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Q8ZSV6 (SYA_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:PAE3565
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length892 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_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm HAMAP MF_00036_A.

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_A

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 – 892892Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075272

Sites

Metal binding5941Zinc By similarity
Metal binding5981Zinc By similarity
Metal binding7021Zinc By similarity
Metal binding7061Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZSV6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B677EF17883846E8

FASTA892100,033
        10         20         30         40         50         60 
MLSARVLKNT GFLRKQCPLC KSYFWTLRRD QEYCGDQPCV PYGFIGNPPT KISIDSLTEL 

        70         80         90        100        110        120 
RERFLRFFER RGHARIKRYP VVARWRDDVY LVGASIYDFQ PWVTSGAVPP PANPLVISQP 

       130        140        150        160        170        180 
SIRLTDVDKV GRSGRHLTGF EMMAHHAFNY PDKFIYWIDE TAEYAYEFFT KELGIPPEEI 

       190        200        210        220        230        240 
TFKESIWEGG GNAGECFEVL VRGLEVATLV FMHYEVKEGK YVELPLKIVD TGYGLERIYW 

       250        260        270        280        290        300 
LIRGTPTIYD AVFGPYLDKA RRSLGFPEPP SELMGKASVY FGQMDPEVIG LEKAYDIIAE 

       310        320        330        340        350        360 
KIGVDPKWLR EVFKPQEALY VLADHSRTVS WMIADGVIPS NSGAGYLARL LLRRILKNLK 

       370        380        390        400        410        420 
LVGVETPLVE LFDMHLKELK ADYPEVWEAR NLILELVDIE ERKYREILKS APGVVKKAYE 

       430        440        450        460        470        480 
EARRRGRAGF DAEDLVSLYD SFGLPPEIVA ETAKSLGVEV KIPDDFYSRL AARHAKREKQ 

       490        500        510        520        530        540 
PEKTLVEMAK IADLPRTREL FYEDPYMKSF KAKVLRVIDG KYVVLDQTAF YAEGGGQPAD 

       550        560        570        580        590        600 
IGILKHGGGA AKVVDVQRVG HVIVHVVEGE APPEGSEVVG EIDWDRRYAL MKMHTGTHVL 

       610        620        630        640        650        660 
IQSIRRVLGP HIWQAGAQKD IPASRIDVTH FKLPTAEEVA EIERLANSVV QANMPVHVKI 

       670        680        690        700        710        720 
LPRNEAEAKY GFILYQGGVV PAREIRVVQI GPDEAPYDVQ ACGGTHLKST GEIGLIKIQK 

       730        740        750        760        770        780 
VERIADGVVR FIFTTGLHAL KYVQEIERQV AEAASLAGGN RDNLVDSVRR LLQRAEEAER 

       790        800        810        820        830        840 
KAQRYTELYA AEFVKNLKAE PVGKYRLAVV ELEDEELAKK VAQIATGRDK ELVLLVVGGG 

       850        860        870        880        890 
RVTVYTGGAD VGPIVKALRE VGFRGGGSRT FAQGVYSGDV KTLIDAVKRA LA

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed: 11792869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009441 Genomic DNA. Translation: AAL65007.1.
RefSeqNP_560825.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZSV6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1466141.
GenomeReviewsGene locus PAE3565 in contig AE009441_GR.
KEGGpai:PAE3565.
NMPDRfig|178306.1.peg.2515.

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycPAER178306:PAE3565-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[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.
IPR022429. Ala-tRNA_synth_arc.
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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_PYRAE
AccessionPrimary (citable) accession number: Q8ZSV6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 56 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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