Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1XP68 (SYA_SYNP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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
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:SYNPCC7002_A1672
OrganismSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]
Taxonomic identifier32049 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length877 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_B

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_B.

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_B

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 877877Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347836

Sites

Metal binding5621Zinc Potential
Metal binding5661Zinc Potential
Metal binding6641Zinc Potential
Metal binding6681Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B1XP68 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: ED2711BD98501FD2

FASTA87796,883
        10         20         30         40         50         60 
MSSVPPVLSG SEIRSKFLEF FNQRQHPILP SASLVPEDPT VLLTIAGMLP FKPIFLGQQD 

        70         80         90        100        110        120 
APSPRATTSQ KCIRTNDIEN VGRTARHHTF FEMLGNFSFG DYFKEQAIAW AWELSTEVFQ 

       130        140        150        160        170        180 
LDPKNIVVSV FREDDEAFEI WRDKVGVNPK RIIRMGEEDN FWKSGPTGPC GPCSELYYDF 

       190        200        210        220        230        240 
KPELGDDNID LEDDTRFIEY YNLVFMQYNR DAEGHLTPLQ NKNIDTGMGL ERMAQILQQV 

       250        260        270        280        290        300 
PNNYETDLIF PIIETAAKAA GIHYEKADEK TKVSLKVIGD HVRSVVHMIA DGITASNTDR 

       310        320        330        340        350        360 
GYVLRRLIRR VVRHGRLIGI DGNFINQVAE TAIQLSEAAY PNTRERESFI KQELEREENN 

       370        380        390        400        410        420 
FLKTLERGEK LLADIIAKEE KQISGVDAFT LFDTFGFPFE LTQEIAEENG LTVDAEGYQA 

       430        440        450        460        470        480 
EMKKQQERSK AAHETIDLTV QGSLDELAEH IHPTAFLGYT DLQSQVKIEA VLVDGHRVET 

       490        500        510        520        530        540 
AEAGVVVQLI CNQTPFYAES GGQIGDRGYF SGDQLVVRIN DVQKESGFFV HHGKVERGSL 

       550        560        570        580        590        600 
TVGDTVNATI DRACRRRAQA NHTATHLLQA ALKNIVDDSI SQAGSLVDFD RLRFDFNCPR 

       610        620        630        640        650        660 
ALTAAELTQI EAQINTWIAE AHEGQVAVMP IAEAKAKGAV AMFGEKYGEE VRVVDFPGVS 

       670        680        690        700        710        720 
MELCGGTHVK NTAEIGLFKI ISETGISSGI RRIEAVAGPA VLEYLKVRDQ VVKDLGDKFK 

       730        740        750        760        770        780 
AKPEEITERV ENIQAELRNT QKELEKVKAE LAIAKSEALV SQAETVGEFQ ILVENMGDLD 

       790        800        810        820        830        840 
AKALQTAAER LQQKLGEAAV VLGSTPEDGK VSLVAAFSEG IYKGKKVQAG KFIGGIAKLC 

       850        860        870 
GGGGGGRPNL AQAGGRDASK LPEALHTAKQ QLRETLG

« Hide

References

[1]"Complete sequence of Synechococcus sp. PCC 7002."
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27264 / PCC 7002 / PR-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000951 Genomic DNA. Translation: ACA99661.1.
RefSeqYP_001734917.1. NC_010475.1.

3D structure databases

ProteinModelPortalB1XP68.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1XP68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6056807.
GenomeReviewsGene locus SYNPCC7002_A1672 in contig CP000951_GR.
KEGGsyp:SYNPCC7002_A1672.
PATRIC23817970. VBISynSp37135_1927.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBB1XP68.
ProtClustDBPRK00252.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
[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.
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_SYNP2
AccessionPrimary (citable) accession number: B1XP68
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 29 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

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