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Protein

Alanine--tRNA ligase

Gene

ala1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi606 – 6061ZincUniRule annotation
Metal bindingi610 – 6101ZincUniRule annotation
Metal bindingi725 – 7251ZincUniRule annotation
Metal bindingi729 – 7291ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligaseUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:ala1
Synonyms:ars1
ORF Names:SPAC23C11.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC23C11.09.
PomBaseiSPAC23C11.09. ala1.

Subcellular locationi

  • Mitochondrion UniRule annotation
  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 959959Alanine--tRNA ligasePRO_0000075286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei389 – 3891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO13914.

PTM databases

iPTMnetiO13914.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi278513. 4 interactions.
MINTiMINT-4668946.

Structurei

3D structure databases

ProteinModelPortaliO13914.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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.UniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000156964.
InParanoidiO13914.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG799302.
PhylomeDBiO13914.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAESEVVNW PANEIRRTFL KYFEDHGHTI VPSSSVIPYD DPTLLFANAG
60 70 80 90 100
MNQFKPIFLG TVDPSSDFAK LKRACDSQKC IRAGGKHNDL EDVGKDNYHH
110 120 130 140 150
TMFEMLGNWS FGDYFKKEAI AMAWDLLTNV YGLKKDQLYV TYFGGHEESG
160 170 180 190 200
LEPDLEARQL WLDIGIDESR VIPGSLKDNF WEMGDQGPCG PCSEIHYDRI
210 220 230 240 250
GNRTVPELVN MDDPNVLEIW NIVFIQFNRE KDGSLRPLPN RHVDTGMGFE
260 270 280 290 300
RLVSVIQNKT SNYDTDVFSP IFAKIQELTN ARPYTGKMGD EDVDGIDTAY
310 320 330 340 350
RVVADHVRTL TFAISDGGVP NNEGRGYVLR RILRRGARYV RKKFGVPIGN
360 370 380 390 400
FFSRLSLTVV EQMGDFFPEL KRKVDDVREL LDEEEESFSR TLDRGEKMFE
410 420 430 440 450
QYAAAAKKTP SKTLQGNDVW RLYETYGFPV DLTHLMAEEA GIKIDEPGFE
460 470 480 490 500
AAQARSKEIS KQASKGGSSG DDLLVLDVHA LGALSKMDDI PETDDVFKHN
510 520 530 540 550
SVSLKSVIKG IYHKGGFQKS TEGFNSGEQL GLLLDRTNFY AEQGGQEYDT
560 570 580 590 600
GHIVIDGVAD FRVTNVQVYA GYVLHTGFLE YGNLTVNDSV VCEYDEIRRW
610 620 630 640 650
HLMNNHTVTH ILNLALRNTL GDGIDQRGSL VSQEKLRFDF SYKSSIPIDK
660 670 680 690 700
LLLVENYCNN VIQDNLSVYS KEVALSKAKE INGLRAVFGE VYPDPVRVVC
710 720 730 740 750
IGVDIDTLLQ EPKKPDWTKY SIEFCGGTHC DKSGEIKDFV ILEENGIAKG
760 770 780 790 800
IRRIVAVTST EANRVSRLAN EFDARIAKLE KMPFSPAKEA ELKKISVDLS
810 820 830 840 850
KLVVAAVRKH AMKERIAKIT KQVQEHVKAI NAAEQKEVVN VVTEYFKENP
860 870 880 890 900
DMSFVVAKVP ISANPKALSF ALTYAKKNLK DKSIYLLASD DTKVAHACLV
910 920 930 940 950
SPEAMKKLTP QEWSQKVCHS IGGRSGGKGD TCQGVGDKPL SIDVAVEEAI

EFFQGKLTI
Length:959
Mass (Da):107,377
Last modified:January 1, 1998 - v1
Checksum:i9F2E4A7275D86FB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11162.1.
PIRiT38247.
RefSeqiNP_593640.1. NM_001019071.2.

Genome annotation databases

EnsemblFungiiSPAC23C11.09.1; SPAC23C11.09.1:pep; SPAC23C11.09.
GeneIDi2542031.
KEGGispo:SPAC23C11.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11162.1.
PIRiT38247.
RefSeqiNP_593640.1. NM_001019071.2.

3D structure databases

ProteinModelPortaliO13914.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278513. 4 interactions.
MINTiMINT-4668946.

PTM databases

iPTMnetiO13914.

Proteomic databases

MaxQBiO13914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23C11.09.1; SPAC23C11.09.1:pep; SPAC23C11.09.
GeneIDi2542031.
KEGGispo:SPAC23C11.09.

Organism-specific databases

EuPathDBiFungiDB:SPAC23C11.09.
PomBaseiSPAC23C11.09. ala1.

Phylogenomic databases

HOGENOMiHOG000156964.
InParanoidiO13914.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG799302.
PhylomeDBiO13914.

Miscellaneous databases

NextBioi20803109.
PROiO13914.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSYA_SCHPO
AccessioniPrimary (citable) accession number: O13914
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.