Reviewed, UniProtKB/Swiss-Prot Q82FK8 (SYS1_STRAW)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase 1
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase 1
    Serine--tRNA ligase 1
      Short name=SerRS 1

Gene names

Name:	serS1
Ordered Locus Names:	SAV_4244

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	425 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 – 425	425	Seryl-tRNA synthetase 1 HAMAP MF_00176		PRO_0000122129
Regions
	Nucleotide binding	261 – 263	3	ATP By similarity
	Nucleotide binding	348 – 351	4	ATP By similarity
	Region	230 – 232	3	Serine binding By similarity
Sites
	Binding site	277	1	ATP; via carbonyl oxygen and amide nitrogen By similarity
	Binding site	284	1	Serine By similarity
	Binding site	382	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82FK8-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: DB844977291DD51B	FASTA	425	47,242
	10 20 30 40 50 60 MIDLRLLRED PDRVRASQRA RGEDVALVDS LLSADERRRS SGVRFDELRS EQKALGKLIP 70 80 90 100 110 120 KASPEERAEL LKKAEQLKAD VKAADVEQHE ADEEAKRLLL QLGNLVHPDV PVGGEEDFVV 130 140 150 160 170 180 LETHGTIRDF GAEGFEPKDH LELGEALGAI DVERGAKVSG SRFYYLTGVG ALLELALVNA 190 200 210 220 230 240 AIAQATEAGF IPMLTPALVR PRAMEGTGFL GQASENVYHL EKDDYYLVGT SEVPLAAYHM 250 260 270 280 290 300 DEILDADKLP MRYAGFSPCF RREAGTYGKD TRGIFRVHQF DKVEMFSYVA PEDAENEHKR 310 320 330 340 350 360 LLEWEKQWLT GLELPFQVID VASGDLGASA TRKFDCEAWI PTQGKYRELT SASNCDSFQA 370 380 390 400 410 420 RRLSVRMRDG KKVQPLATLN GTLCAVPRTI VAILENHQLP DGSVRVPEML RPYLGGRELL EPVAK

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000030 Genomic DNA. Translation: BAC71956.1.
RefSeq	NP_825421.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1210915.
GenomeReviews	Gene locus SAV_4244 in contig BA000030_GR.
KEGG	sma:SAV_4244.
NMPDR	fig|227882.1.peg.4247.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q82FK8.
OMA	KNEAVFL.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV4244-MON.
BRENDA	6.1.1.11. 140873.
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

SYS1_STRAW

Accession

Primary (citable) accession number: Q82FK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 40 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)