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A2ST96 (SYP_METLZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline--tRNA ligase

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS
Gene names
Name:proS
Ordered Locus Names:Mlab_1386
OrganismMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) [Complete proteome] [HAMAP]
Taxonomic identifier410358 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum

Protein attributes

Sequence length477 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) By similarity. HAMAP MF_01571

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_01571

Subcellular location

Cytoplasm By similarity HAMAP MF_01571.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity. HAMAP MF_01571

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proline-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Proline--tRNA ligase HAMAP MF_01571
PRO_0000288420

Sequences

Sequence LengthMass (Da)Tools
A2ST96 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 3B42FA602354F866

FASTA47753,873
        10         20         30         40         50         60 
MAEETGALPS RTDFSAWYNE VIRRADIMDV RYPVKGLYVW YPFGFALRNH TYTLLRSLLN 

        70         80         90        100        110        120 
RDHEETLFPL LIPETEFMKE AEHIKGFEDE VYWVTHGGLS PLDVKLALRP TSETAIYPMY 

       130        140        150        160        170        180 
ALWVRSHADL PLKLYQVVNT FRYETKHTRP LIRLREITSF MESHTVHTDW DDANKQVEYE 

       190        200        210        220        230        240 
LGLATEFYRD LGVPIIISRR PDWDKFPGAD FTMAIDAVMP DGRTLQIGTV HHLGDHFSTT 

       250        260        270        280        290        300 
YNITYEDVNG EQKLASQTCF GISERCIAAI IAVHGDDKGL VLPATVAPTQ VVIIPIIVGK 

       310        320        330        340        350        360 
RGDEIMAAVE KLESELKAAG LRVKTDARDM RPGAKYYHWE LHGVPLRVEL GPRDLDNNQL 

       370        380        390        400        410        420 
VCANRLGVKT TIPRENAADS VKRLLDEAHD QILEKAEDHL SSHLKTVKTV DECNQSLEEN 

       430        440        450        460        470 
IVIVHWCGEK ACADKLEELT NSSLLGTGVR SKYVVDDEGP CIVCGKPGKT ALVGRSY 

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References

[1]"Complete genome sequence of Methanocorpusculum labreanum type strain Z."
Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:197-203(2009) [PubMed: 21304657] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43576 / DSM 4855 / Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000559 Genomic DNA. Translation: ABN07552.1.
RefSeqYP_001030819.1. NC_008942.1.

3D structure databases

ProteinModelPortalA2ST96.
SMRA2ST96. Positions 13-477.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2ST96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4795368.
GenomeReviewsGene locus Mlab_1386 in contig CP000559_GR.
KEGGmla:Mlab_1386.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBA2ST96.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycMLAB410358:MLAB_1386-MONOMER.

Family and domain databases

HAMAPMF_01571. Pro_tRNA_synth_type3.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-synth_IIa.
IPR004499. Pro-tRNA-synth_IIa_arc-type.
IPR017449. Pro-tRNA_synth_II.
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.
KOK01881.
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.
SMARTSM00946. ProRS-C_1. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF64586. Pro-tRNA_synth_II_C. 1 hit.
TIGRFAMsTIGR00408. ProS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_METLZ
AccessionPrimary (citable) accession number: A2ST96
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 6, 2007
Last modified: January 25, 2012
This is version 33 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