Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2NFL1 (SYP_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Msp_1004
OrganismMethanosphaera stadtmanae (strain DSM 3091) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera

Protein attributes

Sequence length469 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 – 469469Proline--tRNA ligase HAMAP MF_01571
PRO_0000249163

Sequences

Sequence LengthMass (Da)Tools
Q2NFL1 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 93378A1173BE701A

FASTA46954,332
        10         20         30         40         50         60 
MKNFSEWFHN ILEEAELMDA RYPIKGMSVW LPRGFQIRKY ALNALQELLD KDHEEVLFPM 

        70         80         90        100        110        120 
LIPQSELAKE AIHVKGFEEE VYWVTKGGKR DLNEHLALRP TSETSIYPMF SLWVRSHMDL 

       130        140        150        160        170        180 
PIKVYQTVNT FRYETKHTRP LIRVREITTF NETHTAHATE EEAEKEVMEG IEIYKTFFDE 

       190        200        210        220        230        240 
LGIPYSISKR PEWDKFPGSK YTMAFDMIMP DGKTLQIATV HNLGTTFAHT FDIQFENEDG 

       250        260        270        280        290        300 
THDYVHQVCY GLSDRVIASL IAAHGDEKGL SLPPVVAPEQ VIIIPIIFKE NQDVVLNFTD 

       310        320        330        340        350        360 
NLEKLLKNNG IRVKQDKREL RPGKKYYEWE KRGVPLRIEV GPRDIENNTI VINRRDTGDK 

       370        380        390        400        410        420 
EFVDYDENTI VDVVKDRLDS ITHDMKEASN KFQEEKTFAI EKPEQIKKTI NKKGGIITCS 

       430        440        450        460 
WCGETDCGKD MEEKFDIDVL GTQESDLENK TCINCGKDAS YKVLISKTY 

« Hide

References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed: 16385054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 3091.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000102 Genomic DNA. Translation: ABC57392.1.
RefSeqYP_448035.1. NC_007681.1.

3D structure databases

ProteinModelPortalQ2NFL1.
SMRQ2NFL1. Positions 4-469.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NFL1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3855285.
GenomeReviewsGene locus Msp_1004 in contig CP000102_GR.
KEGGmst:Msp_1004.
NMPDRfig|339860.6.peg.963.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBQ2NFL1.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycMSTA339860:MSP_1004-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_METST
AccessionPrimary (citable) accession number: Q2NFL1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 44 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