Alanine--tRNA ligase - Bacillus anthracis

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Q81LK0 (SYA_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	BA_4616, GBAA_4616, BAS4284

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 880

880

Alanine--tRNA ligase HAMAP MF_00036_B

PRO_0000075050

Sites

Metal binding

567

Zinc Potential

Metal binding

571

Zinc Potential

Metal binding

669

Zinc Potential

Metal binding

673

Zinc Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q81LK0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 59EC95C8BB33BC3C
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FASTA

880

97,441

        10         20         30         40         50         60 
MKQLTGAQIR QMFLDFFQEK GHAVEPSASL VPHEDPSLLW INSGVATLKK YFDGRVIPQN 

        70         80         90        100        110        120 
PRITNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAITWAWE FLTSDKWIGF 

       130        140        150        160        170        180 
DKELLSVTIH PEDEEAFTIW NEKMGVPKER IIRLEENFWD IGEGPSGPNT EIFYDRGEAY 

       190        200        210        220        230        240 
GNDFSDPELY PGGENERYLE VWNLVFSQFN HNPDGSYTPL PKKNIDTGMG LERMTSIVQD 

       250        260        270        280        290        300 
VPTNFDTDLF MPMIGATETI SGEKYRNGDL EKDMAFKVIA DHIRTVTFAV GDGALPSNEG 

       310        320        330        340        350        360 
RGYVLRRLLR RAVRYSKKLN INRPFMFELV PVVGEVMKDF YPEVLEKKDF IAKVVKNEEE 

       370        380        390        400        410        420 
RFHETLHDGE AILSEVIAKA KEEKTTVISG VDAFRLYDTY GFPIELTEEY AEEAGMTVDH 

       430        440        450        460        470        480 
EGFENEMEKQ RERARAARQD VDSMQVQGGV LGEVKVASEF VGYGTVATES NVVALVKNGE 

       490        500        510        520        530        540 
YTDSLQVGEE GQLMLDVTPF YAESGGQIAD RGCLLADGVK VLVKDVQKAP NGQNLHQVVV 

       550        560        570        580        590        600 
EEGTLTKDAA VKAIIDTKNR SSVVKNHTAT HLLHQALKDV LGTHVNQAGS LVTSERLRFD 

       610        620        630        640        650        660 
FSHFGQVQAD ELEKIERIVN EKIWESIDVE ISQKAIEEAK EMGAMALFGE KYGDVVRVVQ 

       670        680        690        700        710        720 
VGDYSLELCG GCHVDNTASI GIFKIVAESG IGAGIRRIEA VTGKSAYELM NDQVGLLKEA 

       730        740        750        760        770        780 
AGKMKTNPKD ILTRVDGLFA EVKQLQKENE SLAAKLSNIE AGNLTDSVMT VDGVNVLAAK 

       790        800        810        820        830        840 
VNVADMNNLR TMMDDLKNKL ESAVVVLASV NDDKVNILAG VTKDLISQGY HAGKLVKEVA 

       850        860        870        880 
SRCGGGGGGR PDMAQAGGKN PAQVEEALAF VQEYVKSVSK

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References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP28321.1. AE017334 Genomic DNA. Translation: AAT33739.1. AE017225 Genomic DNA. Translation: AAT56583.1.
RefSeq	NP_846835.1. NC_003997.3. YP_021264.1. NC_007530.2. YP_030532.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81LK0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q81LK0. 5 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000009698; EBBACP00000009454; EBBACG00000009690. EBBACT00000016176; EBBACP00000015797; EBBACG00000016168. EBBACT00000022998; EBBACP00000022483; EBBACG00000022989.
GeneID	1088737. 2815019. 2849985.
GenomeReviews	Gene locus BA_4616 in contig AE016879_GR. Gene locus BAS4284 in contig AE017225_GR. Gene locus GBAA_4616 in contig AE017334_GR.
KEGG	ban:BA_4616. bar:GBAA_4616. bat:BAS4284.
TIGR	BA_4616. GBAA_4616.
Phylogenomic databases
GeneTree	EBGT00050000001776.
HOGENOM	HBG354397.
OMA	VILEMES.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	BANT260799:BAS4284-MONOMER. BANT261594:GBAA4616-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. [Tree]
InterPro	IPR002318. 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]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00344. AlaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_BACAN

Accession

Primary (citable) accession number: Q81LK0
Secondary accession number(s): Q6HT06, Q6KM96

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents