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Q5WHM8 (SYA_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:ABC1592
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length876 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 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 – 876876Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075054

Sites

Metal binding5631Zinc Potential
Metal binding5671Zinc Potential
Metal binding6651Zinc Potential
Metal binding6691Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q5WHM8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 5AB72CAF3457DC56

FASTA87697,328
        10         20         30         40         50         60 
MQRLSSASVR QMFIDFFKEK GHSVEPSASL VPFEDPSLLW INSGVATLKK YFDGRVIPEN 

        70         80         90        100        110        120 
PRIVNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEQAIEWAWE FLTDKKWIGF 

       130        140        150        160        170        180 
PQERLSVTVH PEDEEAYRYW HQHIGLPEER IIRLEGNFWD IGEGPSGPNS EIFYDRGPEY 

       190        200        210        220        230        240 
GDDPNDPELY PGGENERYLE IWNLVFSQFN HNADGTYTPL PKKNIDTGMG LERMVSVIQD 

       250        260        270        280        290        300 
TPTNFETDLF MPIIEATEAL ASTTYKEADT AFKVIADHIR TVAFAVGDGA LPSNEGRGYV 

       310        320        330        340        350        360 
LRRLLRRAVR FAKSIGIDRP FMYELVPVVG AIMKDFYPEV ADKQDFIARV IRTEEERFHE 

       370        380        390        400        410        420 
TLNEGLAILS DIIEKAKATN KETIAGEDAF RLYDTYGFPI DLTEEYVHDE GLTVDRAGFD 

       430        440        450        460        470        480 
QEMEQQRQRA RAARQESASM SVQEDVFGEV KTPSVFVGYE HTETDAVITT LVRGKEKVEQ 

       490        500        510        520        530        540 
AVQGDVIQFF LDETPFYAES GGQVADRGMI VTDTGQAVVK DVKKAPNGQH LHTAEVTIGE 

       550        560        570        580        590        600 
ISTGQQASAR IEVRERLDIV KNHTATHLLH QALKDVLGEH VNQAGSLVSS ERLRFDFSHF 

       610        620        630        640        650        660 
GQVTPNELQQ IEEIVNEKVW QALPVDISIQ RLEEAKAAGA MALFGEKYGS EVRVVRVGDY 

       670        680        690        700        710        720 
SLELCGGCHV RNTAEIGLFK ITSESGIGAG VRRIEAVTSK GAYQFLSEQT AILKDAAERL 

       730        740        750        760        770        780 
KAKRLSDVPQ RIESLQEELR KAQRENESLT AKLGQAEAGN LNDQVKEIGG VAVIAAQVDA 

       790        800        810        820        830        840 
KDTEALRSMV DTLKQAHEKA VIVLAAKTGN KLAFVAGVTK PAIAEGFHAG KLIKEVAART 

       850        860        870 
GGGGGGRPDM AQAGGKDPAK LDEALAYVHE YVKSIS

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References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006627 Genomic DNA. Translation: BAD64127.1.
RefSeqYP_175088.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WHM8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WHM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000048691; EBBACP00000047452; EBBACG00000048682.
GeneID3201695.
GenomeReviewsGene locus ABC1592 in contig AP006627_GR.
KEGGbcl:ABC1592.
NMPDRfig|66692.3.peg.1554.
PATRIC18922646. VBIBacCla58185_1691.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
GeneTreeEBGT00050000001776.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBCLA66692:ABC1592-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.
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.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_BACSK
AccessionPrimary (citable) accession number: Q5WHM8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 48 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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