ID A0A0Q9KLA0_9MICO Unreviewed; 463 AA.
AC A0A0Q9KLA0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KRE38611.1};
GN ORFNames=ASG73_04820 {ECO:0000313|EMBL:KRE38611.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE38611.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE38611.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE38611.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE38611.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE38611.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE38611.1}.
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DR EMBL; LMRZ01000003; KRE38611.1; -; Genomic_DNA.
DR RefSeq; WP_055992688.1; NZ_LMRZ01000003.1.
DR AlphaFoldDB; A0A0Q9KLA0; -.
DR STRING; 1736393.ASG73_04820; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000051572; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {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:KRE38611.1}.
FT DOMAIN 1..123
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 228..232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 266..273
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 366..368
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 463 AA; 51312 MW; 880F77E366D5CA98 CRC64;
MTALLWFRRD LRLSDHPALL AAADEGEVLP FVVVEPQVLS DHRPSARRML RSIAALHEAT
GGALVVRCGD PVDLVPQAAA AVGAERVHIT RDTTPAGRVR DEDVGGRLQE QGAQLVTTGT
PCAVGPGLVL TGEGTPYKVF TPFARAWRDH GWPAPADRVG DDVWLRDGAD LLAEVGEDGL
ERVLAAADED AIDGPAGEDA AQERWRSFLR DDLAGYDTDR DRPDRDATSR MSIHLTHGEI
HTRTMLADLA AHPAADSDAA QRFVTELAWR EFYADVLWHR PDSAWADLRD ALAGLPYDDG
SETDRLVEAW RQGRTGYPFV DAGMRQLLAE GFMHNRVRMV VASFLTKDLH VWWPVGARHF
LDHLLDGDLA SNSHGWQWVA GTGTDASPYF RVFNPITQGE RFDPDGAYVR RWVPELAHLS
GKAAHTPWTH PDGAAHGYPE RVLDHAEERR EALDRYEMAR AQR
//
