ID G3GYH7_CRIGR Unreviewed; 577 AA.
AC G3GYH7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cryptochrome-2 {ECO:0000313|EMBL:EGW03917.1};
GN ORFNames=I79_002856 {ECO:0000313|EMBL:EGW03917.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW03917.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR EMBL; JH000067; EGW03917.1; -; Genomic_DNA.
DR AlphaFoldDB; G3GYH7; -.
DR SMR; G3GYH7; -.
DR STRING; 10029.G3GYH7; -.
DR PaxDb; 10029-XP_007632599-1; -.
DR eggNOG; KOG0133; Eukaryota.
DR InParanoid; G3GYH7; -.
DR OMA; WHRTDLR; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF15; CRYPTOCHROME-2; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT DOMAIN 6..135
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 516..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 292..299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 390..392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 323
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 377
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 400
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 577 AA; 65595 MW; 698DF3D799120A51 CRC64;
MGADGASSVH WFRKGLRLHD NPALLAAVRG ARCVRCVYIL DPWFAASSSV GINRWRFLLQ
SLEDLDTSLR KLNSRLFVVR GQPADVFPRL FKEWGVTRLT FEYDSEPFGK ERDAAIMKMA
KEAGVEVVTE NSHTLYDLDR IIELNGQKPP LTYKRFQAII SRMELPKKPV GAVTSQQMEN
CRAEIQENHD DTYGVPSLEE LGFPTEGLGP AVWQGGETEA LARLDKHLER KAWVANYERP
RMNANSLLAS PTGLSPYLRF GCLSCRLFYY RLWDLYKKVK RNSTPPLSLF GQLLWREFFY
TAATNNPRFD RMEGNPICIQ IPWDRNPEAL AKWAEGKTGF PWIDAIMTQL RQEGWIHHLA
RHAVACFLTR GDLWVSWESG VRVFDELLLD ADFSVNAGSW MWLSCSAFFQ QFFHCYCPVG
FGRRTDPSGD YIRRYLPKLK GFPSRYIYEP WNAPESVQKA AKCIIGVDYP RPIVNHAETS
RLNIERMKQI YQQLSRYRGL CLLASVPSCV EDLSHPVAEP SSSQAGSISN TGSRPLSSGP
ASPKRKLEAA EEPPGEELSK RARVTEMPAQ EPQTKDA
//
