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A6VJ32 (SYA_METM7) 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
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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:MmarC7_1395
OrganismMethanococcus maripaludis (strain C7 / ATCC BAA-1331) [Complete proteome] [HAMAP]
Taxonomic identifier426368 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length892 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

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 – 892892Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000074511

Sites

Metal binding5961Zinc By similarity
Metal binding6001Zinc By similarity
Metal binding7001Zinc By similarity
Metal binding7041Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VJ32 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: BAAF213B5E22EFF2

FASTA892101,489
        10         20         30         40         50         60 
MEINHDYRVK LFDELGFERK QCTECNQWFW TLDKDRTTCG DSPCDEYSFI GSPITRKKYT 

        70         80         90        100        110        120 
YNEMVREFTN FFAEKGHSPV KRSPVVAKRW RDDILLTIAS IAVFQPWVTN GLVKPVKNPL 

       130        140        150        160        170        180 
VIAQPCIRLN DIDNVGRTGR HLTCFTMGAH HAFNSKDDYK YWTDKTVEYC FELMNRLGID 

       190        200        210        220        230        240 
GKTITFIESW WEGGGNAGPC YEVITHGVEL ATLVFMQYKK VGSEYEEIPL KIVDTGYGIE 

       250        260        270        280        290        300 
RFAWASQGTP TVYESLFSEV IEKLKEDAGI PGVDEKIMAE SATLAGLMDI ENVGDLRVLR 

       310        320        330        340        350        360 
QKVAEKIGMD VDELDKLISP LEYIYAIADH TRCLSFMFGD GIVPSNVKEG YLARLVLRKT 

       370        380        390        400        410        420 
LRYMEKIGIS MSIKDIISMQ LENMKEIYPE LSEMKEYIMD VLDSEEKKYI QTVNRGRGIV 

       430        440        450        460        470        480 
ERMAASKSEI TLDDLIELYD SNGLPPEIVK DVVDELNKKG KKTIAITVPD NFYTIVAERH 

       490        500        510        520        530        540 
EEEKPEEVVS TKKELPEVEV SETELLFFKH PTQVEFEAKV LKTVEKYVVL DKTLFYAEGG 

       550        560        570        580        590        600 
GQKYDIGQIN GIEVIDVQKK NGIVFHKVSD ISKFKEGDIV KGTVNWENRL KLMRNHTATH 

       610        620        630        640        650        660 
VINAAATRVL GKHIWQTGSN VDTEKGRLDI THYERISREQ VKEIERIANE IVLSKMPVNS 

       670        680        690        700        710        720 
TFMDRNDAEQ KYGFTIYQGG VVPGDTLRII EIEGTDVEAC GGTHCSNTSE IGYIKVLKTE 

       730        740        750        760        770        780 
RIQDGVERLE YSTGMGSVSE IAVLEDTLID SAEILGIPND QLPKTVKRFF EEWKEQKKTI 

       790        800        810        820        830        840 
EELQKKVGEL VKYELADKFE KYGNYEVLVE QVSGTPNELM SIADNLAVGN KLIVLMNEND 

       850        860        870        880        890 
YLLCKRGENV ELSMKELIRN IGKGGGKDNL AQGKYSENKE QITEKIIQIL NK

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C7."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C7 / ATCC BAA-1331.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000745 Genomic DNA. Translation: ABR66458.1.
RefSeqYP_001330609.1. NC_009637.1.

3D structure databases

ProteinModelPortalA6VJ32.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VJ32.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5329195.
GenomeReviewsGene locus MmarC7_1395 in contig CP000745_GR.
KEGGmmz:MmarC7_1395.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMMAR426368:MMARC7_1395-MONOMER.

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.
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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_METM7
AccessionPrimary (citable) accession number: A6VJ32
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 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

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