Reviewed, UniProtKB/Swiss-Prot A1WBD4 (SYS_ACISJ)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS

Gene names

Name:	serS
Ordered Locus Names:	Ajs_3445

Organism

Acidovorax sp. (strain JS42) [Complete proteome] [HAMAP]

Taxonomic identifier

232721 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	442 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 442	442	Seryl-tRNA synthetase HAMAP MF_00176		PRO_1000019602
Regions
	Nucleotide binding	280 – 282	3	ATP By similarity
	Nucleotide binding	367 – 370	4	ATP By similarity
	Region	249 – 251	3	Serine binding By similarity
Sites
	Binding site	303	1	Serine By similarity
	Binding site	402	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1WBD4-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: C3E6EE71D6AECCBC	FASTA	442	48,728
	10 20 30 40 50 60 MLDILLLRKD LASAVARLET RKKPQAFLNV EAFQALESER KTIQMRTEEL QSQRNQLSKQ 70 80 90 100 110 120 IGMLMGKGEK DAAEAAKAQV AAIKAELDGS ATRLDQIQGE LQTMLAAVPN LPHESVPVGS 130 140 150 160 170 180 DESANVEVRR WSPDGQQPRS LGFTPKDHVD LGEPLGLDFD MGVKLSGSRF TVMKGGIARL 190 200 210 220 230 240 HRALAQFMLD VQTQEHGYTE CYVPYVVNAD SLKGTGQLPK FEGDLFAAQK GGQDAEPVPD 250 260 270 280 290 300 NAQLYLIPTS EVPLTNFVRD EVLAEAQLPL KLTAHTPCFR SEAGSYGRDT RGMIRQHQFD 310 320 330 340 350 360 KVEMVQIVHP DKSYEALEEM TRHAEAVLQK LGLPYRVMSL CTGDMGFGAA KTYDLEVWLP 370 380 390 400 410 420 AQNTYREISS VSNCEAFQAR RLQARFKNAQ GKNELVHTLN GSGLAVGRTL VAVLENYQNE 430 440 DGSVTIPEVL RPYMGGQATL SV

References

[1]

"Complete sequence of chromosome 1 of Acidovorax sp. JS42." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000539 Genomic DNA. Translation: ABM43559.1.
RefSeq	YP_987635.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1WBD4.
Genome annotation databases
GeneID	4674357.
GenomeReviews	Gene locus Ajs_3445 in contig CP000539_GR.
KEGG	ajs:Ajs_3445.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	EHFEIGE.
Family and domain databases
HAMAP	MF_00176. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTS	PR00981. TRNASYNTHSER.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_ACISJ

Accession

Primary (citable) accession number: A1WBD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)