A4SNK6 (SYS_AERS4) 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:	ASA_2435

Organism

Aeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]

Taxonomic identifier

382245 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	431 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 – 431	431	Serine--tRNA ligase HAMAP MF_00176		PRO_1000019605
Regions
	Nucleotide binding	271 – 273	3	ATP By similarity
	Nucleotide binding	358 – 361	4	ATP By similarity
	Region	240 – 242	3	Serine binding By similarity
Sites
	Binding site	294	1	Serine By similarity
	Binding site	392	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4SNK6 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 39382CFE5161015B	FASTA	431	48,177
	10 20 30 40 50 60 MLDPKYLRSE IDEAAARLAT RGYVLDVAAV NALEEKRKDL QSRTQELQAE RNARSKSIGE 70 80 90 100 110 120 AARRGEDVAP LKAEVTKIND ELETSKIELD ALLTEIKSIS DAIPNLPSET TPVGRDENDN 130 140 150 160 170 180 VEVRRWGTPR QFTFPVRDHI DLGEAAKGVD FKNGVKLSGA RFVVMKGQIA RLHRALAQFM 190 200 210 220 230 240 LDLHTLQHGY TECYVPYLVN PDSLYGTGQL PKFSQDLFNT GIEGEGEDEG KMRKFSLIPT 250 260 270 280 290 300 SEVPLTNMAR DEIFDEQELP IKMTAHSPCF RSEAGSYGRD TRGLIRMHQF DKVEMVQLVH 310 320 330 340 350 360 PEKSWEALEE MAGHAEKVLQ LLELPYRVMA LATGDMGFCA AKTYDLEVWL PAQNTYREIS 370 380 390 400 410 420 SVSNCTDFQA RRMQARVRID GKPQLLHTLN GSGLAVGRTL VAVIENYQQE DGRIAIPAAL 430 QSYMGGLTHI G

References

[1]

"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen." Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L. BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: A449.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000644 Genomic DNA. Translation: ABO90478.1.
RefSeq	YP_001142226.1. NC_009348.1.
3D structure databases
ProteinModelPortal	A4SNK6.
SMR	A4SNK6. Positions 1-426.
ModBase	Search...
Protein-protein interaction databases
STRING	A4SNK6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4995409.
GenomeReviews	Gene locus ASA_2435 in contig CP000644_GR.
KEGG	asa:ASA_2435.
PATRIC	20791230. VBIAerSal2987_2399.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	PKFADDM.
PhylomeDB	A4SNK6.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	ASAL382245:ASA_2435-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_AERS4

Accession

Primary (citable) accession number: A4SNK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 15, 2007
Last modified:	January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program