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P27652 (LUCI_RENRE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Renilla-luciferin 2-monooxygenase

EC=1.13.12.5
Alternative name(s):
Renilla-type luciferase
OrganismRenilla reniformis (Sea pansy)
Taxonomic identifier6136 [NCBI]
Taxonomic lineageEukaryotaMetazoaCnidariaAnthozoaOctocoralliaPennatulaceaSessilifloraeRenillidaeRenilla

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Renilla luciferin + O2 = oxidized Renilla luciferin + CO2 + light.

Subunit structure

Monomer.

Miscellaneous

This luciferase produces light with a wavelength of 480 nm. In presence of a green fluorescence protein (GFP) it produces a green fluorescence at 509 nm.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Renilla-luciferin 2-monooxygenase
PRO_0000084523

Experimental info

Sequence conflict2191W → L AA sequence Ref.1

Secondary structure

......................................................... 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27652 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 0A3FD025B4EC33FD

FASTA31136,022
        10         20         30         40         50         60 
MTSKVYDPEQ RKRMITGPQW WARCKQMNVL DSFINYYDSE KHAENAVIFL HGNAASSYLW 

        70         80         90        100        110        120 
RHVVPHIEPV ARCIIPDLIG MGKSGKSGNG SYRLLDHYKY LTAWFELLNL PKKIIFVGHD 

       130        140        150        160        170        180 
WGACLAFHYS YEHQDKIKAI VHAESVVDVI ESWDEWPDIE EDIALIKSEE GEKMVLENNF 

       190        200        210        220        230        240 
FVETMLPSKI MRKLEPEEFA AYLEPFKEKG EVRRPTLSWP REIPLVKGGK PDVVQIVRNY 

       250        260        270        280        290        300 
NAYLRASDDL PKMFIESDPG FFSNAIVEGA KKFPNTEFVK VKGLHFSQED APDEMGKYIK 

       310 
SFVERVLKNE Q 

« Hide

References

[1]"Isolation and expression of a cDNA encoding Renilla reniformis luciferase."
Lorenz W.W., McCann R.O., Longiaru M., Cormier M.J.
Proc. Natl. Acad. Sci. U.S.A. 88:4438-4442(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63501 mRNA. Translation: AAA29804.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PSDX-ray1.40A3-311[»]
2PSEX-ray2.50A3-311[»]
2PSFX-ray1.40A/B3-311[»]
2PSHX-ray1.79A/B1-311[»]
2PSJX-ray1.80A/B1-311[»]
ProteinModelPortalP27652.
SMRP27652. Positions 3-309.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2303641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16919.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSPR00412. EPOXHYDRLASE.
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP27652.

Entry information

Entry nameLUCI_RENRE
AccessionPrimary (citable) accession number: P27652
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references