Q81JC4 (SYS_BACCR) 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:	BC_0017

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	424 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 MF_00176
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity HAMAP 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 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	seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 424	424	Serine--tRNA ligase HAMAP MF_00176		PRO_0000121999
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)
	Q81JC4 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 2A876A0D7C280B26	FASTA	424	48,790
	10 20 30 40 50 60 MLDIKFLRTN FEEVKAKLQH RGEDLTDFGR FEELDTRRRE LLVQTEELKS KRNEVSQQIS 70 80 90 100 110 120 VLKREKKDAE ALILEMREVG EKVKDLDNEL RTVEEDLERL MLSIPNIPHE SAPVGETEDD 130 140 150 160 170 180 NVVARTWGEV KEFTYEPKPH WDLATDLGIL DFERAGKVTG SRFVFYKGAG ARLERALISF 190 200 210 220 230 240 MLDLHTDEHG YEEVLPPYMV NRASMTGTGQ LPKFEEDAFR IESEDYFLIP TAEVPVTNMH 250 260 270 280 290 300 RDEILNKEQL PIRYAAFSSC FRSEAGSAGR DTRGLIRQHQ FNKVELVKFV KPEDSYEELE 310 320 330 340 350 360 KLTNDAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW IPSYGTYREI SSCSNFEAFQ 370 380 390 400 410 420 ARRANIRFRR EPNGKPEHVH TLNGSGLAIG RTVAAILENY QQEDGTIIIP EVLRPYMGGK TVIK

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP07122.1.
RefSeq	NP_829921.1. NC_004722.1.
3D structure databases
ProteinModelPortal	Q81JC4.
SMR	Q81JC4. Positions 1-424.
ModBase	Search...
Protein-protein interaction databases
STRING	Q81JC4.
Proteomic databases
PRIDE	Q81JC4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000032250; EBBACP00000031456; EBBACG00000032241.
GeneID	1202370.
GenomeReviews	Gene locus BC_0017 in contig AE016877_GR.
KEGG	bce:BC0017.
PATRIC	32595635. VBIBacCer54481_0037.
Phylogenomic databases
eggNOG	COG0172.
GeneTree	EBGT00050000002086.
HOGENOM	HBG629391.
OMA	PKFADDM.
PhylomeDB	Q81JC4.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	BCER226900:BC_0017-MONOMER.
Family and domain databases
HAMAP	MF_00176. Ser_tRNA_synth_type1. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-synth_IIa. IPR015866. Ser-tRNA-synth_IIa_N. IPR010978. tRNA-bd_arm. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KO	K01875.
PANTHER	PTHR11778. tRNA-synt_ser. 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_BACCR

Accession

Primary (citable) accession number: Q81JC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program