Reviewed, UniProtKB/Swiss-Prot Q3MCE0 (SYS_ANAVT)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS

Gene names

Name:	serS
Ordered Locus Names:	Ava_1724

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

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 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. HAMAP MF_00176
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	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP 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	Seryl-tRNA synthetase HAMAP MF_00176		PRO_1000019610
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)
	Q3MCE0-1 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: D9F2509398315C22	FASTA	426	47,740
	10 20 30 40 50 60 MLDIKQIREN PQLIQERLNS RSGTYDIQPI LQLDKQQREL EATRSQIQAR SNEIGKIVGQ 70 80 90 100 110 120 KIKSGINPQD PEIQALRDEG NSIKAQLSEL EPREKELKAE IEQLILALPN LPSDSTPIGK 130 140 150 160 170 180 SEEENVEVRR WGDEYLPQNP NIIPHWEIGE KLGILNFERA VKVAQSRFVN LIGAGAALER 190 200 210 220 230 240 ALINFMLKTQ TVAGYVEVSP PLLVNTDSLT GTGQLPKFAE ESFKCADDEL WLIPTAEVPV 250 260 270 280 290 300 TNLYRGEILA AENLPIYHCA YTPCFRREAG SYGRDMRGLI RLHQFNKVEL VKVVHPSTSF 310 320 330 340 350 360 DELEKLVGNA EAILQALKLP YRVINLCTGD LGFGATKTYD LEVWLPSSGK YREISSCSNC 370 380 390 400 410 420 FDFQARRADI RFKEAGKKGT QFVHTLNGSG LAVGRTMAAI LENYQQPDGT ILIPEVLQVY LGREVL

References

[1]

"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000117 Genomic DNA. Translation: ABA21346.1.
RefSeq	YP_322241.1.
3D structure databases
HSSP	HSSP built from PDB template 1WLE based on UniProtKB Q9N0F3.
SMR	Q3MCE0. Positions 1-426.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3MCE0.
Genome annotation databases
GeneID	3682145.
GenomeReviews	Gene locus Ava_1724 in contig CP000117_GR.
KEGG	ava:Ava_1724.
NMPDR	fig|240292.3.peg.2804.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	PKFADDM.
PhylomeDB	Q3MCE0.
Enzyme and pathway databases
BioCyc	AVAR240292:AVA_1724-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_cons-dom. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. 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.
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.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_ANAVT

Accession

Primary (citable) accession number: Q3MCE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 25, 2005
Last modified:	February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)