ID   PHR_POTTR               Reviewed;         532 AA.
AC   Q28811;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE            EC=4.1.99.3;
DE   AltName: Full=DNA photolyase;
DE   AltName: Full=Photoreactivating enzyme;
GN   Name=PHR;
OS   Potorous tridactylus (Potoroo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Potoroidae; Potorous.
OX   NCBI_TaxID=9310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7813451; DOI=10.1002/j.1460-2075.1994.tb06961.x;
RA   Yasui A., Eker A.P., Yasuhira S., Yajima H., Kobayashi T., Takao M.,
RA   Oikawa A.;
RT   "A new class of DNA photolyases present in various organisms including
RT   aplacental mammals.";
RL   EMBO J. 13:6143-6151(1994).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC       Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl
CC       pyrimidine dimers (in cis-syn configuration), which are formed between
CC       adjacent bases on the same DNA strand upon exposure to ultraviolet
CC       radiation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC         DNA).; EC=4.1.99.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
CC       {ECO:0000305}.
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DR   EMBL; D26020; BAA05041.1; -; mRNA.
DR   PIR; S52046; S52046.
DR   AlphaFoldDB; Q28811; -.
DR   SMR; Q28811; -.
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; 3.40.50.620; -; 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   Pfam; PF00875; DNA_photolyase; 1.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   TIGRFAMs; TIGR00591; phr2; 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   2: Evidence at transcript level;
KW   Chromophore; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase.
FT   CHAIN           1..532
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000085120"
FT   DOMAIN          97..229
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..376
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          442..443
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         322
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         468..470
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   532 AA;  61631 MW;  0865B1BFDE7BB25B CRC64;
     MDSKKRSHST GGEAENMESQ ESKAKRKPLQ KHQFSKSNVV QKEEKDKTEG EEKGAEGLQE
     VVRQSRLRTA PSVLEFRFNK QRVRLISQDC HLQDQSQAFV YWMSRDQRVQ DNWAFLYAQR
     LALKQKLPLH VCFCLAPCFL GATIRHYDFM LRGLEEVAEE CEKLCIPFHL LLGLPKDVLP
     AFVQTHGIGG IVTDFSPLLH HTQWVKDVQD ALPRQVPFVQ VDAHNIVPCW VASDKQEYGA
     RTIRHKIHDR LPHFLTEFPP VICHPYTSNV QAEPVDWNGC RAGLQVDRSV KEVSWAKPGT
     ASGLTMLQSF IAERLPYFGS DRNNPNKDAL SNLSPWFHFG QVSVQRAILE VQKHRSRYPD
     SVTNFVEEAV VRRELADNFC FYNKNYDKLE GAYDWAQTTL RLHAKDKRPH LYSLEQLESG
     KTHDPLWNAA QMQTVKEGKM HGFLRMYWAK KILEWTRSPE EALEFAIYLN DRFQLDGWDP
     NGYVGCMWSI CGIHDQGWAE REIFGKIRYM NYAGCKRKFD VAEFERKISP AD