Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - O77059 (CRY1_DROME)

Entry version 164 (25 May 2022)
Sequence version 1 (01 Nov 1998)
Previous versions | rss
Add a publicationFeedback
Protein

Cryptochrome-1

Gene

cry

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Blue light-dependent regulator that is the input of the circadian feedback loop. Has no photolyase activity for cyclobutane pyrimidine dimers or 6-4 photoproducts. Regulation of expression by light suggests a role in photoreception for locomotor activity rhythms. Functions, together with per, as a transcriptional repressor required for the oscillation of peripheral circadian clocks and for the correct specification of clock cells. Genes directly activated by the transcription factors Clock (Clk) and cycle (cyc) are repressed by cry. Necessary for light-dependent magnetosensitivity, an intact circadian system is not required for the magnetoreception mechanism to operate. Required for both the naive and trained responses to magnetic field, consistent with the notion that cry is in the input pathway of magnetic sensing.

9 Publications

Miscellaneous

Unstable upon light exposure. Light induces the degradation of cry, likely due to conformational change in the photoreceptor leading to targeting to the proteasome.
Appears to bind 5,10-methenyltetrahydrofolate at substoichiometric levels.1 Publication

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD4 PublicationsNote: Binds 1 FAD per subunit. The bound form of FAD in the inactive state of cry is oxidized FAD, not reduced. After activation by blue light the FAD is in an anionic radical state, which would be paramagnetic. Green light, which reduces levels of radical intermediate, has an antagonistic effect on function.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei237FAD2 Publications1
Binding sitei265FAD2 Publications1
Binding sitei267FAD; via amide nitrogenBy similarity1
Binding sitei311FAD2 Publications1
Binding sitei378FAD2 Publications1
Binding sitei416FAD2 Publications1
Binding sitei419FAD2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi410 – 412FAD2 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPhotoreceptor protein, Receptor, Repressor
Biological processBiological rhythms, Sensory transduction, Transcription, Transcription regulation
LigandChromophore, FAD, Flavoprotein, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-DME-432395, Degradation of TIM
R-DME-432553, Phosphorylation of PER and TIM
R-DME-538864, Degradation of CRY

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O77059

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cryptochrome-1
Short name:
DmCRY1Imported
Short name:
dcryImported
Alternative name(s):
Blue light photoreceptorImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cryImported
ORF Names:CG3772
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3R

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0025680, cry

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		VectorBase:FBgn0025680

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Flies exhibit poor synchronization to light-dark cycles and show no response to brief light pulses. Mutant abolishes rhythmic tim and per expression in photoreceptor and glial cells, but not within certain pacemaker neurons of adult brain.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi337C → A: Accelerates formation and decay of the FAD radical. 1 Publication1
Mutagenesisi397W → F: Abolishes formation of the FAD radical. 1 Publication1
Mutagenesisi410D → N in cryb: Loss of accumulation. 1 Publication1
Mutagenesisi416C → A: Accelerates decay of the FAD radical. 1 Publication1
Mutagenesisi420W → A: Abolishes formation of the FAD radical. 1 Publication1
Mutagenesisi523C → A: Accelerates formation and decay of the FAD radical. 1 Publication1
Mutagenesisi526S → A: Slows down the decay of the FAD radical. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003485971 – 542Cryptochrome-1Add BLAST542

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O77059

PRoteomics IDEntifications database

More...PRIDEi		O77059

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed at higher levels in the head than in body and it is more expressed in antennae than in legs, wings and mouth appendages. Prominent expression is seen in cells of the lateral brain, which are close to or coincident with the clock neurons. Abundance oscillates in a circadian manner.3 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is regulated by light and circadian rhythms. Under circadian regulation, expression is influenced by the clock pacemaker genes period, timeless, Clock and cycle.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0025680, Expressed in adult Malpighian tubule (Drosophila) and 39 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O77059, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with tim and per; promoted by light conditions (PubMed:10417378, PubMed:11448767). Interaction with tim irreversibly commits tim to proteasomal degradation (PubMed:10417378).

Interacts with l1G0136/CG8198 (PubMed:26569474).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		67302, 28 interactors

Database of interacting proteins

More...DIPi		DIP-29424N

Protein interaction database and analysis system

More...IntActi		O77059, 1 interactor

STRING: functional protein association networks

More...STRINGi		7227.FBpp0083150

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1542
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		O77059

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O77059

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 140Photolyase/cryptochrome alpha/betaAdd BLAST136

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

FAD-binding region regulates cry stability, cry-tim interaction, and circadian photosensitivity.1 Publication
Photolyase/cryptochrome alpha/beta domain is sufficient for light detection and phototransduction.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DNA photolyase class-1 family.Sequence analysis

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0133, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_010348_3_4_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O77059

Identification of Orthologs from Complete Genome Data

More...OMAi		IWFRHGL

Database of Orthologous Groups

More...OrthoDBi		378952at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O77059

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.620, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50267

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036134, Crypto/Photolyase_FAD-like_sf
IPR036155, Crypto/Photolyase_N_sf
IPR005101, Cryptochr/Photolyase_FAD-bd
IPR002081, Cryptochrome/DNA_photolyase_1
IPR006050, DNA_photolyase_N
IPR014729, Rossmann-like_a/b/a_fold

The PANTHER Classification System

More...PANTHERi		PTHR11455, PTHR11455, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00875, DNA_photolyase, 1 hit
PF03441, FAD_binding_7, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00147, DNAPHOTLYASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48173, SSF48173, 1 hit
SSF52425, SSF52425, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51645, PHR_CRY_ALPHA_BETA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

O77059-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATRGANVIW FRHGLRLHDN PALLAALADK DQGIALIPVF IFDGESAGTK 
        60         70         80         90        100
NVGYNRMRFL LDSLQDIDDQ LQAATDGRGR LLVFEGEPAY IFRRLHEQVR 
       110        120        130        140        150
LHRICIEQDC EPIWNERDES IRSLCRELNI DFVEKVSHTL WDPQLVIETN 
       160        170        180        190        200
GGIPPLTYQM FLHTVQIIGL PPRPTADARL EDATFVELDP EFCRSLKLFE 
       210        220        230        240        250
QLPTPEHFNV YGDNMGFLAK INWRGGETQA LLLLDERLKV EQHAFERGFY 
       260        270        280        290        300
LPNQALPNIH DSPKSMSAHL RFGCLSVRRF YWSVHDLFKN VQLRACVRGV 
       310        320        330        340        350
QMTGGAHITG QLIWREYFYT MSVNNPNYDR MEGNDICLSI PWAKPNENLL 
       360        370        380        390        400
QSWRLGQTGF PLIDGAMRQL LAEGWLHHTL RNTVATFLTR GGLWQSWEHG 
       410        420        430        440        450
LQHFLKYLLD ADWSVCAGNW MWVSSSAFER LLDSSLVTCP VALAKRLDPD 
       460        470        480        490        500
GTYIKQYVPE LMNVPKEFVH EPWRMSAEQQ EQYECLIGVH YPERIIDLSM 
       510        520        530        540 
AVKRNMLAMK SLRNSLITPP PHCRPSNEEE VRQFFWLADV VV
Length:542
Mass (Da):62,513
Last modified:November 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAB0019E5447BF56E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti232L → H in BAA35000 (Ref. 3) Curated1
Sequence conflicti335D → E in BAA35000 (Ref. 3) Curated1
Sequence conflicti348N → D in BAA35000 (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF099734 mRNA Translation: AAC83828.1
AB018400 mRNA Translation: BAA33787.1
AB019389 mRNA Translation: BAA35000.1
AE014297 Genomic DNA Translation: AAF55649.1
AY051514 mRNA Translation: AAK92938.1

NCBI Reference Sequences

More...RefSeqi		NP_732407.1, NM_169852.2

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0083736; FBpp0083150; FBgn0025680

Database of genes from NCBI RefSeq genomes

More...GeneIDi		42305

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG3772

UCSC genome browser

More...UCSCi		CG3772-RA, d. melanogaster

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099734 mRNA Translation: AAC83828.1
AB018400 mRNA Translation: BAA33787.1
AB019389 mRNA Translation: BAA35000.1
AE014297 Genomic DNA Translation: AAF55649.1
AY051514 mRNA Translation: AAK92938.1
RefSeqiNP_732407.1, NM_169852.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GU5X-ray2.30A/B1-539[»]
4JZYX-ray2.34A/B1-540[»]
4K03X-ray3.20A/B1-542[»]
6WTBX-ray2.58A/B1-539[»]
AlphaFoldDBiO77059
SMRiO77059
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi67302, 28 interactors
DIPiDIP-29424N
IntActiO77059, 1 interactor
STRINGi7227.FBpp0083150

Proteomic databases

PaxDbiO77059
PRIDEiO77059

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		42305

Genome annotation databases

EnsemblMetazoaiFBtr0083736; FBpp0083150; FBgn0025680
GeneIDi42305
KEGGidme:Dmel_CG3772
UCSCiCG3772-RA, d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		42305
FlyBaseiFBgn0025680, cry
VEuPathDBiVectorBase:FBgn0025680

Phylogenomic databases

eggNOGiKOG0133, Eukaryota
HOGENOMiCLU_010348_3_4_1
InParanoidiO77059
OMAiIWFRHGL
OrthoDBi378952at2759
PhylomeDBiO77059

Enzyme and pathway databases

ReactomeiR-DME-432395, Degradation of TIM
R-DME-432553, Phosphorylation of PER and TIM
R-DME-538864, Degradation of CRY
SignaLinkiO77059

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		42305, 0 hits in 3 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		cry, fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		42305

Protein Ontology

More...PROi		PR:O77059

Gene expression databases

BgeeiFBgn0025680, Expressed in adult Malpighian tubule (Drosophila) and 39 other tissues
GenevisibleiO77059, DM

Family and domain databases

Gene3Di3.40.50.620, 1 hit
IDEALiIID50267
InterProiView protein in InterPro
IPR036134, Crypto/Photolyase_FAD-like_sf
IPR036155, Crypto/Photolyase_N_sf
IPR005101, Cryptochr/Photolyase_FAD-bd
IPR002081, Cryptochrome/DNA_photolyase_1
IPR006050, DNA_photolyase_N
IPR014729, Rossmann-like_a/b/a_fold
PANTHERiPTHR11455, PTHR11455, 1 hit
PfamiView protein in Pfam
PF00875, DNA_photolyase, 1 hit
PF03441, FAD_binding_7, 1 hit
PRINTSiPR00147, DNAPHOTLYASE
SUPFAMiSSF48173, SSF48173, 1 hit
SSF52425, SSF52425, 1 hit
PROSITEiView protein in PROSITE
PS51645, PHR_CRY_ALPHA_BETA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCRY1_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O77059
Secondary accession number(s): Q9TYA0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 1, 1998
Last modified: May 25, 2022
This is version 164 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again