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UniProtKB/Swiss-Prot entry P27652

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LUCI_RENRE
Primary accession number P27652
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 47)
Name and origin of the protein
Protein name Renilla-luciferin 2-monooxygenase
Synonyms EC 1.13.12.5
Renilla-type luciferase
Gene name None
From
Renilla reniformis (Sea pansy) [TaxID: 6136] 
Taxonomy Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Pennatulacea; Sessiliflorae; Renillidae; Renilla.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1674607 [NCBI, ExPASy, EBI, Israel, Japan]
Lorenz W.W., McCann R.O., Longiaru M., Cormier M.J.;
"Isolation and expression of a cDNA encoding Renilla reniformis luciferase.";
Proc. Natl. Acad. Sci. U.S.A. 88:4438-4442(1991).
Comments
  • CATALYTIC ACTIVITY: Renilla luciferin + O2 = oxidized Renilla luciferin + CO2 + light.
  • SUBUNIT: 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.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M63501; AAA29804.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
2PSD; X-ray; 1.40 A; A=3-311.[ExPASy / RCSB / EBI]
2PSE; X-ray; 2.50 A; A=3-311.[ExPASy / RCSB / EBI]
2PSF; X-ray; 1.40 A; A/B=3-311.[ExPASy / RCSB / EBI]
2PSH; X-ray; 1.79 A; A/B=1-311.[ExPASy / RCSB / EBI]
2PSJ; X-ray; 1.80 A; A/B=1-311.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2PSD; -.
2PSE; -.
2PSF; -.
2PSH; -.
2PSJ; -.
ModBase P27652.
Ontologies
GO
GO:0016831; Molecular function: carboxy-lyase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0050248; Molecular function: Renilla-luciferin 2-monooxygenase activity (inferred from electronic annotation from EC).
GO:0008218; Biological process: bioluminescence (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000073; AB_hydrolase_1.
IPR000639; Epox_hydrolase-like.
Graphical view of domain structure.
Pfam PF00561; Abhydrolase_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00412; EPOXHYDRLASE.
BLOCKS P27652.
ProtoNet P27652.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Decarboxylase; Direct protein sequencing; Luminescence; Lyase; Monooxygenase; Oxidoreductase; Photoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   311  311     Renilla-luciferin 2-monooxygenase. PRO_0000084523
CONFLICT   219   219        W -> L (in Ref. 1; AA sequence). 
HELIX   10    13  4      
HELIX   17    23  7      
STRAND   25    29  5      
STRAND   32    38  7      
STRAND   45    50  6      
HELIX   57    60  4      
TURN   61    63  3      
HELIX   64    66  3      
TURN   67    70  4      
STRAND   71    76  6      
HELIX   94   105  12      
STRAND   112   119  8      
HELIX   121   132  12      
STRAND   136   144  9      
HELIX   160   167  8      
HELIX   170   175  6      
TURN   176   178  3      
HELIX   180   183  4      
HELIX   185   188  4      
HELIX   196   203  8      
HELIX   204   206  3      
STRAND   208   210  3      
HELIX   211   213  3      
HELIX   214   221  8      
TURN   226   228  3      
HELIX   231   245  15      
STRAND   252   259  8      
HELIX   263   270  8      
STRAND   273   286  14      
HELIX   287   289  3      
HELIX   292   307  16      
Sequence information
Length: 311 AA [This is the length of the unprocessed precursor] Molecular weight: 36022 Da [This is the MW of the unprocessed precursor] CRC64: 0A3FD025B4EC33FD [This is a checksum on the sequence] 
        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
P27652 in FASTA format

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