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A8MC04 (SYP_CALMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:Cmaq_1972
OrganismCaldivirga maquilingensis (strain ATCC 700844 / DSMZ 13496 / JCM 10307 / IC-167) [Complete proteome] [HAMAP]
Taxonomic identifier397948 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeCaldivirga

Protein attributes

Sequence length481 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 – 481481Proline--tRNA ligase HAMAP MF_01571
PRO_1000215547

Sequences

Sequence LengthMass (Da)Tools
A8MC04 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 466D63DF3D7D93A6

FASTA48155,799
        10         20         30         40         50         60 
MVRGPQGRPR SRWVSFIEWF NKVIMDAEVY DYRYPVKGAY IWRPYGVAIR RNVEALIRRL 

        70         80         90        100        110        120 
HDETGHQEVL FPVFIPYEFF SKESEHIRGF ESEVFWVSKG TGGEERLVLR PTSETAMMPM 

       130        140        150        160        170        180 
FKLWIRDHTD LPLRVYQIVS VFRAETKMTH PMIRLREISM FKEAHTAHAD RDDAERQVKE 

       190        200        210        220        230        240 
AVGIYRRIMD ELCIPYLISR RPDWDKFAGA VYTIAFDTIM PDGRTMQIGT VHYLGENFSR 

       250        260        270        280        290        300 
VFDVKYLGKD GQMHYIHTTS YGISERIIAS MIAVNGDDRG LLLPPRYAPI QVVVIPIMYG 

       310        320        330        340        350        360 
EDQSVLNYAK GVSGELLNAG VRVHVDDRRD KTPGWKYYHW ELKGVPIRLE VGPSDVKDNA 

       370        380        390        400        410        420 
VTLTRRDTFE KYAVERSNVV DAVRELMKAI EDNMRKSTWE WLRSHVRRSS NVSEAKALLN 

       430        440        450        460        470        480 
EGGVVEVPWS GDDECGRRIM ELTESDALGI PLDTDETPSD LRDAACSEKK AEYWLRLSRR 


Y 

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References

[1]"Complete sequence of Caldivirga maquilingensis IC-167."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700844 / DSMZ 13496 / JCM 10307 / IC-167.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000852 Genomic DNA. Translation: ABW02788.1.
RefSeqYP_001541778.1. NC_009954.1.

3D structure databases

ProteinModelPortalA8MC04.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8MC04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5708446.
GenomeReviewsGene locus Cmaq_1972 in contig CP000852_GR.
KEGGcma:Cmaq_1972.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
OMAKFAEYEL.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycCMAQ397948:CMAQ_1972-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_CALMQ
AccessionPrimary (citable) accession number: A8MC04
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 29 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