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Q7V419 (SYA_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:PMT_2157
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

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_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 – 892892Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075173

Sites

Metal binding5741Zinc Potential
Metal binding5781Zinc Potential
Metal binding6761Zinc Potential
Metal binding6801Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q7V419 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7C87B13F8F589313

FASTA89296,492
        10         20         30         40         50         60 
MAVARSLRSG DSRPRTGSEI RTAFLTFFAE RAHQVIPSAS LVPEDPTVLL TIAGMLPFKP 

        70         80         90        100        110        120 
VFMGQAERPA PRATSSQKCI RTNDIENVGR TARHHTFFEM LGNFSFGDYF KQQAIEWAWE 

       130        140        150        160        170        180 
LTTEVFGLDP KNLVVSVFRE DDEAETIWRD VVGVNPKRIM RMDEADNFWA SGPTGPCGPC 

       190        200        210        220        230        240 
SEIYYDFKPD LGNDDIDLED DGRFVEFYNL VFMQYNRDGE GNLTPLANRN IDTGMGLERM 

       250        260        270        280        290        300 
AQILQGVPNN YETDIIYPLI ETAAGLAGLD YQKLDEKGKT SFKVIGDHCR AITHLICDGV 

       310        320        330        340        350        360 
TASNLGRGYI MRRLLRRVVR HGRLVGIEKP FLQAMGEAAI ALMVEAYPQL EERRKLILAE 

       370        380        390        400        410        420 
LNREEARFLE TLERGEKVLA DVLVANPQMI SGGQAFELYD TYGFPLELTQ EIAEEHGLTV 

       430        440        450        460        470        480 
DLQGFEQAMD QQRQRAKAAA VSIDLTLQGA IEQMAAELEA TRFQGYEVLE QPCCVLALVV 

       490        500        510        520        530        540 
NGESAERASA GDSVQIVLDT TPFYGESGGQ VGDHGVLSGE GSGGNGVIVT VDDVSRHRNV 

       550        560        570        580        590        600 
FVHFGRIERG TLALGDLVNA QVDRACRRRA QANHTATHLL QAALKQVVDS GIGQAGSLVD 

       610        620        630        640        650        660 
FDRLRFDFHC ARAVTAKELE QIEALINGWI MESHDLIVEE MSIQEAKAAG AVAMFGEKYA 

       670        680        690        700        710        720 
DVVRVVDVPG VSMELCGGTH VANTAEIGLF KIVAESSVAA GIRRIEAVAG PAVLAYLNER 

       730        740        750        760        770        780 
DEVVKKLLER LKVQPSEIVE RVTSLQEELK SSQKALTAAR AELAVAKSAA LATQAVAVGE 

       790        800        810        820        830        840 
YQLLVARLDG VEGAGLQNAA QGLLDQLGDG AAVVLGGLPD PSDEGKVILV AAFGKQLIAQ 

       850        860        870        880        890 
GQQAGKFIGS IAKRCGGGGG GRPNLAQAGG RDGAALDGAL EAAKVDLQQA LG

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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: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX548175 Genomic DNA. Translation: CAE22331.1.
RefSeqNP_895981.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V419.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1727594.
GenomeReviewsGene locus PMT_2157 in contig BX548175_GR.
KEGGpmt:PMT2157.
NMPDRfig|74547.1.peg.2148.
PATRIC23013229. VBIProMar135351_2737.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBQ7V419.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycPMAR74547:PMT2157-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_PROMM
AccessionPrimary (citable) accession number: Q7V419
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 53 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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