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Database: UniProt
Entry: A0A0N1ARP8_9PROT
LinkDB: A0A0N1ARP8_9PROT
Original site: A0A0N1ARP8_9PROT 
ID   A0A0N1ARP8_9PROT        Unreviewed;       509 AA.
AC   A0A0N1ARP8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KPF57373.1};
GN   ORFNames=D621_08150 {ECO:0000313|EMBL:KPF57373.1};
OS   beta proteobacterium AAP51.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523421 {ECO:0000313|EMBL:KPF57373.1, ECO:0000313|Proteomes:UP000037990};
RN   [1] {ECO:0000313|EMBL:KPF57373.1, ECO:0000313|Proteomes:UP000037990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP51 {ECO:0000313|EMBL:KPF57373.1,
RC   ECO:0000313|Proteomes:UP000037990};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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 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:KPF57373.1}.
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DR   EMBL; LJHT01000027; KPF57373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1ARP8; -.
DR   PATRIC; fig|1523421.3.peg.1756; -.
DR   Proteomes; UP000037990; 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; 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:KPF57373.1}.
FT   DOMAIN          14..150
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         302..309
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         402..404
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            333
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            389
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            412
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   509 AA;  57057 MW;  1B1662AC372666A8 CRC64;
     MKKTQHPHPA PKIDRALVWL RRDLRVDDHA ALHHALKAAR QVWCVFVFDR DILDPLPRQD
     RRVEFIRDSL VGVDAELRAL AASHGVEGAG LIVMHGWPVQ AIPALAARLQ VQAVYASHDD
     EPAAETRDAQ VRGRLADAGV MLHTMKDHVV FERSEVLTLS GGAFSVFTPY KNAWLKKCEP
     YFLSAWPVAK HAGALAPRPA GEPGVPALED IGFARTNLHQ LRLPSGPAGA QELLADFLER
     MDRYGETRDF PAIKGPSYLS THLRFGTVSV RQLARLAMER RNASPPAPPD GPRSGAEVWL
     SELIWRDFYH QVLHHHPRVV TGAFKPEYDR IRWEHGKHAD ELFAAWCEGR TGYPLVDAAM
     HQLAQTGYMH NRLRMVVASF LAKDLGLDWR RGEAWFALHL NDFDLAANNG GWQWAASSGC
     DAQPYFRIFN PVSQSEKFDP QGRFIRRYLP QLAALPDKLI HAPWQARPVD LLAANIELGK
     HYPRPVVDHA EAREKTLARY AVVKAGAAG
//
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