P57398 (SYS_BUCAI) 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:	BU313

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum)

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 Reference 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_0000122018
Regions
	Nucleotide binding	264 – 266	3	ATP By similarity
	Nucleotide binding	351 – 354	4	ATP By similarity
	Region	233 – 235	3	Serine binding By similarity
Sites
	Binding site	287	1	Serine By similarity
	Binding site	387	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57398 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: A4B485CD1DBD4026	FASTA	427	49,523
	10 20 30 40 50 60 MLNPYLLRNE LHLTAKKLLK KGYKLNISKI SSMEEKRKTL QIQTENLQFK HNALSNLFKE 70 80 90 100 110 120 NKNIKNKNEL LRHQVIQSSK DLNASKIELN SLKEKIHHFS MCIPNIPSDD VPEGNTSINN 130 140 150 160 170 180 KEIKYWGQKK KYDFEIQDHI ELGKKFNELD WKSSAQMSGS RFVIMKGKIA LLHRALSQFM 190 200 210 220 230 240 LDLHTLKHGY IESYVPYLVH SEALYGTGQL PKFSDDLFHI NLTDKKKYIL IPTGEVPLTN 250 260 270 280 290 300 LVYDQIIDEK DLPIMLTAHT PCFRSEASSY GRDTKGLIRL HQFDKVELVQ IVKPEKSYEA 310 320 330 340 350 360 LEKLTNHAEK VLQLLNLPYR KMLLCTGDTG FAAVKTYDLE VWFPSEKKYR EVSSCSNMSD 370 380 390 400 410 420 FQARRIKARY RKKSEQKNFF VHTLNGSGLA IGRTLAAILE NYQHSNGRIE IPKVLQKKYM QGLEFIN

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB13021.1.
RefSeq	NP_240135.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57398.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB13021; BAB13021; BAB13021.
GeneID	1110012.
KEGG	buc:BU313.
PATRIC	21244154. VBIBucAph127364_0325.
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HOG000035938.
KO	K01875.
OMA	NTVRESI.
ProtClustDB	PRK05431.
Enzyme and pathway databases
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_BUCAI

Accession

Primary (citable) accession number: P57398

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program