Reviewed, UniProtKB/Swiss-Prot Q1RKF4 (SYS_RICBR)

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:	RBE_0079

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia

Protein attributes

Sequence length	426 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 – 426	426	Seryl-tRNA synthetase HAMAP MF_00176		PRO_0000278053
Regions
	Nucleotide binding	260 – 262	3	ATP By similarity
	Nucleotide binding	347 – 350	4	ATP By similarity
	Region	229 – 231	3	Serine binding By similarity
Sites
	Binding site	283	1	Serine By similarity
	Binding site	383	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RKF4-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 5F2DE56BB2F78081	FASTA	426	48,559
	10 20 30 40 50 60 MLNIKWIREN QELFDDKLRQ RFIEPMAKRI EELDGKKRKI TNLIQEFQHA RKVKSKILGN 70 80 90 100 110 120 INPKSGEEFE GLQRDVKDIN EKLEELEQDL NNNNELNELL NTLPNIPDEE VPYGIDESMN 130 140 150 160 170 180 KLIRTHGEVD LNAQNKKQHF ELGVKLDLMD FEQTAKISGA RFVTLKGDLA KLERALANFM 190 200 210 220 230 240 LDVHTGEFGF LEVSPPVLVR DNAMYNSGQL PKFADESFAT TNGYRLIPTA EVSLVNMVAD 250 260 270 280 290 300 TIIPREKLPM RLVAYTPCFR SEAGSSGRDT RGMIRLHQFS KVELVSITTP EESKNEHEYM 310 320 330 340 350 360 TNASETILQK LGLHYRTMLL CTGDMGFASQ KTYDIEVWLP GQKQYREIAS CSNCGDFQAR 370 380 390 400 410 420 RMKARYKEFG SHDTTLVHTL NASGLPIGRT MVAILENYQN EDGSITVPDV LVNYMGGLQK ITAYKE

References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed: 16703114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000087 Genomic DNA. Translation: ABE04160.1.
RefSeq	YP_537249.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RKF4.
Genome annotation databases
GeneID	3995070.
GenomeReviews	Gene locus RBE_0079 in contig CP000087_GR.
KEGG	rbe:RBE_0079.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1RKF4.
OMA	AHWDLGP
Enzyme and pathway databases
BioCyc	RBEL336407:RBE_0079-MON.
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. 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_RICBR

Accession

Primary (citable) accession number: Q1RKF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	May 16, 2006
Last modified:	November 24, 2009
This is version 27 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)