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A0RX10 (SYA_CENSY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:CENSYa_1254
OrganismCenarchaeum symbiosum (strain A)
Taxonomic identifier414004 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaCenarchaealesCenarchaeaceaeCenarchaeum

Protein attributes

Sequence length894 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 By similarity 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 – 894894Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347878

Sites

Metal binding5871Zinc By similarity
Metal binding5911Zinc By similarity
Metal binding6911Zinc By similarity
Metal binding6951Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RX10 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: A1438318B1D4878F

FASTA89497,118
        10         20         30         40         50         60 
MEKQEILREF SSDPEKYYTV RLFREEGFER RACSVCGRYF WALDGRPACP EDSDDTYSFI 

        70         80         90        100        110        120 
GDPPAPRAYD YAQAWRTIEE YFVKNGHESV PRYPVVCRWR DDLYFTIASI VDFQRVMGSS 

       130        140        150        160        170        180 
VVFEFPANPL VVPQTCLRFK DLENVGVTGR HFSSFCMIGQ HAVPGNGGYW KDECIDLDYG 

       190        200        210        220        230        240 
LLVRQLGIPK EEVVFVEDVW AGGGSFGPSL EYYVRGLELG NAVFTEFQGE LGNHTTLDRR 

       250        260        270        280        290        300 
IIDMGAGLER FAWITTGTPT AYDCCFGPVM GRLAESLGAD QDSAELAAYY TRVAVNLGRC 

       310        320        330        340        350        360 
GDLNEARRRS AQEAGISDSR MAGAIAPLGE AYMVADHIRT LIFAISDGAL PSNVGGGYNL 

       370        380        390        400        410        420 
RMMLRRVAGA MERTFPGLDL DELVDLHIDY LMGTYPELDG ARQDVKTILD IEASRYGDSK 

       430        440        450        460        470        480 
ERMGKITAKI TDRGRAPGVD ELVTLYESDG ITPEYLIEAG AIQEVPPEFY SRLDELHAPP 

       490        500        510        520        530        540 
PKAAGPGPEL AGLADTEMLF YGEDPPEFEA RVMHSSDGGV VLDRTSFYAR GGGQEPDHGT 

       550        560        570        580        590        600 
IGGFRVTDVS KHGGIILHRL DGGSLAEGST VRCIRDEKRR AGITRNHTST HILNASARGV 

       610        620        630        640        650        660 
LGSWVWQHSA FKEEDHARLD ITHHSPLSAA EVKKIEAAAN GIVKEDRGVS IGYHPRGEAE 

       670        680        690        700        710        720 
QKYGFRIYQG GVVPVSTVRI VTIKGYDDEA CGGTHVKSTG EVGLIRITRT KRIQDGVVRL 

       730        740        750        760        770        780 
EFVSGDAAIE HERTAAARAE GDRAAEEAKG RLQEERDAGR LKSREIIPGM LEEITGGGSA 

       790        800        810        820        830        840 
EGMEVATGPG GRRCLAAGIH DEYFHTSFGK KLVAMDPACA YCAIFEAGPT VRVLAYAGSK 

       850        860        870        880        890 
SGAGADEIVR EVSAVLGGSG GGAAGFAQGG GKDSSKMAEA VARARVLLFG GDNT 

« Hide

References

[1]"Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum symbiosum."
Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.
Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006) [PubMed: 17114289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DP000238 Genomic DNA. Translation: ABK77877.1.

3D structure databases

ProteinModelPortalA0RX10.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.

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.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 2 hits.
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.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_CENSY
AccessionPrimary (citable) accession number: A0RX10
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: January 9, 2007
Last modified: January 25, 2012
This is version 36 of the entry and version 1 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