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Database: UniProt
Entry: A0A3P8PHY6_ASTCA
LinkDB: A0A3P8PHY6_ASTCA
Original site: A0A3P8PHY6_ASTCA 
ID   A0A3P8PHY6_ASTCA        Unreviewed;       557 AA.
AC   A0A3P8PHY6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000256|ARBA:ARBA00014046};
DE            EC=4.1.99.3 {ECO:0000256|ARBA:ARBA00013149};
DE   AltName: Full=DNA photolyase {ECO:0000256|ARBA:ARBA00031671};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000016671.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000016671.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000016671.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC         DNA).; EC=4.1.99.3; Evidence={ECO:0000256|ARBA:ARBA00033999};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
CC       {ECO:0000256|ARBA:ARBA00006409}.
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DR   AlphaFoldDB; A0A3P8PHY6; -.
DR   STRING; 8154.ENSACLP00000016671; -.
DR   Ensembl; ENSACLT00000017075.1; ENSACLP00000016671.1; ENSACLG00000011360.1.
DR   GeneTree; ENSGT00390000010302; -.
DR   OMA; IHNYLRM; -.
DR   OrthoDB; 1341644at2759; -.
DR   Proteomes; UP000265100; Chromosome 18.
DR   Bgee; ENSACLG00000011360; Expressed in anal fin and 7 other cell types or tissues.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd00293; USP_Like; 1.
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; IPR008148; DNA_photolyase_2.
DR   InterPro; IPR032673; DNA_photolyase_2_CS.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00591; phr2; 1.
DR   PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR   PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS01083; DNA_PHOTOLYASES_2_1; 1.
DR   PROSITE; PS01084; DNA_PHOTOLYASES_2_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          120..253
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          50..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  64222 MW;  2677A7E07B10A35A CRC64;
     MLHCVWRSTS PFCAPGRFLK LLPHHHQRPS SPALFFLTSF FSCQPTMSGT KRKASSATAG
     KDHRAKQQKL APVKQEKKEK VGGWLQSLVQ LQRSEKKDVK FNKKRLRFLS DTEKIKQGSE
     GVLYWMLRDQ RVQDNWALIH AQRLAVKENL PLHVCFCLVV PKSELSTLRH YSFMLKGLEE
     VAKECEQLNV QFHLLHGAPE KVLPGFVSDH SFGAVVTDFS PIREPLQWLE DVKKKLSKDI
     PFIQVDAHNI VPCWVASPKQ EYSARTIRGK ITNLLPEFLT DFPLVDAHPH TATRTAKGVD
     WDKTLASLDV DRNVKEPEWA KPGTKAGMDM LESFIDVRLK LFGSQRNDPN APALSQLSPW
     LRFGQISAQR VAWQVQRNGK NASQSVPAFI EELVVRRELT DNFCFYNKKY DSVEGAYEWA
     QKTLKDHAKD ERPYLYTREQ LEEAKTHDKL WNAAQYQMVT EGKMHGFLRM YWAKKILEWT
     SSPEEALSIA LYLNDRYELD GQDPNGFVGC MWSICGIHDQ GWAERAVFGK IRYMNYKGCL
     RKFNVAQFER KYCPKSL
//
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