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Database: UniProt
Entry: A0A1Z5SJX1_9BACT
LinkDB: A0A1Z5SJX1_9BACT
Original site: A0A1Z5SJX1_9BACT 
ID   A0A1Z5SJX1_9BACT        Unreviewed;       438 AA.
AC   A0A1Z5SJX1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:OSZ82550.1};
GN   ORFNames=CAP35_04585 {ECO:0000313|EMBL:OSZ82550.1};
OS   Chitinophagaceae bacterium IBVUCB1.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX   NCBI_TaxID=1985173 {ECO:0000313|EMBL:OSZ82550.1, ECO:0000313|Proteomes:UP000194327};
RN   [1] {ECO:0000313|EMBL:OSZ82550.1, ECO:0000313|Proteomes:UP000194327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVUCB1 {ECO:0000313|EMBL:OSZ82550.1,
RC   ECO:0000313|Proteomes:UP000194327};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-2017) 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:OSZ82550.1}.
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DR   EMBL; NFUW01000001; OSZ82550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5SJX1; -.
DR   STRING; 1985173.CAP35_04585; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000194327; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:OSZ82550.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194327}.
FT   DOMAIN          2..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         213
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         225..229
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         256..263
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         353..355
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            287
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            340
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            363
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   438 AA;  51490 MW;  3FC902E11FA7C47D CRC64;
     MDVSVFWFRR DLRLHDNAGL YHALKSGKPV VPIFIFDTNI LDELEDRFDK RVDFIHRSLA
     NIQKQLVAMG STLHVLYGTP LDCYKKLTGI YNIHAVYTNH DYEPYAKERE QLIADYLLAQ
     NIPLYTYKDQ VLFEKDEVVK DNGEPYTVYT PYSKKVKIKL NDFYLKSYPT EKYFNNFYKQ
     PPVSLPTLSD MSFLETDLDI VSPTLNTNIA KKYHETRDIP GILGTTRLSV HLRFGTVSIR
     QLASEAAPIS EKLLNELIWR DFYQMILWQF PRVVNQAFHI EYDNIKWRNN EEEFEKWCNG
     QTGYPIVDAG MRELNQTGYM HNRVRMVVAS FLTKHLLIDW RWGEAYFAKK LLDFDLASNN
     GGWQWAAGSG CDAAPYFRIF NPYLQTTKFD PDFAYIKKWV PEFQEFSYPK PIVVHEDARD
     RCLKVYKAAL ADKMKIER
//
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