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Database: UniProt
Entry: A0A433T5M7_ELYCH
LinkDB: A0A433T5M7_ELYCH
Original site: A0A433T5M7_ELYCH 
ID   A0A433T5M7_ELYCH        Unreviewed;       529 AA.
AC   A0A433T5M7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN   ORFNames=EGW08_015338 {ECO:0000313|EMBL:RUS76899.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS76899.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS76899.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS76899.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS76899.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) 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   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUS76899.1}.
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DR   EMBL; RQTK01000625; RUS76899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433T5M7; -.
DR   STRING; 188477.A0A433T5M7; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
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:SF9; (6-4)-PHOTOLYASE, ISOFORM A; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 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:UP000271974}.
FT   DOMAIN          6..135
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          488..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         251..255
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         291..298
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         389..391
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            322
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            376
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            399
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   529 AA;  60204 MW;  0E5C65BD889E8F2E CRC64;
     MSQKCHRVIH WFRKGLRLHD NPALIEACKD ASELYPVFVL DPWFVTNSNV GANRWRFLAQ
     TLDDLDKQLK LLKLRLFVVR GNPETELEKL CKKWKITKLT YEVDTEPYAV ARDERVGKTM
     EDLGVSVIPC VSHTLYDVHS IVKINGGKAP LTYQSFQTAA SRLGPPPQAL PAPTLQDLPG
     CRNLASDAHG KEFEIPSLTE LRVCESDLGP NLYPGGETEA LDRMERHLKK VNWICSFEKP
     KTEPNSLLPS TTVLSPYLKF GCLSARLFYH KIINVYKGKK HSQPPVSLIG QVLWREFYYT
     VAAVTPNFDK MEGNPVCKQI PWQENADHLN AWKQGRTGYP FIDAVMTQLR QEGWIHHLAR
     HAVACFLTRG DLWVSWEEGQ KEFEKLLLDA DWSLNAGNWM WLSASAFFHQ YFRVYSPVAF
     GKKTDPNGDF IRKYIPVLKK FPAKFIFEPW KAPASMQQAA GCIIGKDYPK PIVDHDVVRQ
     KNIQKMAAAY AKSKSSTSET NKNGHKELSS KKRQSDDVGD GPSKKKKKS
//
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