A6VNC3 (SYS_ACTSZ) 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:	Asuc_1104

Organism

Actinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]

Taxonomic identifier

339671 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	429 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 – 429	429	Serine--tRNA ligase HAMAP MF_00176		PRO_1000071630
Regions
	Nucleotide binding	266 – 268	3	ATP By similarity
	Nucleotide binding	353 – 356	4	ATP By similarity
	Region	235 – 237	3	Serine binding By similarity
Sites
	Binding site	289	1	Serine By similarity
	Binding site	389	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6VNC3 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 58E33F01F3C22073	FASTA	429	48,299
	10 20 30 40 50 60 MIDPNLLRNN LEETAQKLKE KRNFILDVKQ LRKLEEQRKA LQVKTETLQA ERNLRSKAIG 70 80 90 100 110 120 AAKARGENIE SLLNEVDHLG IELAQAKALF DDVSAELNTI LLTIPNIPAD EVPQGKDDTE 130 140 150 160 170 180 NQEVARWGTP RTFDFEVKDH VTLGENIDGL DFSAGVKLSG ARFAVMKGRI AKLHRALAQF 190 200 210 220 230 240 MLDLHTEKHG YLETYVPYLV NHTTLYGTGQ LPKFGEDLFH TKALEGEQPY ALIPTAEVPV 250 260 270 280 290 300 TNLVRDEILS VENLPLKMTA HTPCFRSEAG SYGRDTRGLI RMHQFDKVEM VQIVEPEKSM 310 320 330 340 350 360 EALEELTGHA EEVLRLLNLP YRKVLLCSGD MGFGACKTYD LEVWLPAQNT YREISSCSNM 370 380 390 400 410 420 WDFQARRMQA RCRAKGDKKT RLVHTLNGSG LAVGRTLVAV LENYQNADGS ITVPEVLRPY MDNVDTIGR

References

[1]

"Complete sequence of Actinobacillus succinogenes 130Z." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000746 Genomic DNA. Translation: ABR74470.1.
RefSeq	YP_001344405.1. NC_009655.1.
3D structure databases
ProteinModelPortal	A6VNC3.
SMR	A6VNC3. Positions 1-428.
ModBase	Search...
Protein-protein interaction databases
STRING	A6VNC3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5349717.
GenomeReviews	Gene locus Asuc_1104 in contig CP000746_GR.
KEGG	asu:Asuc_1104.
PATRIC	20760582. VBIActSuc117883_1170.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	ERSIINY.
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_ACTSZ

Accession

Primary (citable) accession number: A6VNC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program