ID A0A091QSN6_9GRUI Unreviewed; 424 AA.
AC A0A091QSN6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Fragment;
GN ORFNames=N332_07071 {ECO:0000313|EMBL:KFQ30198.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ30198.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ30198.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ30198.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK803077; KFQ30198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QSN6; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
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 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, ECO:0000313|EMBL:KFQ30198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369}.
FT DOMAIN 1..119
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ30198.1"
FT NON_TER 424
FT /evidence="ECO:0000313|EMBL:KFQ30198.1"
SQ SEQUENCE 424 AA; 48985 MW; 5BEABCE8CF9A3B47 CRC64;
DNWAFLYAQR LALKQELPLR ICFCLVPKFL DATIRHYGFM LRGLKEVAEE CTELNIPFHL
LLGYAKDVLP QFVVEHSVGG LVTDFCPLRL PRQWVEDIRE RLPEDVPFVQ VDAHNIVPCW
VASPKQEYSA RTIRGKIHAQ LPEFLTEFPP VIRHPYPPSC PAEPIAWEAC YSSLQVDRSV
KEVRWATPGT AAGMAVLQSF IVERLKSFGS HRNDPNKAAL SNLSPWLHFG QVSTQRAILE
VQKHRGKHKE SVDAFVEEAV VRRELAENFC YYNENYDSVQ GAYDWAQTTL KLHAKDKRPY
LYKLQELEQG TTHDPLWNAA QLQMVWEGKM HGFLRMYWAK KILEWTRSPE EALGFAIYLN
DRYELDGMDP NGYVGKDGGC LWSICGIHDQ GWAERAIFGK IRYMNYAGCK RKFDVGQFER
RYAP
//
