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B4RMJ8 (B4RMJ8_NEIG2) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Proline--tRNA ligase HAMAP-Rule MF_01569
EC=6.1.1.15 HAMAP-Rule MF_01569
Alternative name(s):
Prolyl-tRNA synthetase HAMAP-Rule MF_01569
Gene names
Name:proS HAMAP-Rule MF_01569
Ordered Locus Names:NGK_1358 EMBL ACF30032.1
OrganismNeisseria gonorrhoeae (strain NCCP11945) [Complete proteome] [HAMAP] EMBL ACF30032.1
Taxonomic identifier521006 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
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. HAMAP-Rule MF_01569 SAAS SAAS023717

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569 SAAS SAAS023717

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01569 SAAS SAAS023717

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01569 SAAS SAAS023717.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP-Rule MF_01569

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. HAMAP-Rule MF_01569

Sequences

Sequence LengthMass (Da)Tools
B4RMJ8 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: D47545836798FB16

FASTA59966,094
        10         20         30         40         50         60 
MEVGAKPAFF ALQSAPDLLL NLPVWKNTFM KASQFFISTL KEAPAEAAFA SHKLMIRAGL 

        70         80         90        100        110        120 
IKANASGLYT WMPMGLRVLR KVENVVREEM ARAGSVELLM PVVQPAELWQ ESGRWEFYGK 

       130        140        150        160        170        180 
ELLRLKDRHE RDFCMGPTCE EVIADIVRKE INSYKQLPKN FYHIQTKFRD EVRPRFGVMR 

       190        200        210        220        230        240 
AREFVMKDAY SFHADYASLQ ATYDAMYDAY CRIFTRLGLA FRPVAADTGS IGGTGSHEFQ 

       250        260        270        280        290        300 
VLAESGEDVI AYSDTSDYAA NIELAPTLPL KGERAAAQAV LTKVHTPNVK TIESLVEFLN 

       310        320        330        340        350        360 
IPVEQTLKSI VVEGENEGEL VLLLLRGDHE FNDIKAEKLA GVKSPLTMAS PAAIVEQFGA 

       370        380        390        400        410        420 
NGGSLGPVGF TGKVYADFAT EKGADWVIGA NEDDYHYTGF NFGRDAAEPE FVDLRNVVEG 

       430        440        450        460        470        480 
DESPDGQGRL KLARGIEVGH VFQLRGKYTQ AMNVSFLDNN GKSQIMEMGC YGIGITRVVA 

       490        500        510        520        530        540 
AAIEQNNDEK GIIWTKAMAP FEVVIVPMNY KKSDTVREAA DRIYAELLAA GADVLLDDRD 

       550        560        570        580        590 
ERAGVLLNDS ELLGIPHRIV IGDRALKEGN VEYAERRGNE AQAVAIGEIV ARVTASLNA

« Hide

References

[1]"Complete genome sequence of Neisseria gonorrhoeae NCCP11945."
Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.
J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCCP11945 EMBL ACF30032.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001050 Genomic DNA. Translation: ACF30032.1.
RefSeqYP_002001983.1. NC_011035.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING521006.NGK_1358.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF30032; ACF30032; NGK_1358.
GeneID6447227.
KEGGngk:NGK_1358.
PATRIC20341183. VBINeiGon87511_1457.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000076893.
KOK01881.
OMAIQPAELW.
ProtClustDBPRK09194.

Enzyme and pathway databases

BioCycNGON521006:GJ73-1382-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPMF_01569. Pro_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004500. Pro-tRNA-synth_IIa_bac-type.
IPR023717. Pro-tRNA-Synthase_IIa_type1.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB4RMJ8_NEIG2
AccessionPrimary (citable) accession number: B4RMJ8
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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