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Reviewed, UniProtKB/Swiss-Prot Q2NJ01 (SYP_AYWBP)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS
Gene names
Name: proS
Ordered Locus Names: AYWB_475
OrganismAster yellows witches'-broom phytoplasma (strain AYWB) [Complete proteome] [HAMAP]
Taxonomic identifier322098 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeCandidatus PhytoplasmaCandidatus Phytoplasma asteris

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) By similarity.

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01571

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprolyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Prolyl-tRNA synthetase HAMAP MF_01571
PRO_0000249115

Sequences

Sequence LengthMass (Da)Tools
Q2NJ01-1 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: CBF9ED2DA45716F8

FASTA47454,536
        10         20         30         40         50         60 
MKTMKRVKTV ATRLSDFGKW YTDICLKAEL IAYSEAKGFI IYLPYGYALW ENIQKHLNCT 

        70         80         90        100        110        120 
LQKTGHQNVY FPLVFPEKLF HKEKEHIQGF SPEAAMITTT GKKNLSEKLV IRPTSEILFS 

       130        140        150        160        170        180 
QYYSKTITSY RDLPKLYNQW CNVVRWEKTT KPFLRGKEFL WQEGHTVHAT EQEAMQQTLS 

       190        200        210        220        230        240 
ILDIYQKLGK DLLALPFVCG KKTETEKFAG ALITYSIEAL MHDGQALQAG TSHYLGIIFA 

       250        260        270        280        290        300 
KSFQIQFQDC DNQKKYAHQT SWGVSTRLIG ALIMVHSDDE GLVLPPYVAP MQIVIIPLQT 

       310        320        330        340        350        360 
QDESVKQVSE NLFSILQKNY RVHLDLQDKT AGWKFSQYEL KGVPLRIEIG KRGLENDEVT 

       370        380        390        400        410        420 
IFQRYNFAKQ NIKIKDFPSQ IPQLFETMHN NMYQKALQHL EQNRKQATTY EEFKTYLKQG 

       430        440        450        460        470 
GYVAMSISGT DAELQIKQET GATARVILET NLITANCPVT NKKALQTVLF ARAY 

« Hide

References

[1]"Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts."
Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.
J. Bacteriol. 188:3682-3696(2006) [PubMed: 16672622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000061 Genomic DNA. Translation: ABC65592.1.
RefSeqYP_456671.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3865854.
GenomeReviewsGene locus AYWB_475 in contig CP000061_GR.
KEGGayw:AYWB_475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2NJ01.
OMAQ2NJ01. CIEAMMQ.

Family and domain databases

HAMAPMF_01571.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR004499. Pro-tRNA-synth_IIa_pro-type.
IPR016061. Pro-tRNA_synth_II_C.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit.
PANTHERPTHR11451:SF6. ProS_fam_I. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00408. proS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_AYWBP
AccessionPrimary (citable) accession number: Q2NJ01
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: February 7, 2006
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents