Skip Header

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

Q2NJ60 (SYA_AYWBP) 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
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:AYWB_416
OrganismAster yellows witches'-broom phytoplasma (strain AYWB) [Complete proteome] [HAMAP]
Taxonomic identifier322098 [NCBI]
Taxonomic lineageBacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Candidatus Phytoplasma › Candidatus Phytoplasma asteris

Protein attributes

Sequence length864 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 – 864864Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347494

Sites

Metal binding5341Zinc Potential
Metal binding5381Zinc Potential
Metal binding6391Zinc Potential
Metal binding6431Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q2NJ60 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 65658154C3A15DC3

FASTA864100,363
        10         20         30         40         50         60 
MTSFEIRQMW IKFFASKNHH IEKSFSLIPR NEDNLLWVNA GITPLKKYFD GTQTPSFRRI 

        70         80         90        100        110        120 
TNVQKCIRTK DIKNVGKTSR HHTFFEMLGN FSIGNYFKKE AIHYAFELLT SPKWFGFPLE 

       130        140        150        160        170        180 
KLYITYFFQD QDTYQYWLDL GVNKNHLIHL KDNFWQIGPG PSGPCTEIFF DRGKTFDPRN 

       190        200        210        220        230        240 
KELIIEDLEN DRFIEIWNIV FSQYNCDPKL PIEKYQELPS KNIDTGAGLE RLACILQNTK 

       250        260        270        280        290        300 
TNFETDLFFP LIKALEKMTQ ITYTGQESFK IIADHLKTLV FAINDGAVLT NEKRGYVLKK 

       310        320        330        340        350        360 
LLRRAANEGK KLGLEKPFLY KLVPPTVAMM KDFYKELCTN QEMIAKVLLQ QENIFEKTLK 

       370        380        390        400        410        420 
TAEKTFLQHL TQNTLSGKNF FKLYDTYGIP ENLILDYAKK KNITTDYQKF QELLHEQQNL 

       430        440        450        460        470        480 
SKKNQTSQTN MNKQEEAFLH FLTPSEFIGY TNFACKTKVI KVFDEGIVLE KTPFYANMGG 

       490        500        510        520        530        540 
QIEDEGWIDN NKVTKITKLP NGQILHEFKG NFCEGQEVYA CIDKTKRKQI SYHHTATHLL 

       550        560        570        580        590        600 
EVVLQKQLGN HIKKQGSSVG FSSLRYDFNH FEKITPQTLL QIEKEVNQLI QKRVPVKIEQ 

       610        620        630        640        650        660 
LSIQDAQKKY ATLLEQNQKA KYKDKVRIVN IDTFSVDLCG GTHATNTKDL EHFTILSYES 

       670        680        690        700        710        720 
ISSGIYRIEA VCNKNCQESL NAKLAPYQNE LHQLTQKAKS LQTQNLDFEI KKFPPITKSY 

       730        740        750        760        770        780 
QDIINYQKHI KTQQQALVLF EKKVLEHHQK KMIQAESNFL PPQINKKMML TIKEEKPLEV 

       790        800        810        820        830        840 
IKFFMNHIFY KYHLEVLFLS YVQPEKIVFL CQSKTLHAGN LIKEGVSLAC GSGGGNASLA 

       850        860 
QGGTKKTQNL EKMLNFVKNK LKIN

« Hide

References

[1]"Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts."
Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.
J. Bacteriol. 188:3682-3696(2006) [PubMed: 16672622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AYWB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000061 Genomic DNA. Translation: ABC65533.1.
RefSeqYP_456612.1. NC_007716.1.

3D structure databases

ProteinModelPortalQ2NJ60.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NJ60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3865575.
GenomeReviewsGene locus AYWB_416 in contig CP000061_GR.
KEGGayw:AYWB_416.
PATRIC21004866. VBIAstYel136969_0475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ2NJ60.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycAYEL322098:AYWB_416-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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
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.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_AYWBP
AccessionPrimary (citable) accession number: Q2NJ60
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 7, 2006
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

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