B1HS47 (SYS_LYSSC) 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:	Bsph_0023

Organism

Lysinibacillus sphaericus (strain C3-41) [Complete proteome] [HAMAP]

Taxonomic identifier

444177 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Lysinibacillus › Lysinibacillus sphaericus

Protein attributes

Sequence length	426 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 – 426	426	Serine--tRNA ligase HAMAP-Rule MF_00176		PRO_1000098090
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)
	B1HS47 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: 51EA6FDACA7ABAA3	FASTA	426	48,892
	10 20 30 40 50 60 MLDIKRVRDN FAEIKEMLLT RNEDLGNLDD FENLDAKRRE LIAKTEELKA ERNKVSEQIS 70 80 90 100 110 120 VMKRNKENAD EVIARMRQVG DEIKELDIQL NDVEDRFKDM MMRLPNVPHE SVPVGTTEDD 130 140 150 160 170 180 NVEEYTWGEI PAFDFEIKAH WDLATDLKIV DFERGAKVTG SRFLFYRGLG ARLERALMTF 190 200 210 220 230 240 MMDLHAEEHG YEEMLPPVIV NRESLTGTGQ LPKFEEDVFK LAETDYFMIP TAEVPVTNFY 250 260 270 280 290 300 RDEILTAEAL PQGFAAYSAC FRSEAGSAGR DTRGLIRQHQ FNKVELVRFV KPEESYEQLE 310 320 330 340 350 360 LLTGHAEKVL QLLGLPYRKL KMCTADLGFT AAKKYDLEVW IPAQNMYREI SSCSNFEDFQ 370 380 390 400 410 420 ARRANIRFRR EPNAKPEYVH TLNGSGLAIG RTVAAILENY QQADGSVVIP EVLRPYMGGK EVIAPK

References

[1]

"Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species." Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., Berry C., Yuan Z. J. Bacteriol. 190:2892-2902(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C3-41.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000817 Genomic DNA. Translation: ACA37665.1.
RefSeq	YP_001695795.1. NC_010382.1.
3D structure databases
ProteinModelPortal	B1HS47.
SMR	B1HS47. Positions 1-426.
ModBase	Search...
Protein-protein interaction databases
STRING	444177.Bsph_0023.
Proteomic databases
PRIDE	B1HS47.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACA37665; ACA37665; Bsph_0023.
GeneID	6022063.
KEGG	lsp:Bsph_0023.
PATRIC	22412495. VBILysSph89750_0185.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HOG000035938.
KO	K01875.
OMA	NTVRESI.
Enzyme and pathway databases
BioCyc	LSPH444177:GJEL-29-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_LYSSC

Accession

Primary (citable) accession number: B1HS47

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 29, 2008
Last modified:	May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program