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Database: UniProt
Entry: H2EP72_HELAM
LinkDB: H2EP72_HELAM
Original site: H2EP72_HELAM 
ID   H2EP72_HELAM            Unreviewed;       528 AA.
AC   H2EP72;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Cryptochrome-1 {ECO:0000256|ARBA:ARBA00021159};
OS   Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Helicoverpa.
OX   NCBI_TaxID=29058 {ECO:0000313|EMBL:AEX49898.1};
RN   [1] {ECO:0000313|EMBL:AEX49898.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu P.J., Wu K.M., Cheng P.;
RT   "Cloning, sequence analysis and expression of cryptochrome 1 gene in cotton
RT   bollworm, Helicpverpa armigera.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGA11657.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu P., Wu K.;
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGA11657.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xiao H., Cheng P.;
RT   "Up-regulated cryptochrome genes expression in cotton bollworm (Helicoverpa
RT   armigera) during migrating over the Bohai Sea.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004556}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862}.
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DR   EMBL; JN997418; AEX49898.1; -; mRNA.
DR   EMBL; JQ713131; AGA11657.1; -; mRNA.
DR   EMBL; JQ713134; AGA11660.1; -; mRNA.
DR   EMBL; JQ713135; AGA11661.1; -; mRNA.
DR   AlphaFoldDB; H2EP72; -.
DR   SMR; H2EP72; -.
DR   EnsemblMetazoa; XM_049843844.1; XP_049699801.1; LOC110372048.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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:SF17; CRYPTOCHROME-1; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
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   2: Evidence at transcript level;
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}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         242
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         300..307
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         399..401
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            331
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            386
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            409
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   528 AA;  60644 MW;  4AFAAD1978257ED2 CRC64;
     MLGGSVLWFR HGLRLHDNPS LHSALEEKGF PFFPIFIFDG ETAGTKLVGY NRMRYLLEAL
     DDLDSQFKKF GGRLIMLKGK PNVVFRRLWE EFGIRKLCFE QDCEPVWRAR DDSVKSACKE
     IGVVCREHVS HTLWEPETVI KANGGIPPLT YQMFLHTVAT IGDPPRPVPN IDFTGVKFGS
     LPECFYQEFT VYDKTPKPED LGVFLENEDI RMIRWVGGET TALKQMQQRL SVEYETFLRG
     SYLPTHGNPD LLGPPISLSP ALRFGCLSVR SFYWAVQDLF RQVHQGRLTT NSASHFITGQ
     LIWREYFYTM SVNNPNYGQM AGNPICLDIP WKNPEGDELQ RWVEGRTGFP FVDAAMRQLR
     TEGWLHHAAR NTVASFLTRG TLWLSWEHGL NHFLKYLLDA DWSVCAGNWM WVSSSAFEAL
     LDSGECACPV RLGQRLDPSG EYVRRYVPEL ARMPVEYIYE PWKAPIDVQE RATCVIGKDY
     PAPVVNHLVA AQRNKNAMKE LRHMLQKAPP HCCPSSEDEI RQFMWLNE
//
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