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Database: UniProt
Entry: A0A3Q1JVY3_ANATE
LinkDB: A0A3Q1JVY3_ANATE
Original site: A0A3Q1JVY3_ANATE 
ID   A0A3Q1JVY3_ANATE        Unreviewed;       675 AA.
AC   A0A3Q1JVY3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Cryptochrome-1-like {ECO:0000313|Ensembl:ENSATEP00000035998.1};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000035998.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000035998.1}
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   AlphaFoldDB; A0A3Q1JVY3; -.
DR   STRING; 64144.ENSATEP00000035998; -.
DR   Ensembl; ENSATET00000036512.2; ENSATEP00000035998.1; ENSATEG00000024740.2.
DR   GeneTree; ENSGT00940000165925; -.
DR   InParanoid; A0A3Q1JVY3; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000265040; 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:SF10; CRYPTOCHROME 2B-RELATED; 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:UP000265040}.
FT   DOMAIN          3..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          510..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..631
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   675 AA;  76334 MW;  2809A9D130571EA9 CRC64;
     MAPNSIHWFR KGLRLHDNPA LQEAVQGAGT VRCVYFLDPW FAGSSNVGVN RWRFLLQCLE
     DLDASLRKLN SRLFVIRGQP ANVFPRLFKE WKISRLTFEY DSEPFGKERD AAIKKLAMEA
     GVEVIVKISH TLYNLDKIIE LNGGQPPLTY KRFQTLISRL DPPEMPVETL SDTLMGRCVT
     PISEDHGDKY GVPSLEELGF DTEGLPSAVW PGGETEALTR IERHLERKAW VANFERPRMN
     ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYRKVKKNS SPPLSLYGQL LWREFFYTAA
     TNNPRFDKME GNPICVRIPW DKNPEALAKW AEAKTGFPWI DAIMTQLRQE GWIHHLARHA
     VACFLTRGDL WISWEEGMKV FEELLLDADW SVNAGSWMWL SCSSFFQQFF HCYCPVGFGR
     RTDPNGDFIR RYLPVLRGFP AKFIYDPWNA PESVQAAAKC IIGVHYPKPM VHHAEASRLN
     IERMKQIYQQ LSRYRGLGLL ASVPSTNGNG NGGMMAYSPG DQQAGTTTNS HLPGMSGSPV
     TTGNGSGSIL LNFDSEEHTG PSGVGQQQRL QPLPQQQQQQ QHGYHSVPEA SQTITSSRLY
     HEFAVPQQPG LLHSRGNVTG KRERESECEG SGEEDPVSCS VHKMQRQSTE IFHRGKVSWC
     NLPHHDTTHD ATQCM
//
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