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O13914 (SYA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase
EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:ala1
ORF Names:SPAC23C11.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length959 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain By similarity.

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).

Cofactor

Binds 1 zinc ion per subunit Potential.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion By similarity. Cytoplasm By similarity.

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 959959Alanine--tRNA ligase
PRO_0000075286

Sites

Metal binding6061Zinc Potential
Metal binding6101Zinc Potential
Metal binding7251Zinc Potential
Metal binding7291Zinc Potential

Amino acid modifications

Modified residue3891Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
O13914 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9F2E4A7275D86FB6

FASTA959107,377
        10         20         30         40         50         60 
MTAESEVVNW PANEIRRTFL KYFEDHGHTI VPSSSVIPYD DPTLLFANAG MNQFKPIFLG 

        70         80         90        100        110        120 
TVDPSSDFAK LKRACDSQKC IRAGGKHNDL EDVGKDNYHH TMFEMLGNWS FGDYFKKEAI 

       130        140        150        160        170        180 
AMAWDLLTNV YGLKKDQLYV TYFGGHEESG LEPDLEARQL WLDIGIDESR VIPGSLKDNF 

       190        200        210        220        230        240 
WEMGDQGPCG PCSEIHYDRI GNRTVPELVN MDDPNVLEIW NIVFIQFNRE KDGSLRPLPN 

       250        260        270        280        290        300 
RHVDTGMGFE RLVSVIQNKT SNYDTDVFSP IFAKIQELTN ARPYTGKMGD EDVDGIDTAY 

       310        320        330        340        350        360 
RVVADHVRTL TFAISDGGVP NNEGRGYVLR RILRRGARYV RKKFGVPIGN FFSRLSLTVV 

       370        380        390        400        410        420 
EQMGDFFPEL KRKVDDVREL LDEEEESFSR TLDRGEKMFE QYAAAAKKTP SKTLQGNDVW 

       430        440        450        460        470        480 
RLYETYGFPV DLTHLMAEEA GIKIDEPGFE AAQARSKEIS KQASKGGSSG DDLLVLDVHA 

       490        500        510        520        530        540 
LGALSKMDDI PETDDVFKHN SVSLKSVIKG IYHKGGFQKS TEGFNSGEQL GLLLDRTNFY 

       550        560        570        580        590        600 
AEQGGQEYDT GHIVIDGVAD FRVTNVQVYA GYVLHTGFLE YGNLTVNDSV VCEYDEIRRW 

       610        620        630        640        650        660 
HLMNNHTVTH ILNLALRNTL GDGIDQRGSL VSQEKLRFDF SYKSSIPIDK LLLVENYCNN 

       670        680        690        700        710        720 
VIQDNLSVYS KEVALSKAKE INGLRAVFGE VYPDPVRVVC IGVDIDTLLQ EPKKPDWTKY 

       730        740        750        760        770        780 
SIEFCGGTHC DKSGEIKDFV ILEENGIAKG IRRIVAVTST EANRVSRLAN EFDARIAKLE 

       790        800        810        820        830        840 
KMPFSPAKEA ELKKISVDLS KLVVAAVRKH AMKERIAKIT KQVQEHVKAI NAAEQKEVVN 

       850        860        870        880        890        900 
VVTEYFKENP DMSFVVAKVP ISANPKALSF ALTYAKKNLK DKSIYLLASD DTKVAHACLV 

       910        920        930        940        950 
SPEAMKKLTP QEWSQKVCHS IGGRSGGKGD TCQGVGDKPL SIDVAVEEAI EFFQGKLTI

« 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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB11162.1.
PIRT38247.
RefSeqNP_593640.1. NM_001019071.1.

3D structure databases

ProteinModelPortalO13914.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC23C11.09.1; SPAC23C11.09.1:pep; SPAC23C11.09.
GeneID2542031.
GenomeReviewsGene locus ala1 in contig CU329670_GR.
KEGGspo:SPAC23C11.09.
NMPDRfig|4896.1.peg.3610.

Organism-specific databases

GeneDB_SpombeSPAC23C11.09.

Phylogenomic databases

eggNOGfuNOG06017.
GeneTreeEFGT00050000005609.
HOGENOMHBG354397.
OMAVILEMES.
OrthoDBEOG44BF9B.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001309-MONOMER.

Gene expression databases

ArrayExpressO13914.

Family and domain databases

InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_synth_euk/bac.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_SCHPO
AccessionPrimary (citable) accession number: O13914
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 82 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents