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Q9UTB2 (SYSM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine--tRNA ligase, mitochondrial

EC=6.1.1.11
Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:dia4
ORF Names:SPAC25B8.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the attachment of serine to tRNA(Ser). Is also probably 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. UniProtKB Q9N0F3

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). UniProtKB Q9N0F3

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). UniProtKB Q9N0F3

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. UniProtKB Q9N0F3

Subunit structure

Homodimer. The tRNA molecule probably binds across the dimer By similarity. UniProtKB Q9N0F3

Subcellular location

Mitochondrion matrix Ref.2 UniProtKB Q9N0F3.

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. UniProtKB P0A8L1

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processseryl-tRNA aminoacylation

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Serine--tRNA ligase, mitochondrial
PRO_0000315879

Regions

Nucleotide binding292 – 2943ATP By similarity UniProtKB Q9N0F3
Nucleotide binding379 – 3824ATP By similarity UniProtKB Q9N0F3
Region262 – 2643Serine binding By similarity UniProtKB Q9N0F3

Sites

Binding site3151Serine By similarity UniProtKB Q9N0F3
Binding site4131Serine By similarity UniProtKB Q9N0F3

Sequences

Sequence LengthMass (Da)Tools
Q9UTB2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 80F2B923E6399565

FASTA45451,268
        10         20         30         40         50         60 
MSQLLYLRTF STHTSYLRSS WQAILNYKYI YQNAEAVQRN CINRNLQAIA ETVPKIRSLI 

        70         80         90        100        110        120 
DEKESLKNEF FPLLSLKKEI TLQIERCSDP NERGKLVNEA KGLKKKTEEY NKIISKVTND 

       130        140        150        160        170        180 
LYQYCLAVPN TTLPTVPVGP EDKAVVVQKI GSPLVKKTGS LKDHLQIANE GINLEDAAQA 

       190        200        210        220        230        240 
SGHSFCYTTG DIALLEMAIT NYAMDFAISK GWCPVIPPTI VRTDIALACG FQPRDEEGQQ 

       250        260        270        280        290        300 
IYELDSYTSP LVSSPKQCLI GTAEISLAAL GFKKTFNNFT ERKVVGVSRA YRREAGARGK 

       310        320        330        340        350        360 
ENRGLYRLHE FTKVELFAWT HPSRSSEMFN EIVNFQKEFV ETLKIPARIL NMPTAELGSS 

       370        380        390        400        410        420 
ASQKYDIEAW MPARQSYGEI TSASNCLEYQ ARRLLTRYRN DKDSGFVHTL NGTAAAIPRL 

       430        440        450 
IIAILENHQQ EDGTVKVPET LVPYIHKEYL FKAK 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB61772.1.
PIRT50193.
RefSeqNP_594466.1. NM_001019895.1.

3D structure databases

HSSPHSSP built from PDB template 1WLE based on UniProtKB Q9N0F3.
ProteinModelPortalQ9UTB2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9UTB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2541567.
GenomeReviewsGene locus dia4 in contig CU329670_GR.
KEGGspo:SPAC25B8.06c.
NMPDRfig|4896.1.peg.4436.

Organism-specific databases

GeneDB_SpombeSPAC25B8.06c.

Phylogenomic databases

eggNOGfuNOG06563.
GeneTreeEFGT00050000004865.
HOGENOMHBG629391.
OMAIRHRIER.
OrthoDBEOG42FWSM.

Gene expression databases

ArrayExpressQ9UTB2.

Family and domain databases

InterProIPR002314. 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]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KOK01875.
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. SerS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYSM_SCHPO
AccessionPrimary (citable) accession number: Q9UTB2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families