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Q7NI36 (SYA_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:gll2348
OrganismGloeobacter violaceus (strain PCC 7421)
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Gloeobacteria › Gloeobacterales › Gloeobacter

Protein attributes

Sequence length871 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
Reference 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 – 871871Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075119

Sites

Metal binding5551Zinc Potential
Metal binding5591Zinc Potential
Metal binding6571Zinc Potential
Metal binding6611Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q7NI36 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: ED8E43054B87BCD2

FASTA87195,254
        10         20         30         40         50         60 
MPTVLNGNAI REKFLQFFES KQHRRLPSAS LVPDDPTVLL TIAGMLPFKP VFMGKRERPA 

        70         80         90        100        110        120 
PRVTTSQKCV RTNDIENVGR TARHHTFFEM LGNFSFGDYF KREAIGWAWE LVTGVFELPP 

       130        140        150        160        170        180 
ERLWVSVYEE DEEALVLWQE VAGLPPVRVR KMGADSNFWE SGPTGPCGPC SEIYYDFHPE 

       190        200        210        220        230        240 
RGEGDIDLDD DSRFLEIYNL VFMQLNRDSE GTFSELPRKN IDTGLGLERM AQVLQGVPNN 

       250        260        270        280        290        300 
YETDLVFPII RKAEVLSGRD YFKADDQQKT SFKIIGDHTR AVVHLVADGV LPGNLGRGYI 

       310        320        330        340        350        360 
LRRLIRRMVR HGRMLGIAGS FLPQMATVAV ELMGGAYPNL LESRELILTR LATEESQFLQ 

       370        380        390        400        410        420 
TLETGERLLD EILGRSEKRI SGVDAFMLYD TYGFPLELTM EVAAERGLEV DVAAYEEAME 

       430        440        450        460        470        480 
KQRERARRAA KTVDLTQGAS LADLERTDFL GYRNVASKAM VKLVLFEGEP IERASAGASV 

       490        500        510        520        530        540 
QLVLDQTPFY PEGGGQIGDR GYLSGPDLLV RIEDVQKRDT VILHTGRIER GTVATGDSVQ 

       550        560        570        580        590        600 
AQIDLADRRR SQAHHTATHL LQAALKKVLG ESVQQQGSLV AFDRLRFDFS WPKALSQAEI 

       610        620        630        640        650        660 
QQVEDLVNTW IAEAHTLSQE VMPIDQAKAR GALAFFGEKY GSEVRVIDVP GVSIELCGGT 

       670        680        690        700        710        720 
HVRNTAEIGL FKMVSETGIA SGVRRIEAVA GPAVLEYLRL RDTVTRQLAD EFKVQVEQIP 

       730        740        750        760        770        780 
QRVAALTSDL KQAQKQIDSL KAALATARAE ALLGQAETTG GFRVLVADLG DTEPEALKSA 

       790        800        810        820        830        840 
AEHLLAKLGE GGAVVLGSAP AADKVSLVAA FGKGAVAKGL NAGKFVGEVA KITGGGGGGR 

       850        860        870 
PNLAQAGGKQ PEKLKNALSE ASSKLSGALG A

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed: 14621292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000045 Genomic DNA. Translation: BAC90289.1.
RefSeqNP_925294.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NI36.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2600749.
GenomeReviewsGene locus gll2348 in contig BA000045_GR.
NMPDRfig|251221.1.peg.2348.
PATRIC22044171. VBIGloVio86258_2386.

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ7NI36.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycGVIO251221:GLL2348-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]
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_GLOVI
AccessionPrimary (citable) accession number: Q7NI36
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 55 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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