Q57DM2 (SYS_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine--tRNA ligase
EC=6.1.1.11

Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase

Gene names

Name:	serS
Ordered Locus Names:	BruAb1_0897

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00176
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP-Rule 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. HAMAP-Rule MF_00176
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 selenocysteinyl-tRNA(Sec) biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 – 427	427	Serine--tRNA ligase HAMAP-Rule MF_00176		PRO_1000019626
Regions
	Nucleotide binding	262 – 264	3	ATP By similarity
	Nucleotide binding	349 – 352	4	ATP By similarity
	Region	231 – 233	3	Serine binding By similarity
Sites
	Binding site	285	1	Serine By similarity
	Binding site	385	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57DM2 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 9452FF0D8CA3F376	FASTA	427	47,548
	10 20 30 40 50 60 MLDIKWIREN PETLDKALAK RGAAPLSSEL IALDEKRREH VGKVQAAQER RNAASKEIGK 70 80 90 100 110 120 AMAAKDMGTA EKLKAEVGEL KDFLAHAEED ERRLSKELSD ALSTIPNIPL DDVPLGKDES 130 140 150 160 170 180 DNVELRRIGN PHNFSFQPKE HFELGEALGY MDFERAAKLA GARFTVLKGP LARLERALGQ 190 200 210 220 230 240 FMLDLHTTEH GYTEVMPPLM VRDEAVYGTG QLPKFSEDLF RTTDGRWLIP TAEVPLTNLV 250 260 270 280 290 300 AEEIVDMKGL PLRFTALTPC FRSEAGSAGR DTRGMLRQHQ FLKVEMVSIT DAESSVAEHE 310 320 330 340 350 360 RMTACAEEVL KRLGLPFRTV VLCTGDMGFG AQRTYDIEVW LPGQNTYREI SSCSTCGDFQ 370 380 390 400 410 420 GRRMNARYRP EGEKSTRFVH TLNGSGVAVG RALIAVMENY QQEDGSIHIP EALQPYMGGL TRIEKAA

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74262.1.
RefSeq	YP_221623.1. NC_006932.1.
3D structure databases
HSSP	HSSP built from PDB template 1WLE based on UniProtKB Q9N0F3.
ProteinModelPortal	Q57DM2.
SMR	Q57DM2. Positions 1-424.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_0897.
Proteomic databases
PRIDE	Q57DM2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX74262; AAX74262; BruAb1_0897.
GeneID	3339513.
KEGG	bmb:BruAb1_0897.
PATRIC	17823422. VBIBruAbo15061_0942.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HOG000035938.
KO	K01875.
OMA	EESWEWH.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-909-MONOMER.
UniPathway	UPA00906; UER00895.
Family and domain databases
Gene3D	1.10.287.40. 1 hit.
HAMAP	MF_00176. Ser_tRNA_synth_type1.
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-ligase_type_1. IPR015866. Ser-tRNA-synth_1_N. IPR010978. tRNA-bd_arm. [Graphical view]
PANTHER	PTHR11778. PTHR11778. 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.
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_BRUAB

Accession

Primary (citable) accession number: Q57DM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program