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Database: UniProt
Entry: V6SJ26_9FLAO
LinkDB: V6SJ26_9FLAO
Original site: V6SJ26_9FLAO 
ID   V6SJ26_9FLAO            Unreviewed;       428 AA.
AC   V6SJ26;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Deoxyribodipyrimidine photolyase-class I {ECO:0000313|EMBL:ESU26663.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:ESU26663.1};
GN   ORFNames=FLJC2902T_26380 {ECO:0000313|EMBL:ESU26663.1};
OS   Flavobacterium limnosediminis JC2902.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1341181 {ECO:0000313|EMBL:ESU26663.1, ECO:0000313|Proteomes:UP000018004};
RN   [1] {ECO:0000313|EMBL:ESU26663.1, ECO:0000313|Proteomes:UP000018004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC2902 {ECO:0000313|EMBL:ESU26663.1,
RC   ECO:0000313|Proteomes:UP000018004};
RA   Lee K., Yi H., Park S., Chun J.;
RT   "Flavobacterium limnosediminis JC2902 genome sequencing.";
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:ESU26663.1}.
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DR   EMBL; AVGG01000018; ESU26663.1; -; Genomic_DNA.
DR   RefSeq; WP_023580196.1; NZ_AVGG01000018.1.
DR   AlphaFoldDB; V6SJ26; -.
DR   STRING; 1341181.FLJC2902T_26380; -.
DR   PATRIC; fig|1341181.4.peg.2597; -.
DR   eggNOG; COG0415; Bacteria.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000018004; Unassembled WGS sequence.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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; 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:ESU26663.1}.
FT   DOMAIN          1..129
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         250
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         253..260
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            284
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            337
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            360
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   428 AA;  50648 MW;  D8F5E3994916FE09 CRC64;
     MTIFWFRRDL RLDDNTALFH ALNSNEKVLP IFIFDENILS QLPKDDARIT FIHKQLEKIQ
     KQLKVIGKSL AIFHGTPEDV FKKLISENKI TTVFTNHDYE PYARKRDKAM NELFKEHAVE
     FKTCKDQVLF EKSEVVKDNG SPYVVYTPYS KKWKENFRKM KLVHYPSETL LEKITAHSYP
     FLSLKDIGFE KSPIEPKPFD ISKQLIANYE ETRNFPAISG TSLLGVYLRF GTISIRKLIS
     LAKESRNETF LNELIWREFF MQILWHFPHT VNRSFREKYY AIQWSNDETL FQKWCEGKTG
     YPFVDAGMRE LNATGHMHNR VRMIVASFLC KHLLIDWRWG ETYFAQKLLD YEQSSNVGNW
     QWAAGSGVDA APYFRIFNPT EQIKKFDKDL KYIKKWIPEL ETSKYPKPIV DHKEAREKCL
     RIYKEAVG
//
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