Serine--tRNA ligase, mitochondrial - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38705 (SYSM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine--tRNA ligase, mitochondrial
EC=6.1.1.11

Alternative name(s):
Digs into agar protein 4
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase

Gene names

Name:	DIA4
Ordered Locus Names:	YHR011W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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). ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Mitochondrion matrix Ref.4.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
Miscellaneous	Present with 405 molecules/cell in log phase SD medium. Ref.5
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	Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	invasive growth in response to glucose limitation Inferred from genetic interaction. Source: SGD mitochondrial seryl-tRNA aminoacylation Inferred from genetic interaction. Source: SGD pseudohyphal growth Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-tRNA ligase activity Inferred from genetic interaction. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 446

446

Serine--tRNA ligase, mitochondrial

PRO_0000122200

Regions

Nucleotide binding

284 – 286

ATP By similarity

Nucleotide binding

371 – 374

ATP By similarity

Region

251 – 253

Serine binding By similarity

Sites

Binding site

300

ATP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

307

Serine By similarity

Binding site

407

Serine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P38705 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 2C0AE2CB644E7C54
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FASTA

446

50,390

        10         20         30         40         50         60 
MIIRRLFSIS NRSFFLKKPQ FDVKKIIEMI PQYQTSIQNR ELIEADSIIR SLQLLGERYQ 

        70         80         90        100        110        120 
NIKEIDKVIA DIQIQRKSIE AQIKKDKTKI TEYSAALKAL KEQYNDQNSK SSELKKKILE 

       130        140        150        160        170        180 
TCKSLPNTLD PTVPLDAPQI EQWINPLKTH KTSEAQAHVD IMLKKNMLDL QTASNVTGMS 

       190        200        210        220        230        240 
WYYLLNDGAR LEQALVAYAL KKANENGFSS CVPPSITKKE LIDACGFNPR DMNNERQIYA 

       250        260        270        280        290        300 
LQDTNLGLVA TAEIPLAGLG ANKVLELNSG ECSKKLVGVS RCYRAEAGAR GKDTKGLYRV 

       310        320        330        340        350        360 
HEFTKVELFC WSKPETSAKV LEEIKQFQIS VVEELGIPAK VLNMPSNDLG NPAFKKYDIE 

       370        380        390        400        410        420 
AWMPGRGKFG EISSASNCTD FQSRRLNTKY RDDNTGKLEY VHTLNGTAMA IPRVIVALVE 

       430        440 
NFYDPSTGKI SVPECLREFM NGQRYI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U10400 Genomic DNA. Translation: AAB68940.1. AY558105 Genomic DNA. Translation: AAS56431.1. BK006934 Genomic DNA. Translation: DAA06700.1.
PIR	S46786.
RefSeq	NP_011875.1. NM_001179141.1.
3D structure databases
ProteinModelPortal	P38705.
SMR	P38705. Positions 20-446.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5573N.
IntAct	P38705. 5 interactions.
MINT	MINT-534407.
STRING	P38705.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR011W; YHR011W; YHR011W.
GeneID	856402.
KEGG	sce:YHR011W.
NMPDR	fig\|4932.3.peg.3020.
Organism-specific databases
CYGD	YHR011w.
SGD	S000001053. DIA4.
Phylogenomic databases
eggNOG	fuNOG06563.
GeneTree	EFGT00050000004865.
HOGENOM	HBG629391.
OMA	SEIVHAC.
OrthoDB	EOG42FWSM.
Gene expression databases
ArrayExpress	P38705.
Genevestigator	P38705.
GermOnline	YHR011W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-synth_IIa. IPR010978. tRNA-bd_arm. [Graphical view]
KO	K01875.
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	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...
Other
NextBio	981937.

Entry information

Entry name

SYSM_YEAST

Accession

Primary (citable) accession number: P38705
Secondary accession number(s): D3DKV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program