P81434 (SYS_BUCAP) 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:	BUsg_303

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

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_0000122019
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
	Compositional bias	371 – 376	6	Poly-Lys HAMAP-Rule MF_00176
Sites
	Binding site	287	1	Serine By similarity
	Binding site	387	1	Serine By similarity
Experimental info
	Sequence conflict	45	1	D → E in AAC05434. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P81434 [UniParc]. Last modified August 30, 2002. Version 2. Checksum: CC416EFD7C861B87	FASTA	427	49,238
	10 20 30 40 50 60 MLNPYLLRNQ IDAISKKLLK KKFKLDISLI SSLEKKRKKL QIKTDNLQYK HNTLSALFKK 70 80 90 100 110 120 EKKIQELDEN LKRTLTKSSK NLSELKIELN LLQEKIHNFS LSIPNIPSDD VPEGNSSENN 130 140 150 160 170 180 KIVKYWGKKR EYSFAVRDHV EIGNKLNQLD WKSSAKISGA RFIVMKGNIA LLHRALSQFM 190 200 210 220 230 240 LDLHTIKHGY TETYVPYLVN HDSLYGTGQL PKFTDDLFHI NSIDKKKYVL IPTAEVPLTN 250 260 270 280 290 300 LFSNQILNET ELPIMLTAHT PCFRSEASSY GRDSKGLIRL HQFDKVELVQ IIQPELSMNA 310 320 330 340 350 360 LELLTHHAEK VLQLLELPYR KVLLCGGEMG FSATKTYDLE VWFPSQKKYR EISSCSNMSD 370 380 390 400 410 420 FQARRMKTRY KKKKEKSNSF VHTLNGSGLA IGRTLAAILE NYQDSDGRVT IPKILQKKYM QGIEYIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a DNA fragment from Buchnera aphidicola (Aphid endosymbiont) containing the genes aspS-trxB-serS-serC-aroA-rpsA-himD-tpiA." Thao M.L., Baumann P. Curr. Microbiol. 35:68-69(1997) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43549 Genomic DNA. Translation: AAC05434.1. AE013218 Genomic DNA. Translation: AAM67857.1.
RefSeq	NP_660646.1. NC_004061.1.
3D structure databases
ProteinModelPortal	P81434.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg303.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67857; AAM67857; BUsg_303.
GeneID	1005507.
KEGG	bas:BUsg303.
PATRIC	21247413. VBIBucAph100086_0316.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
KO	K01875.
OMA	NTVRESI.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-359-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_BUCAP

Accession

Primary (citable) accession number: P81434

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 30, 2002
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program