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Reviewed, UniProtKB/Swiss-Prot Q3MAQ7 (SYP_ANAVT)

Last modified November 24, 2009. Version 29. 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: Ava_2311
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length604 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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity.

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 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 – 604604Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000248639

Sequences

Sequence LengthMass (Da)Tools
Q3MAQ7-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: BA6200BEB7384C11

FASTA60467,688
        10         20         30         40         50         60 
MRLSQMLFVT LRDDPADAEI PSHKLLLRAG YIRRIGSGIY AYLPLMWRVL QKVSQIVREE 

        70         80         90        100        110        120 
MNAAGAQECL LPQLQPSELW KESGRWDTYT KAEGIMFSLI DRREQQLGLG PTHEEVITAI 

       130        140        150        160        170        180 
ARDMIRSYRQ LPLHLYQLQT KFRDEIRPRF GLMRGREFIM KDGYSFHVDE DSLKKTYQDM 

       190        200        210        220        230        240 
YQAYSNMLRR AGLAFRPVEA DSGAIGGSGS TEFMVLAEAG EDEVLYTDDG KYAANVEKAV 

       250        260        270        280        290        300 
SLPADAEPSQ FTAFEKRETP GTETIEKVTQ FLKASPTQIV KNVLYQTVYD NGVTVLVLVI 

       310        320        330        340        350        360 
IRGDQEVNEV KLQNELTKLA PNYGAKAIIN LTVPSAENQQ TWTAKSLPLG YIAPDIADEY 

       370        380        390        400        410        420 
IAANKQIHPK FVRFVDKTAV DLKNFITGAN EAGYHVVGAN WGEQFPLPEI VVDVRKARPG 

       430        440        450        460        470        480 
DRAIHDSTQI LKSARGIEVG HIFQLGTKYS QALGATYTNE QGEEKPLVMG CYGVGVSRLA 

       490        500        510        520        530        540 
QSAVEQSYDK DGIIWPVAIA PYHAIVTIPN INDAQQVEIA ERLYTELNQS GVETLLDDRN 

       550        560        570        580        590        600 
ERAGVKFKDA DLIGIPYRIV TGRAITNGKV EIVERATRQS QEIPIDEVIT TLQQWIKAAI 


EQKN 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000117 Genomic DNA. Translation: ABA21929.1.
RefSeqYP_322824.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MAQ7.

Genome annotation databases

GeneID3678919.
GenomeReviewsGene locus Ava_2311 in contig CP000117_GR.
KEGGava:Ava_2311.
NMPDRfig|240292.3.peg.191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3MAQ7.
OMADFVLGPT

Enzyme and pathway databases

BioCycAVAR240292:AVA_2311-MON.

Family and domain databases

HAMAPMF_01569.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR007214. YbaK/aa-tRNA-synth-assoc-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 2 hits.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_ANAVT
AccessionPrimary (citable) accession number: Q3MAQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 25, 2005
Last modified: November 24, 2009
This is version 29 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