Reviewed, UniProtKB/Swiss-Prot A0JR71 (SYS_ARTS2)

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:	Arth_0140

Organism

Arthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]

Taxonomic identifier

290399 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	426 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 – 426	426	Seryl-tRNA synthetase HAMAP MF_00176		PRO_1000019612
Regions
	Nucleotide binding	259 – 261	3	ATP By similarity
	Nucleotide binding	346 – 349	4	ATP By similarity
	Region	228 – 230	3	Serine binding By similarity
Sites
	Binding site	275	1	ATP; via carbonyl oxygen and amide nitrogen By similarity
	Binding site	282	1	Serine By similarity
	Binding site	386	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0JR71-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 90619D46F2F0339B	FASTA	426	46,771
	10 20 30 40 50 60 MIDVKDLSEN PDKFRASQRA RGADESVVDA IISADAARRA ALIRFENLRA EQNAFGKKVA 70 80 90 100 110 120 QAKGEEKQAL LAEVKVLAAS VKAASAEADV AQAQQEELLR AIPNLIVDGV PEGGEDDYIV 130 140 150 160 170 180 VKTVGEPREF PDFEPKDHLE IGELIGAIDM ERGAKVSGSR FYFLRGVGAR LEMALLQMAM 190 200 210 220 230 240 EQAIDAGFIP MITPTLVRPE TMQGTGFDVK HDAEIYRLAE DDLYLVGTSE VALAGYHADE 250 260 270 280 290 300 ILDLSAGPIR YAGQSSCYRR EAGSHGKDTR GIIRVHQFNK VEMFIYTTVE EAAAEHERLL 310 320 330 340 350 360 AWEEEMLAKC ELPYRVIDTA AGDLGNSAAR KFDCEAWVPT QGAYRELTST SNCTTFQARR 370 380 390 400 410 420 LNIRERVLNE DGAPKGTRAV ATLNGTLATT RWIVAILEHH QNEDGSVNVP RALQKYLGGL EVLPVL

References

[1]

"Complete sequence of chromosome 1 of Arthrobacter sp. FB24." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000454 Genomic DNA. Translation: ABK01541.1.
RefSeq	YP_829641.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0JR71.
Genome annotation databases
GeneID	4447403.
GenomeReviews	Gene locus Arth_0140 in contig CP000454_GR.
KEGG	art:Arth_0140.
TIGR	Arth_0140.
Phylogenomic databases
OMA	KNEAVFL.
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_ARTS2

Accession

Primary (citable) accession number: A0JR71

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 12, 2006
Last modified:	November 3, 2009
This is version 24 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)