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Q9Z714 (SYA_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. 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:CPn_0892, CP_0974, CpB0923
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length872 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-Rule MF_00036

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00036

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00036.

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-Rule MF_00036

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
tRNA-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 872872Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075087

Sites

Metal binding5581Zinc Potential
Metal binding5621Zinc Potential
Metal binding6601Zinc Potential
Metal binding6641Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q9Z714 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DAD99C43E273CAF8

FASTA87297,670
        10         20         30         40         50         60 
MLSNTIRSNF LKFYANRHHT ILPSSPVFPH NDPSILFTNA GMNQFKDIFL NKEKVSYSRA 

        70         80         90        100        110        120 
TTSQKCIRAG GKHNDLDNVG HTSRHLTFFE MLGNFSFGDY FKAEAIAFAW EVSLSVFNFN 

       130        140        150        160        170        180 
PEGIYATVHE KDDEAFALWE AYLPTDRIFR LTDKDNFWSM ANTGPCGYCS ELLFDRGPSF 

       190        200        210        220        230        240 
GNASSPLDDT DGERFLEYWN LVFMEFNRTS EGSLLALPNK HVDTGAGLER LVSLIAGTHT 

       250        260        270        280        290        300 
VFEADVLREL IAKTEQLSGK VYHPDDSGAA FRVIADHVRS LSFAIADGLL PGNTERGYVL 

       310        320        330        340        350        360 
RKILRRSVNY GRRLGFRNPF LAEIVPSLAD AMGEAYPELK NSLSQIQKVL TLEEESFFKT 

       370        380        390        400        410        420 
LDRGGNLLQQ VLKSSSSSSC ISGEDAFKLK DTYGMPIDEI SLLAKDYDYS VDMDTFHKLE 

       430        440        450        460        470        480 
QEAKERSRKN VVQSQGTSES IYNELHLTSE FIGYDHLSCD TFIEAIISKD HIVSSLQEKQ 

       490        500        510        520        530        540 
EGAIVLKVSP FYAEKGGQVG DSGEIFCSEG TFIVTHTTSP KAGLIVHHGR ISQGSLTVEA 

       550        560        570        580        590        600 
AVTAQVNRYR RKRIANNHTA CHLLHKALEI TLGDHIRQAG SYVDDTKIRL DFTHPQAISP 

       610        620        630        640        650        660 
EDLLCIETLV NESIRENEPV DIREALYSDV MNSSEIKQFF GDKYSDVVRV VSAGHSHELC 

       670        680        690        700        710        720 
GGTHAEATGD IGFFRITKEH AVAMGIRRIE AVTGEKAEAT VHQQSEVLEE IATLLQVPRD 

       730        740        750        760        770        780 
QIVSRLTATL DERKQQDKRL NELENSLIQT KLDKLIHNCH QRQGITCLVH HLAEHENHRL 

       790        800        810        820        830        840 
QQYAQCLHQR IPEKLISLWT TEKNGKYIVL SRVSDDLITQ GVHAQDLLKA VLTPCGGRWG 

       850        860        870 
GKDQSAQGSA PALPATEVLN ETLWQWISTQ LI 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD19030.1.
AE002161 Genomic DNA. Translation: AAF38754.1.
BA000008 Genomic DNA. Translation: BAA99100.1.
AE009440 Genomic DNA. Translation: AAP98852.1.
PIRB86602.
H72023.
RefSeqNP_225087.1. NC_000922.1.
NP_300949.1. NC_002491.1.
NP_445511.1. NC_002179.2.
NP_877195.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD19030; AAD19030; CPn_0892.
AAF38754; AAF38754; CP_0974.
AAP98852; AAP98852; CpB0923.
BAA99100; BAA99100; BAA99100.
GeneID1467602.
895680.
919656.
963442.
KEGGcpa:CP0974.
cpj:CPj0892.
cpn:CPn0892.
cpt:CpB0923.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156965.
KOK01872.
OMAISQPSIR.
OrthoDBEOG6Q2SQ2.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-1005-MONOMER.
CPNE115713:GHEY-932-MONOMER.
CPNE138677:GH8N-924-MONOMER.
CPNE182082:GH4N-954-MONOMER.
BRENDA2.5.1.55. 1311.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
InterProIPR002318. 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. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
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. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_CHLPN
AccessionPrimary (citable) accession number: Q9Z714
Secondary accession number(s): Q9JQE1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries