Q1LTE8 (SYS_BAUCH) 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:	BCI_0318

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	430 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 – 430	430	Serine--tRNA ligase HAMAP MF_00176		PRO_1000019618
Regions
	Nucleotide binding	268 – 270	3	ATP By similarity
	Nucleotide binding	355 – 358	4	ATP By similarity
	Region	237 – 239	3	Serine binding By similarity
Sites
	Binding site	291	1	Serine By similarity
	Binding site	391	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LTE8 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 90A8E0735E80F9E5	FASTA	430	49,484
	10 20 30 40 50 60 MLDPYLLRHD IKIVAKKLAS KNFLLAVDKV NQQEALRKQL QIKKEHLQFI RKSKSRIVNL 70 80 90 100 110 120 AKANGENITI LCQEINQINE QLKQTKSELS SLKQLINDYM LLLPNIPADD VPYGSDKKDN 130 140 150 160 170 180 IEIKRWGEPR KYNFPIKDHV NLGYITGNID FTAGVKLAGT RFVVIRGQIA RLYRALSQFM 190 200 210 220 230 240 LDLHTQQHGY EEYYLPYLVN RTSLYGTGHL PKFYEDLFHI QSINKENISN IYTLIPTAEV 250 260 270 280 290 300 PLINLLRDKI FDENILPLKM TANTPCFRAE AGSYGRDTHG LIRMHQFDKV EMVQAIKPEH 310 320 330 340 350 360 SMIALEEMTK HAEKVLQLLN LHYRKVLLCT GDTGFASSKT YDLEVWLPSQ NIYCEVSSCS 370 380 390 400 410 420 NTSDFQTRRV LARYRNKKDK QLRFLHTING SGLAIGRTLI AILENYQLAD GRIEVPKSLR 430 SYMQGLTILG

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF14125.1.
RefSeq	YP_588766.1. NC_007984.1.
3D structure databases
ProteinModelPortal	Q1LTE8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LTE8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056311.
GenomeReviews	Gene locus BCI_0318 in contig CP000238_GR.
KEGG	bci:BCI_0318.
PATRIC	21074143. VBIBauCic75062_0305.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HBG629391.
OMA	HTKPLEE.
PhylomeDB	Q1LTE8.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0318-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_BAUCH

Accession

Primary (citable) accession number: Q1LTE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program