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Q2NEW4 (SYA_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:Msp_1262
OrganismMethanosphaera stadtmanae (strain DSM 3091) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera

Protein attributes

Sequence length903 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 – 903903Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347888

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q2NEW4 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 832CC37BC029CE3D

FASTA903102,117
        10         20         30         40         50         60 
MTYELEQLGY KKQVCQKCGN TFWSIRERAT CGDAPCDEYE FIGNPVTDKQ YDLMGIQKKF 

        70         80         90        100        110        120 
KGFFKDHGHT PINRYPVLAK RWRNDVFLVG ASIYDFQPWV TSGMVRPPAN PLVVAQPSIR 

       130        140        150        160        170        180 
LNDVDNVGRT GRHMTCFTMG AHHAFNTDET PIYWKNETLR YCHEFLVSIG INPEEITYIE 

       190        200        210        220        230        240 
SWWKGGGNEG PSFEICAHGV ELATLVFIQY ATTKDGLKEI PLKIVDTGYG LERIAWVSQG 

       250        260        270        280        290        300 
TPTAYDATFG SVIDKLTDIS GVELNTEILS ENARIAGMMD IEDISDLKLL RKKVADKLSL 

       310        320        330        340        350        360 
DPDMLKKTTA PMEAIYIVAD HTRCLSFMLA DGIIPSNVKE GYLARLVLRR TVKYMNELGL 

       370        380        390        400        410        420 
NESLSDIMKM QVDYLSKTYP EIKDNKDHII NITDLEEERY HTTLTKGKNL VKRSIKTLKK 

       430        440        450        460        470        480 
QNKKSFPTDM LINFYDSHGI PPETVEAISK ENAFDANIPD NFYTQIAAAH EEEEEEEIEE 

       490        500        510        520        530        540 
MELNFPKTKL SFYDDLKQRT FTAKVLGVVD SNKIILNQTI YYPEGGGQPS DIGTITRVNG 

       550        560        570        580        590        600 
EVLNITYAQK VDGIVLHHVA KEDESKLDNI VGEEITGEID SKRRDLLTRN HTATHLVIAS 

       610        620        630        640        650        660 
AREVLGKHIW QAGAQKGLDK TRIDLSHYKR ISHEEVQEIE RLANKRVQEN HPVNIQWYDR 

       670        680        690        700        710        720 
TDAEVKYGFK LYQGGIVPGK NIRVVEIPGI DVQACAGTHC EKTGDIGVIK LLRTERVQDG 

       730        740        750        760        770        780 
VERLEYAVSD SGIKKIQDDD DIIRNSSDVF GVDAEQLPRT CKRFFNEWKE QQKRIKSLEK 

       790        800        810        820        830        840 
QLAQVKIFSL ENEIANINGY NVITEVLDVD NNQLREIAIN LVEKEEVADI AILINNNGNI 

       850        860        870        880        890        900 
VASSNNKILE KGMKMGDVVN DIGKFLGGRG GGKPTLAQGA KMTDLSRKDE AFESVKEQIR 


SWN 

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References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed: 16385054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 3091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000102 Genomic DNA. Translation: ABC57639.1.
RefSeqYP_448282.1. NC_007681.1.

3D structure databases

ProteinModelPortalQ2NEW4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NEW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3855828.
GenomeReviewsGene locus Msp_1262 in contig CP000102_GR.
KEGGmst:Msp_1262.
NMPDRfig|339860.6.peg.1209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ2NEW4.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMSTA339860:MSP_1262-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.
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_METST
AccessionPrimary (citable) accession number: Q2NEW4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 46 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