ID   PHR_HALSA               Reviewed;         481 AA.
AC   Q9HQ46; P20377;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 102.
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; Synonyms=phr2; OrderedLocusNames=VNG_1335G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2681164; DOI=10.1128/jb.171.11.6323-6329.1989;
RA   Takao M., Kobayashi T., Oikawa A., Yasui A.;
RT   "Tandem arrangement of photolyase and superoxide dismutase genes in
RT   Halobacterium halobium.";
RL   J. Bacteriol. 171:6323-6329(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=coenzyme F420-(gamma-Glu)n; Xref=ChEBI:CHEBI:133980;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 coenzyme F420 non-covalently per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG19671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M24544; AAA72749.1; -; Genomic_DNA.
DR   EMBL; AE004437; AAG19671.1; ALT_INIT; Genomic_DNA.
DR   PIR; B32580; B32580.
DR   PIR; C84288; C84288.
DR   RefSeq; WP_012289312.1; NC_002607.1.
DR   AlphaFoldDB; Q9HQ46; -.
DR   SMR; Q9HQ46; -.
DR   STRING; 64091.VNG_1335G; -.
DR   PaxDb; Q9HQ46; -.
DR   EnsemblBacteria; AAG19671; AAG19671; VNG_1335G.
DR   GeneID; 5954311; -.
DR   KEGG; hal:VNG_1335G; -.
DR   PATRIC; fig|64091.14.peg.1019; -.
DR   HOGENOM; CLU_010348_2_2_2; -.
DR   InParanoid; Q9HQ46; -.
DR   OrthoDB; 21461at2157; -.
DR   PhylomeDB; Q9HQ46; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
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; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR   InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR   InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000085109"
FT   DOMAIN          1..136
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          283..290
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          349..350
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         240..244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         380..382
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         412
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   SITE            314
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            367
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            390
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  54097 MW;  E25C7B470E05A9F7 CRC64;
     MQLFWHRRDL RTTDNRGLAA AAPGVTAVDG GHDQGPVAAV FCFDDEVLAH AAPPRVAFML
     DALAALRERY RDLGSDLIVR HGDPAAVLPA VANDLDATRV VWNHDYSGLA TDRDAGVRDA
     LDAAGVAHAQ FHDAVHHRPG EIRTNAGDPY SVYTYFWRKW QDREKNPPAP EPEPADLAAD
     TALADTSPLP SVQELGFAEP EAAVPDAGTA AARSLLDAFR ESGDIYRYED RRDYPHEEPT
     SRLSPHLKFG TIGIRTVYEA ARAAKSDADT DDERENVAAF IGQLAWREFY AQVLYFNQNV
     VSENFKAYEH PIEWRDDPAA LQAWKDGETG YPIVDAGMRQ LRAEAYMHNR VRMIVAAFLT
     KDLLVDWRAG YDWFREKLAD HDTANDNGGW QWAASTGTDA QPYFRVFNPM TQGERYDPDA
     DYITEFVPEL RDVPADAIHS WHELSLSERR RHAPEYPDPI VDHSQRREDA IAMFERARGD
     E