A3NY56 (SYS_BURP0) 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:	BURPS1106A_3038

Organism

Burkholderia pseudomallei (strain 1106a) [Complete proteome] [HAMAP]

Taxonomic identifier

357348 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › Burkholderia pseudomallei

Protein attributes

Sequence length	433 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 HAMAP-Rule MF_00176.
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 – 433	433	Serine--tRNA ligase HAMAP-Rule MF_00176		PRO_1000019632
Regions
	Nucleotide binding	266 – 268	3	ATP By similarity
	Nucleotide binding	353 – 356	4	ATP By similarity
	Region	235 – 237	3	Serine binding By similarity
Sites
	Binding site	289	1	Serine By similarity
	Binding site	388	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3NY56 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 08EEE6AB03CE85A4	FASTA	433	47,607
	10 20 30 40 50 60 MLDIQLLRKD LDGVAKRLAD RGYPLDVAAF SALEAERRAI QTRTEELQAR RNSLSKQIGA 70 80 90 100 110 120 MKGRGEDTSA VMAEVGGIGD EMKASAVKLD EIQARLSELM LEMPNVPHES VPVGRDETEN 130 140 150 160 170 180 VEVRRWGAPR QFDFDVKDHV DVGTPLGLDF ETGAKLSGAR FTVLRGPIAR LHRALAQFML 190 200 210 220 230 240 DTHTQQHGYS ETYTPYIVNP DVLYGTGQLP KFAEDMFRVE KGGAENTVTQ YLISTSEISL 250 260 270 280 290 300 TNTVRDSIVE ASALPIKLTA HSPCFRSEAG SYGRDTRGMI RQHQFDKVEM VQIVAPEASY 310 320 330 340 350 360 AALDEMVGHA EAILQKLELP YRVVALCTGD MGFSAAKTFD LEVWLPAQNT YREISSCSNT 370 380 390 400 410 420 ESFQARRMQA RFRNAQGKPE LVHTLNGSGL AVGRTLVAVL ENYQNADGSV TVPVALRPYM 430 GGVERIDAPS SAA

References

[1]	DeShazer D., Woods D.E., Nierman W.C. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1106a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000572 Genomic DNA. Translation: ABN91940.1.
RefSeq	YP_001067277.1. NC_009076.1.
3D structure databases
ProteinModelPortal	A3NY56.
SMR	A3NY56. Positions 1-427.
ModBase	Search...
Protein-protein interaction databases
STRING	357348.BURPS1106A_3038.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN91940; ABN91940; BURPS1106A_3038.
GeneID	4902635.
KEGG	bpl:BURPS1106A_3038.
PATRIC	19224434. VBIBurPse14980_2863.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HOG000035938.
KO	K01875.
OMA	NTVRESI.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	BPSE357348:GHVF-3038-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_BURP0

Accession

Primary (citable) accession number: A3NY56

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	May 29, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program