Q68VW6 (SYS_RICTY) 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:	RT0770

Organism

Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]

Taxonomic identifier

257363 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › Rickettsia typhi

Protein attributes

Sequence length	425 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-Rule MF_00176
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP-Rule 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. HAMAP-Rule 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 selenocysteinyl-tRNA(Sec) biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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 – 425	425	Serine--tRNA ligase HAMAP-Rule MF_00176		PRO_0000122111
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	382	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q68VW6 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: E5347E965510EDA5	FASTA	425	48,674
	10 20 30 40 50 60 MLNIKWIREN QELFDEKLSQ RFIEPMSSKI AMLDREKRKI TSLIQEFQHA RKVKSKILGN 70 80 90 100 110 120 MVSKSGEEFE ELQRDVNHIN EKLEELEQTL DNNNELNELL NMLPNIPDEE VPYGIDESMN 130 140 150 160 170 180 KLVRSYGNTN KNALNKQHFE LGTKLNLMDF EQTAKISGSR FVTLKGDLAK LERALINFMV 190 200 210 220 230 240 DIHTKEFDFF EISPPLLVRD SAMYNAGQLP KFSEESFITT NGYRLIPTAE VSLVNIVADT 250 260 270 280 290 300 IIQREKLPMR YVAYTTCFRS EAGSSGRDTR GMIRLHQFGK VELVSITTPE ESKNEHEYIT 310 320 330 340 350 360 NASETILKKL DLPYRVMLLC TGDMGFAAKK TYDIEVWLPG QNQYREIASC SNCGDFQARR 370 380 390 400 410 420 MKARYKEFGS NETTLVHTLN ASGLPIGRTI VAILENYQNN DGSITIPDVL INYMGGLKKI TTYSE

References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. , Hong C., Yu X.-J., Walker D.H., Weinstock G.M. J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017197 Genomic DNA. Translation: AAU04226.1.
RefSeq	YP_067708.1. NC_006142.1.
3D structure databases
ProteinModelPortal	Q68VW6.
ModBase	Search...
Protein-protein interaction databases
STRING	257363.RT0770.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU04226; AAU04226; RT0770.
GeneID	2959021.
KEGG	rty:RT0770.
PATRIC	17910794. VBIRicTyp34752_0790.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0172.
HOGENOM	HOG000035938.
KO	K01875.
OMA	GPIRYAG.
ProtClustDB	PRK05431.
Enzyme and pathway databases
BioCyc	RTYP257363:GJEQ-810-MONOMER.
UniPathway	UPA00906; UER00895.
Family and domain databases
Gene3D	1.10.287.40. 1 hit.
HAMAP	MF_00176. Ser_tRNA_synth_type1.
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-ligase_type_1. IPR015866. Ser-tRNA-synth_1_N. IPR010978. tRNA-bd_arm. [Graphical view]
PANTHER	PTHR11778. PTHR11778. 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_RICTY

Accession

Primary (citable) accession number: Q68VW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program