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P35029 (SYA_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:Saci_1455
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length907 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
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 – 907907Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075276

Sites

Metal binding6061Zinc By similarity
Metal binding6101Zinc By similarity
Metal binding7101Zinc By similarity
Metal binding7141Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P35029 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 86807784D2351F3E

FASTA907103,899
        10         20         30         40         50         60 
MVKANENEYR LNFFLSRGYE RKICRSCSTP FWTLDKSKEN CSDVPCTDYY FFDIKIKSPP 

        70         80         90        100        110        120 
LTVRESREKF LRFFEKRGHT IVPPKPVVAK WRDDLYLTIA SIVDFQPFVT SGLAKPPANP 

       130        140        150        160        170        180 
LVVSQPCIRL EDVDNVGITF GRHLTTFEMA AHHAFNYPDK QIYWKDETVA FAKEFFTEEL 

       190        200        210        220        230        240 
GIPEDQLNFK ESWWEGGGNA GPCFEVTVGG LELATLVFMQ YEIRGQDYVP LKLKIVDTGY 

       250        260        270        280        290        300 
GVERIAWFTQ RTPTAFHAIY GNLVSSFYKK IGVGEVNNEL LKAAAIYAGR IDPDIKETIT 

       310        320        330        340        350        360 
AHREHLAKQL GLDLKYVNEE LTRAARVFQV LDHTKTIALM LADGLVPSNS GEGYLGRLLI 

       370        380        390        400        410        420 
RRALRVLRLL GSDVKLHELI KDQIDYWKED FPQMLKNKDY IVDAVINEEE KYNDTISKIP 

       430        440        450        460        470        480 
SILSTLSKKS KVDLDELINI YDSNGISPDL ILDEARKRNI NINVEIPHNF YSIVAKKHQN 

       490        500        510        520        530        540 
ALVRENRKDK IPKEVIDEIN NKKIEPTVPL YYKDQYLRTF NAKVLLNYKN FLVLDQTTFY 

       550        560        570        580        590        600 
PEGGGQIGDT GIIRSIEGNK QAKVIDTQKY KGVIVHILDK DSPFIQGEQV YGEIDWQRRY 

       610        620        630        640        650        660 
RIMKHHTVTH VILSATRRVL GEHAWQAGAE KTEYKGRLDV THYKLPTEEE IRKIEDFANY 

       670        680        690        700        710        720 
IINDRRKVRP LYIERTEAEM KYGVSIYAGG IPEGSEIRLI EIENWDIEGC GGTHLINTGE 

       730        740        750        760        770        780 
IGGVKIVNVE KLQDGVIRLE YVAGDMVSNY ARQQDEKLNE ISKLLNSPVS QINVRLKKHL 

       790        800        810        820        830        840 
EEYENLQNLL DKYRKIVLDR IQEIAERISV NGITIYILRD FIDEQLIKEV MRKITSNNQN 

       850        860        870        880        890        900 
IVISIRGKDT KNVEIATSKD IKVDKIVDEL RKIGGRGGGK GTYGSVSITV EEEKIIDTIR 


SAITNGV 

« Hide

References

« Hide 'large scale' references
[1]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed: 15995215] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[2]"Structure and transcription of the L11-L1-L10-L12 ribosomal protein gene operon from the extreme thermophilic archaeon Sulfolobus acidocaldarius."
Ramirez C., Shimmin L.C., Leggatt P., Matheson A.T.
J. Mol. Biol. 244:242-249(1994) [PubMed: 7966335] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-182.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000077 Genomic DNA. Translation: AAY80776.1.
X59038 Genomic DNA. Translation: CAA41766.1.
PIRS53652.
RefSeqYP_256069.1. NC_007181.1.

3D structure databases

ProteinModelPortalP35029.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3473494.
GenomeReviewsGene locus Saci_1455 in contig CP000077_GR.
KEGGsai:Saci_1455.
NMPDRfig|330779.3.peg.2148.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG392147.
OMAGESKTDQ.
PhylomeDBP35029.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycSACI330779:SACI_1455-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_SULAC
AccessionPrimary (citable) accession number: P35029
Secondary accession number(s): Q4J8V2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: August 30, 2005
Last modified: January 25, 2012
This is version 78 of the entry and version 2 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