Reviewed, UniProtKB/Swiss-Prot Q2NIJ4 (SYS_AYWBP)

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:	AYWB_632

Organism

Aster yellows witches'-broom phytoplasma (strain AYWB) [Complete proteome] [HAMAP]

Taxonomic identifier

322098 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Candidatus Phytoplasma › Candidatus Phytoplasma asteris

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
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 – 424	424	Seryl-tRNA synthetase HAMAP MF_00176		PRO_1000019613
Regions
	Nucleotide binding	263 – 265	3	ATP By similarity
	Nucleotide binding	350 – 353	4	ATP By similarity
	Region	232 – 234	3	Serine binding By similarity
Sites
	Binding site	286	1	Serine By similarity
	Binding site	386	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2NIJ4-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: DBC2937B3A681216	FASTA	424	48,749
	10 20 30 40 50 60 MLDLNFVVQN LPSVIAKLEK RQQSFAYLNK LPLLAQQRKS LLLQIQNLRS QKNQSAKKVA 70 80 90 100 110 120 QKANAKEDIA LFLQENNFLR DDLQKLEQKL KLQEQEIFDI LSITPNLPHD SLPIGTDDKD 130 140 150 160 170 180 NKELYCEGQI RTFPFTPKDH VYLAEKLDIL DFKRASKISG SGFVVCKGLG ARLERALIQF 190 200 210 220 230 240 MMDLHSKKGY QEIIPPYIIN EKSMFATGQL PKFEDEVYKL YNSKNNWYLN PTAEVPTINL 250 260 270 280 290 300 HREEIFKPGT LPIKYVSYTT AFRQEAGSAG KDTRGIFRQH QFNKVELIQF CHPQNSYEYL 310 320 330 340 350 360 EQMLKDSEEI LKLLKLPYRV VLLSTGDLGF SMSKTYDLEV FLPSYNCYRE IGSISNSCDF 370 380 390 400 410 420 QARRANIKMK NPKNNKNEYV HILNGSGLAV GRTVIAILEN YQNQDGTITV PEILQSYLGT DIIK

References

[1]

"Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts." Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A. J. Bacteriol. 188:3682-3696(2006) [PubMed: 16672622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000061 Genomic DNA. Translation: ABC65749.1.
RefSeq	YP_456828.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3865699.
GenomeReviews	Gene locus AYWB_632 in contig CP000061_GR.
KEGG	ayw:AYWB_632.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2NIJ4.
OMA	Q2NIJ4. LKPYMGG.
Family and domain databases
HAMAP	MF_00176. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [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_AYWBP

Accession

Primary (citable) accession number: Q2NIJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 7, 2006
Last modified:	June 16, 2009
This is version 31 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)