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Database: UniProt
Entry: A0A0A0JI95_9MICO
LinkDB: A0A0A0JI95_9MICO
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ID   A0A0A0JI95_9MICO        Unreviewed;       459 AA.
AC   A0A0A0JI95;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:KGN37100.1};
GN   ORFNames=N803_14650 {ECO:0000313|EMBL:KGN37100.1};
OS   Knoellia subterranea KCTC 19937.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN37100.1, ECO:0000313|Proteomes:UP000030011};
RN   [1] {ECO:0000313|EMBL:KGN37100.1, ECO:0000313|Proteomes:UP000030011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN37100.1,
RC   ECO:0000313|Proteomes:UP000030011};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia subterranea.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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 family.
CC       {ECO:0000256|RuleBase:RU004182}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGN37100.1}.
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DR   EMBL; AVPK01000006; KGN37100.1; -; Genomic_DNA.
DR   RefSeq; WP_035905256.1; NZ_AVPK01000006.1.
DR   AlphaFoldDB; A0A0A0JI95; -.
DR   STRING; 1385521.N803_14650; -.
DR   eggNOG; COG0415; Bacteria.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000030011; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
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; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|RuleBase:RU004182};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW   1}; Lyase {ECO:0000313|EMBL:KGN37100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030011}.
FT   DOMAIN          1..126
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         215
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         227..231
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         259
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         262..269
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         359..361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   459 AA;  51044 MW;  058B03CAA5FA8223 CRC64;
     MTSILWLRRD LRRADHPALL AARDAADGDL VVAYVLDPAL WSSAGPVRRA WLAATLEATA
     RDYGDALTLL WGNSRIVVPE LAKRLGATSV HVTRETTPFG RRRDEDIANS LAAQGVSWLE
     TGTPYAVGPG LVVNGTGTPY KVFTPFARAW REHGWPDPAP RPRDLPLRHA RNDADATRAL
     RDALTQPDLP TLPDAGEEAA HARWREFLET GVTAYATDRD LPGRDGTSRL SPHLKLGTIH
     PRTLLADLAS RRGTGKETFV DELAWREFYA DVLWHNPSSA WTDLRDALAG MEYDEPADAI
     EAWRAGTTGY PIVDAGMRQL LATGWMHNRV RMITASFLTK DLHVWWPVGA RHFLDHLVDG
     DIASNSHGWQ WVAGTGTDAS PYFRVFNPVT QGEKFDPDGD YVREWVPELA HLAGKAAHQP
     WEHADGYARG YPARIVDHAE ERREALRRLD AVKRGTAAR
//
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