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B2UKT4 (SYA_AKKM8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:Amuc_1383
OrganismAkkermansia muciniphila (strain ATCC BAA-835) [Complete proteome] [HAMAP]
Taxonomic identifier349741 [NCBI]
Taxonomic lineageBacteriaVerrucomicrobiaVerrucomicrobiaeVerrucomicrobialesVerrucomicrobiaceaeAkkermansia

Protein attributes

Sequence length942 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 – 942942Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347482

Sites

Metal binding5861Zinc Potential
Metal binding5901Zinc Potential
Metal binding6951Zinc Potential
Metal binding6991Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B2UKT4 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: ED53F46EB999D0D9

FASTA942103,645
        10         20         30         40         50         60 
MMTATEIRQS FLDFFREKQH TVVPSASLMP QSPGLLFTNA GMNQFVPYFL GVWTPPWTPA 

        70         80         90        100        110        120 
RATDTQKCIR AGGKHNDLED VGYDSYHHTF FEMLGNWSFG DYFKREAIRW AWELVVERWG 

       130        140        150        160        170        180 
FPAERLYATV YAPDKSKGDP GEFDREAWDF WAELFRSRGL DPDVHIVHGN VKDNFWMMGE 

       190        200        210        220        230        240 
TGPCGPCSEL HVDLTPEGNT KGSLVNKDSD QCIEIWNLVF IQYNAESDGS MRNLPACHVD 

       250        260        270        280        290        300 
TGMGFERACS IMQCTNGFKD FSRKPSNYAT DVFRPLFDRL EVLSGRKYAD VYPAPGSKRV 

       310        320        330        340        350        360 
DAEDGTLQEA IAFRVIADHL RTLSFSIADG ILPGNNGRNY VLRRILRRAV RYGRRLGFTQ 

       370        380        390        400        410        420 
PFLAELVDTL VESFGQVFPE LAARATTVKE VLNREEASFN ETLDRGLELF DAETASAGKV 

       430        440        450        460        470        480 
SGEFAFKLYD TYGFPIDLTA LLAEERGLDI DMERFNRLME EQRERARAAR KSEVVRALDL 

       490        500        510        520        530        540 
KTDAVTEFTG YDVDECAATV LEVSRQGDSL FIITDKTPFY AEMGGQVSDA GLIEIGGESY 

       550        560        570        580        590        600 
HVMAVQQIGN ARAHVVEARP GLEVKPGDRV HLSIDAERRR RIEAHHTATH LLHCALHQVV 

       610        620        630        640        650        660 
SPDAAQQGSF VSEDRLRFDF NSSAVSPDQL RLIEEKVNGW IEESLPVHCT ERAYADVKGN 

       670        680        690        700        710        720 
AAIAQFFGDK YGDVVRVVQV GGCRDGLDGV SMEFCGGTHI ANTKNIGLFK IKSEGAIASG 

       730        740        750        760        770        780 
VRRIEAMTGD AALEMIRQHV VAKSLEIAKA VEKIKEVNYE LADMGLEQVP VPTIEGKPGL 

       790        800        810        820        830        840 
TALGASDIRT VNDSLARFDA SVEHFKQTAL DAEKKLKKAR AGQSAAKADA LLNEWLSDAP 

       850        860        870        880        890        900 
SSLIQVAEGA GELLQELLNG LKKRQYAGAA FLLCVDSSSL LLGAYCGKDA IADGLSAGDM 

       910        920        930        940 
IREVAALAGG KGGGRADQAR GSAPQDADPQ ALAAAARNII NG 

« Hide

References

[1]"Complete sequence of Akkermansia muciniphila ATCC BAA-835."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N. expand/collapse author list , Smidt H., Derrien M., Plugge C.M., Zoetendal E.G., de Vos W.M., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-835.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001071 Genomic DNA. Translation: ACD05207.1.
RefSeqYP_001877988.1. NC_010655.1.

3D structure databases

ProteinModelPortalB2UKT4.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2UKT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6274625.
GenomeReviewsGene locus Amuc_1383 in contig CP001071_GR.
KEGGamu:Amuc_1383.
PATRIC20835640. VBIAkkMuc16855_1557.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAVILEMES.
ProtClustDBPRK00252.

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_AKKM8
AccessionPrimary (citable) accession number: B2UKT4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 25 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