ID A0A3N0VL49_9GAMM Unreviewed; 486 AA.
AC A0A3N0VL49;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ROH93440.1};
GN ORFNames=ED208_02680 {ECO:0000313|EMBL:ROH93440.1};
OS Stagnimonas aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stagnimonas.
OX NCBI_TaxID=2689987 {ECO:0000313|EMBL:ROH93440.1, ECO:0000313|Proteomes:UP000282106};
RN [1] {ECO:0000313|EMBL:ROH93440.1, ECO:0000313|Proteomes:UP000282106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=THS-13 {ECO:0000313|EMBL:ROH93440.1,
RC ECO:0000313|Proteomes:UP000282106};
RA Chen W.-M.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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:ROH93440.1}.
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DR EMBL; RJVO01000001; ROH93440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0VL49; -.
DR InParanoid; A0A3N0VL49; -.
DR Proteomes; UP000282106; 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:ROH93440.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282106}.
FT DOMAIN 5..134
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 240..244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 313
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 369
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 392
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 486 AA; 54585 MW; E19ACAE77C2B8C1B CRC64;
MHSTDTAIVW LRRDLRLADQ PALHAAAQRH ARVLPLYLHA PEEESPWLPG AASRWWLHHS
LSALAESLAA LGSPLLIRRG PSTEALRQLA RETGAGAVYW TRLYEPTGIA RDRMVKEALR
ADGLLAESFN AALLFEPWEL KTGGGEPYRV FSPFWRNAEA RLDHLPAPLP APARLSPPER
SVAGLSIAEL NLLPRIPWDE GFYPHWTPGE AGARQRLEQF AASAIGRYKE QRDQPAVPAT
SGLSPHLHFG ELSPRSALLA AREAARTASP GWLASAEHFV RELGWREFSH HLLFHYPATD
RLPMYDKFAA FPWRQPDDYA SDLAAWQQGR TGIPIVDAGM RQLWQSGWVH NRVRMIVASL
LTKNLLIPWQ EGAQWFWDTL VDASLPQNSL GWQWSAGCGA DAAPYFRIFN PVLQGEKFDP
EGSYTRRWLP ELARLPAKYL HRPWEAPSEI RRAAGLGLDS VYARPIVDLA RSRDRALAAY
EQIKAG
//
