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P96041 (SYA_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Alanine--tRNA ligase

EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:SSO0341
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length900 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm HAMAP MF_00036_A.

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. HAMAP MF_00036_A

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 900900Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075277

Sites

Metal binding6041Zinc By similarity
Metal binding6081Zinc By similarity
Metal binding7081Zinc By similarity
Metal binding7121Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P96041 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 6CB15A31210E153F

FASTA900102,980
        10         20         30         40         50         60 
MKASEEEYKL NFFIKNDFKR KICKSCQTPF WTKDDKKEYC SDIPCTDYYF FDINIKSQPL 

        70         80         90        100        110        120 
TVKEAREKFL SFFEKRGHTR IPPKPVLARW REDLYLTIAS IVDFQPHVTS GLVPPPANPL 

       130        140        150        160        170        180 
VVSQPSIRLE DIDNVGVTFG RHLTTFEMAA HHAFNYPDRY VYWKDETTAY ATEFFTKELG 

       190        200        210        220        230        240 
IPEEELNFKE SWWEGGGNAG PCLEVTVGGL ELATLVFMQY KITDNGDYIP LKLKIVDTGY 

       250        260        270        280        290        300 
GVERIAWVTQ KTPSAFHAIY GNLVYKFFDK IGVAYIDETL LKVASRFAGK IDPDNPDTIK 

       310        320        330        340        350        360 
IHRQMVSKEL GIDIKNVEEE LDRAAKVFQI LDHTKTIMLM LADGLVPSNS GEGYLGRLVI 

       370        380        390        400        410        420 
RRALKVLRLL KSDVRLYELV KEQIGFWKED FPQVLKNKDY ILDAVELEQQ RFEKILEKVP 

       430        440        450        460        470        480 
SIASTLARKS EITTEDLIQV YDSNGVPPDL LEEELKKKRV KFELPRNFYA LVAKRHQTST 

       490        500        510        520        530        540 
IKNVYDKVKL PKDLLEYITT LQPTEKLYYK DQYMRSFEGK VLGIYKNYLI LDKTTFYPEG 

       550        560        570        580        590        600 
GGQLGDTGLI IDEKSSKRYE VVDTQKVNDV IIHVLKEEPS TIKVGDNVRG EINWERRYRL 

       610        620        630        640        650        660 
MRHHTVTHVI LAAAKKVLGD HIWQAGAEKT PEKGRLDITH HKALTEEEVK LIENYANSVI 

       670        680        690        700        710        720 
SDRRPVKPLE MNRMEAEMKY GVSIYEGGVP NSATIRLLEI KDWDIESCGG THVSNTSEIG 

       730        740        750        760        770        780 
AVKIINVERI QDGIIRLEYV AGPALVDYIR ETEAKIAEAS KIIGTSPDQL PSRLRRILNE 

       790        800        810        820        830        840 
VEKKNNLIIQ YRRIVETELL NSLKPYEING NKIYIIEGLN DEEENKEILR KLTSTDNTIA 

       850        860        870        880        890        900 
ISISDNRLQI ATSKNMRVDK IVEELLKGGG KGGGKGTFAN VILSSKKSKE EIIDIVRKSL 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"Nucleotide sequence of a gene cluster encoding NusG and the L11-L1-L10-L12 ribosomal proteins from the thermophilic archaeon Sulfolobus solfataricus."
Geiger M., Groebner P., Piendl W.
Biochim. Biophys. Acta 1340:170-177(1997) [PubMed: 9252104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006641 Genomic DNA. Translation: AAK40671.1.
U85262 Genomic DNA. Translation: AAB99528.1.
PIRH90176.
RefSeqNP_341881.1. NC_002754.1.

3D structure databases

ProteinModelPortalP96041.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1455481.
GenomeReviewsGene locus SSO0341 in contig AE006641_GR.
KEGGsso:SSO0341.
NMPDRfig|273057.1.peg.304.

Phylogenomic databases

HOGENOMHBG392147.
OMAGESKTDQ.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycSSOL273057:SSO0341-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR022429. Ala-tRNA_synth_arc.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PfamPF01411. 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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_SULSO
AccessionPrimary (citable) accession number: P96041
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families