Reviewed, UniProtKB/Swiss-Prot Q5PAH7 (SYS_ANAMM)

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:	AM759

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

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. 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 – 429	429	Seryl-tRNA synthetase HAMAP MF_00176		PRO_0000121993
Regions
	Nucleotide binding	259 – 261	3	ATP By similarity
	Nucleotide binding	346 – 349	4	ATP By similarity
	Region	228 – 230	3	Serine binding By similarity
Sites
	Binding site	282	1	Serine By similarity
	Binding site	384	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PAH7-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 2C2275B41C1B7393	FASTA	429	48,312
	10 20 30 40 50 60 MHDIELIKKD PELFDRAMIS RGFGEQAEKI IELDLKKRGE LSTLYSLREQ RNAVTREVAL 70 80 90 100 110 120 LKRSGIECTP QIEASKKLAE EIATLEHSIK EDTKLSNLLE SLPNVPDPIV PVGKDESHNV 130 140 150 160 170 180 EVRSHGQRRD FAFGIRPHYE LGEMLNLLDF KRAAVLSGAR FSILKGQLAE LERALASFML 190 200 210 220 230 240 DMHTKEFGYT EISHPVLVNE RTMYNVGQLP KFHDDSFRTT NNFRLAPTSE VALANLVSGT 250 260 270 280 290 300 TLPRDSLPMR FTAYSQCFRA EAGSAGLDTR GMMRQHQFGK VELVSITTSD ASNAELERMT 310 320 330 340 350 360 SIAEEVLKRL ELPYRVMLLC SGDMGFSASI SYDLEVWMPA QDKYREISSC SNCRDFQARR 370 380 390 400 410 420 MGAKYFFFEN KKKHSTLVHT LNGSALAIGR TIAAIMENYQ NEDGSITIPD VLRKYTGASA IMRAEDALP

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86703.1. Different initiation.
RefSeq	YP_153958.2.
3D structure databases
SMR	Q5PAH7. Positions 1-421.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PAH7.
Genome annotation databases
GeneID	3171045.
GenomeReviews	Gene locus AM759 in contig CP000030_GR.
KEGG	ama:AM759.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	PKFADDM.
PhylomeDB	Q5PAH7.
Enzyme and pathway databases
BioCyc	AMAR234826:AM759-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_ANAMM

Accession

Primary (citable) accession number: Q5PAH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	May 1, 2007
Last modified:	February 9, 2010
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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