Alanine--tRNA ligase - Agrobacterium tumefaciens (strain C58 / ATCC 33970)

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Q8UE87 (SYA_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. 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:	Atu1873
ORF Names:	AGR_C_3437

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	887 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 – 887

887

Alanine--tRNA ligase HAMAP MF_00036_B

PRO_0000075044

Sites

Metal binding

564

Zinc Potential

Metal binding

568

Zinc Potential

Metal binding

676

Zinc Potential

Metal binding

680

Zinc Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q8UE87 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: 4AB5CDB1C58A4238
Show »

FASTA

887

95,738

        10         20         30         40         50         60 
MSGVNEIRST FLDYFKKNGH EIVPSSPLVP RNDPTLMFTN AGMVQFKNVF TGLESRPYST 

        70         80         90        100        110        120 
AASAQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKEEAITHA WNLITKEFGI 

       130        140        150        160        170        180 
DRNRLLVTVY HTDDEAFNLW KKIAGFSDDR IIRIPTSDNF WAMGDTGPCG PCSEIFYDHG 

       190        200        210        220        230        240 
DHIWGGPPGS PEEDGDRFIE IWNLVFMQYE QLTKEERIDL PRPSIDTGMG LERISALLQG 

       250        260        270        280        290        300 
KHDNYDTDLF RALIAASVEA TGVPAEGEHR ASHRVIADHL RSSAFLIADG VLPSSEGRGY 

       310        320        330        340        350        360 
VLRRIMRRAM RHAELLGSRD PLIYRLLPAL IQQMGRAYPE LVRAEALISE TLKLEETRFR 

       370        380        390        400        410        420 
KTLERGLSLL SDATSTLHKG DMLDGETAFK LYDTYGFPLD LTQDALRARE IGVDISGFTD 

       430        440        450        460        470        480 
AMQRQKAEAR SHWAGSGDKA TETVWFELKE KFGATEFLGY DTESAEGVIQ AIVRDGKEVD 

       490        500        510        520        530        540 
SAAEGETVHI VVNQTPFYGE SGGQMGDTGV IVGDAGTFDV SGTQKKGEGL FVHSGTVSKG 

       550        560        570        580        590        600 
GLKVNEAVQL TVDHDRRSRL RANHSATHLL HEALREVLGT HVAQKGSLVA PERLRFDVSH 

       610        620        630        640        650        660 
PKPMSAEELK VVEDMANEIV LQNSPVVTRL MSVDDAIAEG AMALFGEKYG DEVRVVSMGT 

       670        680        690        700        710        720 
GLHGAKANRP YSVELCGGTH VAATGQIGLI RILGESAVGS GVRRLEAVTG QGALAYLAEQ 

       730        740        750        760        770        780 
DERVKALASS LKVQPGDVLS RVEGLLDERK KLERELADAR KKLAMGGGSS DAGANDVQQV 

       790        800        810        820        830        840 
AGVNFLAKSL SGIDAKDLKG LADEAKANLG SGVVLLIAVS DDGKASAVAA VTEDLTGRFS 

       850        860        870        880 
AVDIVRTASA ALGGKGGGGR PDMAQAGGPD GTKAKEAIEA VAAALAA

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References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58."
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J.

Nester E.W.
Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C58 / ATCC 33970.

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58."
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C.

Slater S.
Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C58 / ATCC 33970.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007869 Genomic DNA. Translation: AAK87639.2.
PIR	AG2806. F97585.
RefSeq	NP_354854.2. NC_003062.2.
3D structure databases
ProteinModelPortal	Q8UE87.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8UE87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1133911.
GenomeReviews	Gene locus Atu1873 in contig AE007869_GR.
KEGG	atu:Atu1873.
PATRIC	20813525. VBIAgrTum91616_1887.
Phylogenomic databases
eggNOG	COG0013.
HOGENOM	HBG354397.
OMA	MFTNSGM.
PhylomeDB	Q8UE87.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	ATUM176299-1:ATU1873-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_AGRT5

Accession

Primary (citable) accession number: Q8UE87

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	August 2, 2002
Last modified:	January 25, 2012
This is version 65 of the entry and version 2 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