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A5UKU6 (SYA_METS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Msm_0619
OrganismMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]
Taxonomic identifier420247 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanobrevibacter

Protein attributes

Sequence length897 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 – 897897Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347884

Sites

Metal binding5911Zinc By similarity
Metal binding5951Zinc By similarity
Metal binding6951Zinc By similarity
Metal binding6991Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UKU6 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 0461A6075C3D10D9

FASTA897100,524
        10         20         30         40         50         60 
MLEIFDKLGY KKQKCKTCGH EFYAQVDRDT CGDAPCDEYE FIGNPATDKP YTLYEIQQVF 

        70         80         90        100        110        120 
REFLEKEGHT PIKRYPILAK RWRDDVFLVG ASIFCFQPWV TSGMVKPPAN PLEIEQPSVR 

       130        140        150        160        170        180 
LNDVDNVGRT GRHMTCFTMG SHTVINTEEN FIYWEDETIR LCHEFFKYIG INTEEICFIK 

       190        200        210        220        230        240 
SWWSGGGNEG PCYEVCVRGV ELATLVFIQY KTLDNGEKEE IPIKVVDTGY GLERIAWISQ 

       250        260        270        280        290        300 
GTPTAYDACF APVVDKLKEL TDVKVNTDIL ARNAQIAGMM DIEDIGDIKE LRQQVANSLG 

       310        320        330        340        350        360 
ITLDELLESA EPMEAIYIIA DHTRCLAFML ADGIIPSNVK EGYLARLVLR RTIRFMKELN 

       370        380        390        400        410        420 
MKESLAEVMG IQLEFLTKFY PEIKDSEDHI MNIISLEEER YQSTIKKGTS IVKRSIKRLK 

       430        440        450        460        470        480 
KEGKTEMPLD MLMDLYDAHG IPPETVVEIA GDNFTVNVPD NFFTLVAGAH EKDTSNKKES 

       490        500        510        520        530        540 
FEIDYPETDL LFYKDFNQKE FEAEVLGVVE KDGKNTLVFD KTVFYPEGGG QPSDVGTISV 

       550        560        570        580        590        600 
DGAVVNINYA EKVNNVVLHH VDGDVDLDNF VGKKVEGKID WNRRITLARH HSATHLIVAA 

       610        620        630        640        650        660 
ARKILGEHIW QAGAQKGVSR SRIDLSHYKR ISQEELNEIE KLANEYVMDN IELDIKFYTR 

       670        680        690        700        710        720 
DEAESLYGFK LYQGGIVPGK SIRVVKIPGI DVQACAGTHV LRTGDIGPIK INKTERVQDG 

       730        740        750        760        770        780 
VERIDFSAGT AAVDSIQNEN KLLRESSGIF KVDDDQLPKT CDRFFSEWKA QKNEIDKLKS 

       790        800        810        820        830        840 
EIASLKMNSL ADDVTEINGL KVVKQLIDAD FKELQKIATD FTDNDKADVV LMGNNDGKIV 

       850        860        870        880        890 
GAASQNAIDA GIKVNEIIKK AAGVLGGGGG GRLTLAQGAG PKCENMNEAL NIAIDLI

« Hide

References

[1]"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut."
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed: 17563350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000678 Genomic DNA. Translation: ABQ86824.1.
RefSeqYP_001273192.1. NC_009515.1.

3D structure databases

ProteinModelPortalA5UKU6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5UKU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5217344.
GenomeReviewsGene locus Msm_0619 in contig CP000678_GR.
KEGGmsi:Msm_0619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAGESKTDQ.
ProtClustDBPRK13902.

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.
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.
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_METS3
AccessionPrimary (citable) accession number: A5UKU6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 10, 2007
Last modified: January 25, 2012
This is version 37 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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