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Q6G2Z4 (SYA_BARHE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BH10220
OrganismBartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier283166 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length887 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 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 – 887887Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075063

Sites

Metal binding5641Zinc Potential
Metal binding5681Zinc Potential
Metal binding6761Zinc Potential
Metal binding6801Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q6G2Z4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 693ABFABFD861219

FASTA88797,711
        10         20         30         40         50         60 
MNSVNSIRST FLDYFQLNGH KIVSSSPLVP RNDPTLMFTN AGMVQFKNVF TGLEQRPYKQ 

        70         80         90        100        110        120 
ATTAQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKEEAIFLS WNLLTKEFCL 

       130        140        150        160        170        180 
PEDKLLVTVY HNDDVSTELW RKISGLPDEK IVRIATADNF WAMGDTGPCG PCSEIFYDHG 

       190        200        210        220        230        240 
DEIWGGPPGS AYEDGDRFIE IWNLVFMQYE QVNKEKRVEL PHPSIDTGMG LERIAAVLQG 

       250        260        270        280        290        300 
GHDNYDIDLF RALIAVSQEI TGVKATGDFI ASHRVIADHL RSSAFLIADG VLPSNEGRGY 

       310        320        330        340        350        360 
VLRRIMRRAM RHAHLLGAKE PLMWRLLPVL IHEMGQAYPE LVRAESLISE TLKLEEIRFR 

       370        380        390        400        410        420 
KTLERGLGLL SEASTDLKEG DHLNGEIAFK LYDTYGFPLD LTQDALRCRG ISVDVAAFNK 

       430        440        450        460        470        480 
AMEGQKAKAR ANWSGSGETV TEAIWFSVRD QLGATEFLGY ETEKSEGILT ALVRDGEIVD 

       490        500        510        520        530        540 
DISSGQKAIL VVNQTPFYGE SGGQIGDSGT ISGKNFVFEV HDTQKKADGV FIHIGEVKSG 

       550        560        570        580        590        600 
QARMSECVEL TVDGVRRKKI RVNHSATHLL HEALRQVLGS HVTQKGSLVS PDRLRFDFSH 

       610        620        630        640        650        660 
PKSVSLEELE KIEDLANEIV LQNSEVTTRL MLVDDAISEG AMALFGEKYG DEVRVVSMGN 

       670        680        690        700        710        720 
RLEKGKLKSR WSIELCGGTH VERTGDIGLI HIVSESSVAA GVRRIEALTG TAARLYLSRQ 

       730        740        750        760        770        780 
DARVHEIADL LKTSATDVEE RVRILLEDRR KLEKELNDER KKSVLSGGIV KSDQEDITII 

       790        800        810        820        830        840 
NGISFMGRVV KNISPRDLKT LVDSGKKKIG SGVVAFIGVS EDGKGSAVLG VTDDLTHKLN 

       850        860        870        880 
AVDLVRILSG ILGGQGGGGR PDMAQSGGPK GNKADEALAV LKASLEG

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX897699 Genomic DNA. Translation: CAF27813.1.
RefSeqYP_033806.1. NC_005956.1.

3D structure databases

ProteinModelPortalQ6G2Z4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2866067.
GenomeReviewsGene locus BH10220 in contig BX897699_GR.
KEGGbhe:BH10220.
NMPDRfig|283166.1.peg.934.
PATRIC20545869. VBIBarHen29080_1070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBQ6G2Z4.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBHEN283166:BH10220-MONOMER.

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_BARHE
AccessionPrimary (citable) accession number: Q6G2Z4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 47 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

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