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Q7V3N0 (SYA_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PMM0044
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length886 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
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 – 886886Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075174

Sites

Metal binding5641Zinc Potential
Metal binding5681Zinc Potential
Metal binding6661Zinc Potential
Metal binding6701Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q7V3N0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 9006E66E828095DB

FASTA88699,139
        10         20         30         40         50         60 
MKSQTKNTPI TGDEIRKEFL NFYHEKLHKI IPSASLIPDD PTVMLTIAGM LPFKPVFLGL 

        70         80         90        100        110        120 
KERPSKRATS SQKCIRTNDI ENVGVTARHH TFFEMLGNFS FGDYFKKEAI EWAWELVTDI 

       130        140        150        160        170        180 
YGLSAENIIV SVFHEDDDSV KIWKEDIGIH PKRIIKLGEK DNFWSSGKTG PCGPCSELYF 

       190        200        210        220        230        240 
DFKPEKGVQN IDLEDGDRFI EFYNLVFMQY NRDPDGQLTD LKYKNIDTGM GLERMAQILQ 

       250        260        270        280        290        300 
KKKNNYETDL IFPIIQKASE ISKIDYYSSG ERTKISLKII GDHIRAVIHL ISDGVIASNL 

       310        320        330        340        350        360 
GRGYILRRLI RRMVRHGRLL GLKNEFLSKL ASVGIKLMQE NYPDLKNNCD HILSEIKIEE 

       370        380        390        400        410        420 
IRFRETLERG EKLLDELISS GQKMITGFKA FELYDTYGFP LELTEEIAQE NNIGVDVKGF 

       430        440        450        460        470        480 
DKEMSAQKER AKAASQIIDL TLEGSLEREI DLFDKTLFNG YDSLDSDAEI KGIFLESTLV 

       490        500        510        520        530        540 
KQASEGQKVL IVLDQTSFYG ESGGQVGDIG TILSNDLEVV VDNVIRKKNV FLHYGIVKKG 

       550        560        570        580        590        600 
ILSLGQKVKT KVNDLARAKA AANHTATHLL QSALKVVVNE SVGQKGSLVA FNKLRFDFNS 

       610        620        630        640        650        660 
SKPITKDQIF KVETLVNSWI LENHSLNIKN MAKSEALERG AVAMFGEKYD DEVRVVDVPS 

       670        680        690        700        710        720 
VSMELCGGTH VKTTSELGCF KIISEEGISA GVRRIEALSG QSAFEYFSDK NSLVSQLCDL 

       730        740        750        760        770        780 
LKANPNQLLD RVNSLQSELI NKNKEIQKMK DEIAYFKYSS LSSSANKVGL FSLIISQLDG 

       790        800        810        820        830        840 
LDGNSLQSAA LDLTSKLGDK SVVILGGIPD KENRKLLFVV SFGEDLVKRG MHAGKLINDI 

       850        860        870        880 
SRICSGGGGG KPNFAQAGAK DIDKLNDALE YARKDLRTKL HSYSDK

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX548174 Genomic DNA. Translation: CAE18503.1.
RefSeqNP_892165.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V3N0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V3N0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1727222.
GenomeReviewsGene locus PMM0044 in contig BX548174_GR.
KEGGpmm:PMM0044.
NMPDRfig|59919.1.peg.44.
PATRIC23030718. VBIProMar68066_0045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ7V3N0.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycPMAR167540:PMM0044-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]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
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_PROMP
AccessionPrimary (citable) accession number: Q7V3N0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 54 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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