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Database: UniProt
Entry: I3J8U6_ORENI
LinkDB: I3J8U6_ORENI
Original site: I3J8U6_ORENI 
ID   I3J8U6_ORENI            Unreviewed;       580 AA.
AC   I3J8U6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Cryptochrome-2 {ECO:0000313|Ensembl:ENSONIP00000005286.2};
GN   Name=LOC100709350 {ECO:0000313|Ensembl:ENSONIP00000005286.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005286.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000005286.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_013129259.1; XM_013273805.2.
DR   AlphaFoldDB; I3J8U6; -.
DR   STRING; 8128.ENSONIP00000044182; -.
DR   Ensembl; ENSONIT00000005290.2; ENSONIP00000005286.2; ENSONIG00000004200.2.
DR   eggNOG; KOG0133; Eukaryota.
DR   GeneTree; ENSGT00940000159073; -.
DR   HOGENOM; CLU_010348_3_4_1; -.
DR   TreeFam; TF323191; -.
DR   Proteomes; UP000005207; Linkage group LG7.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT   DOMAIN          3..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          509..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         289..296
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         387..389
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            320
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            374
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            397
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   580 AA;  66331 MW;  8C9BAE50AA078DE4 CRC64;
     MVVNSVHWFR KGLRLHDNPA LQEALNGADA VRCVYILDPF FAGAANVGIN RWRFLLEALE
     DLDSSLKKLN SRLFVVRGQP TDVFPRLFKE WNVTRLTFEY DPEPYGKERD GAIIKMAQEF
     GVETIVRNSH TLYNLDRIIE MNNNSPPLTF KRFQTIVSRL ELPRRPLPPI TQQQMDKCHT
     KIGDNHDQLY SIPSLEELGF RTAGLPPAVW RGGESQALDR LSKHLDKKVW VTSLEHPRVN
     TCSLYASPTG LSPYLRFGCL SCRVLYYNLR ELYMKVRKRC SPPLSLFGQL LWREFFYTAA
     TNNPNFDRMD GNPICVQIPW DQNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA
     VACFLTRGDL WISWESGMKV FEELLLDADW SVNAGSWMWL SCSAFFQQFF HCYCPVGFGR
     RTDPTGDYIR HYIPILKDYP NRYIYEPWNA PESLQKAANC VVGVDYPKPM INHAESSRLN
     IERMKQVYQQ LSHYRGLSLL ASVPTIQEEA EPPMTDESQT SSGPDSPQRV PANTEGAGCY
     EAPDSSTVCP SSTSAPHPDQ EHQAPCISSV ILIGNKEKRP
//
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