ID   A0A3B4X2A2_SERLL        Unreviewed;       683 AA.
AC   A0A3B4X2A2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Cryptochrome-2-like {ECO:0000313|Ensembl:ENSSLDP00000006958.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000006958.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000006958.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3B4X2A2; -.
DR   Ensembl; ENSSLDT00000007182.1; ENSSLDP00000006958.1; ENSSLDG00000005500.1.
DR   GeneTree; ENSGT00940000159073; -.
DR   Proteomes; UP000261360; Unplaced.
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}.
FT   DOMAIN          3..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          494..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..664
FT                   /note="Basic and acidic 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   683 AA;  77962 MW;  52B36066E8D84B2E CRC64;
     MVVNSVHWFR KCLRLHDNPA LQEALNGADT VRCVYILDPW FAGAANVGIN RWRFLLEALE
     DLDSSLKKLN SRLFVIRGQP TDVFPRLFKE WKVTRLTFEY DPEPYGKERD GAIIKMAQEF
     GVETIVRNSH TLYNLDRIIE MNNNSPPLTF KRFQTIVSRL ELPRRPLLPI TQQQMEKCHT
     KIADNHDQLY SIPSLEELGF RTEGLPQAVW RGGESEALDR LNKHLDKKVW VANLEHPRVN
     TCSLYASPTG LSPYLRFGCL SCRVLYYNLR ELYMKLRKRC SPPLSLFGQL LWREFFYTAA
     TNNPNFDRME GNPICVQIPW DQNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA
     VACFLTRGDL WISWESGMKV FEELLLDADW SVNAGSWMWL SCSAFFQQFF HCYCPVGFGR
     RTDPSGDYIR RYIPILKDYP NRYIYEPWNA PEPVQKAANC VVGVDYPKPM INHAEGSRLN
     IERMKQVYQQ LSHYRGLNSP PRDPVDNEAA GCSTAPDSST VCASSTFALH PDLEDTLNCR
     PFQTPCTFSH TQASAAVTST SANHPLSLAA SPSLASTPIQ GSLSRSKPSS PSSSCPTLSS
     SSSPVLTLAQ TFPKRKSLAR KVRRSQRQRG RQICTPSGRE GERRAEEEER DDTGGDKRME
     EDVEPDEERM EEETSEKLAG LQQ
//