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Q8TJA2 (SYP_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. 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:MA_3886
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifier188937 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length480 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
Reference 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 – 480480Proline--tRNA ligase HAMAP MF_01571
PRO_0000249160

Sequences

Sequence LengthMass (Da)Tools
Q8TJA2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F458E8DE74D77E7A

FASTA48054,869
        10         20         30         40         50         60 
MAESEKEAAL PPKEEFSDWY NELLWMAEIM DVRYPVKGLY VWYPFGFAIR RSTYNIIREI 

        70         80         90        100        110        120 
LDNSGHQETL FPLLIPENEF MKEAEHIKGF ENEVYWVTHG GKDSLDIPLA LRPTSETAIY 

       130        140        150        160        170        180 
PMYKMWVRSH ADFPIKLYQI VNTFRYETKH TRPLIRLREI TSFKEAHTVH ATWEDAEAQV 

       190        200        210        220        230        240 
KEAVELYTEI YRRLAVPVLR SRRPDWDKFP GADYTDAIDA MMPDGRTLQI GTVHHLGDNF 

       250        260        270        280        290        300 
AKTFDIKYEA PDGEQRYAHQ TCYGISERSI AATISIHGDD KGLVLPPEIA PVQVVIIPII 

       310        320        330        340        350        360 
FKKGAEEVLA ACRDVQERLK KTGVKVEIDA SDLRPGAKYY RWEMKGVPLR LEIGPRDLEN 

       370        380        390        400        410        420 
NVAVSVRRDT GEKEQIPLPE IETGVLQKFE AIQNSLYEKA KVGLESRIFD CTELEEVKEK 

       430        440        450        460        470        480 
IQKGVATIPW CGKKECGLAM EDRIGAGILG IPLTPRGKGK EKCPVCGAET ETRVYVARTY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010299 Genomic DNA. Translation: AAM07237.1.
RefSeqNP_618757.1. NC_003552.1.

3D structure databases

HSSPHSSP built from PDB template 1NJ2 based on UniProtKB O26708.
ProteinModelPortalQ8TJA2.
SMRQ8TJA2. Positions 15-480.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1475779.
GenomeReviewsGene locus MA_3886 in contig AE010299_GR.
KEGGmac:MA3886.
NMPDRfig|188937.1.peg.3783.

Phylogenomic databases

HOGENOMHBG334108.
OMAKFAEYEL.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycMACE188937:MA3886-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_METAC
AccessionPrimary (citable) accession number: Q8TJA2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2002
Last modified: January 25, 2012
This is version 65 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