B7J4C9 (SYS_ACIF2) 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:	AFE_0380

Organism

Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) [Complete proteome] [HAMAP]

Taxonomic identifier

243159 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus

Protein attributes

Sequence length	421 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
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 – 421	421	Serine--tRNA ligase HAMAP MF_00176		PRO_1000199460
Regions
	Nucleotide binding	259 – 261	3	ATP By similarity
	Nucleotide binding	346 – 349	4	ATP By similarity
	Region	230 – 232	3	Serine binding By similarity
Sites
	Binding site	282	1	Serine By similarity
	Binding site	381	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7J4C9 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 38FBE6783C6BD2A5	FASTA	421	46,558
	10 20 30 40 50 60 MLDPSLLRSS PETVAAGLAR RHFTLDVAAL NALDQQRKAL QIQLEQLRNA RNEASRQIGQ 70 80 90 100 110 120 ARRQGLDTGA MQAAAASNGE EIKTLEQSLE RTLAEWDTLT IGLPNIPQDS VPDGRDEADN 130 140 150 160 170 180 VVLRHWGSPS TFAFPPRDHV ELGEALGIID FAAGARLAGT RFVVLRGAGA RLERALTQFM 190 200 210 220 230 240 LDLHTTEHGY TEIAPPFLAN ADSLYGTGQL PKFEEDLFAL RDDPYYLIPT AEVPLTNLLR 250 260 270 280 290 300 GEIVASLPQR FCAYTPCFRR EAGAYGRDTR GMIRQHQFDK VELVQIVRPE DSAQAHETLT 310 320 330 340 350 360 AHAEKVLQLL ELPYRVTALC AGDLGFSAAK TYDLEVWLPG QNQYREISSC SNFESFQARR 370 380 390 400 410 420 LQLRYRAEDG KPQLVHTLNG SGLAVGRTLV ALLENHQQAD GRIRIPAALR PYLGGMTVIQ A

References

[1]

"Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications." Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S. BMC Genomics 9:597-597(2008) [PubMed: 19077236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23270 / DSM 14882 / NCIB 8455.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001219 Genomic DNA. Translation: ACK80353.1.
RefSeq	YP_002424882.1. NC_011761.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B7J4C9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7136933.
GenomeReviews	Gene locus AFE_0380 in contig CP001219_GR.
KEGG	afr:AFE_0380.
PATRIC	20652097. VBIAciFer29821_0369.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG629391.
OMA	PKFADDM.
ProtClustDB	PRK05431.
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_ACIF2

Accession

Primary (citable) accession number: B7J4C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program