding_arm; 1.
DR   TIGRFAMs; TIGR00414; SerS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   HOGENOMDNA; ECOL6_1.PE1004; -.
KW   AAN79502.1000068575old_1320000031;
KW   Seryl-tRNA synthetase ;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   430 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLDPNLLRNE PDAVAEKLAR RGFKLDVDKL GALEERRKVL QVKTENLQAE RNSRSKSIGQ
     AKARGEDIEP LRLEVNKLGE ELDAAKAELD ALQAEIRDIA LTIPNLPADE VPVGKDENDN
     VEVSRWGTPR EFDFEVRDHV TLGEMHSGLD FAAAVKLTGS RFVVMKGQIA RMHRALSQFM
     LDLHTEQHGY SENYVPYLVN QDTLYGTGQL PKFAGDLFHT RPLEEEADTS NYALIPTAEV
     PLTNLVRGEI IDEDDLPIKM TAHTPCFRSE AGSYGRDTRG LIRMHQFDKV EMVQIVRPED
     SMAALEEMTG HAEKVLQLLG LPYRKIILCT GDMGFGACKT YDLEVWIPAQ NTYREISSCS
     NVWDFQARRM QARCRSKSDK KTRLVHTLNG SGLAVGRTLV AVMENYQQAD GRIEVPEVLR
     PYMNGLEYIG
//

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