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Database: UniProt
Entry: A0A238L090_9RHOB
LinkDB: A0A238L090_9RHOB
Original site: A0A238L090_9RHOB 
ID   A0A238L090_9RHOB        Unreviewed;       473 AA.
AC   A0A238L090;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:SMX48504.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:SMX48504.1};
GN   Name=phr {ECO:0000313|EMBL:SMX48504.1};
GN   ORFNames=MAA8898_03966 {ECO:0000313|EMBL:SMX48504.1};
OS   Maliponia aquimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Maliponia.
OX   NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX48504.1, ECO:0000313|Proteomes:UP000207598};
RN   [1] {ECO:0000313|EMBL:SMX48504.1, ECO:0000313|Proteomes:UP000207598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX48504.1,
RC   ECO:0000313|Proteomes:UP000207598};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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}.
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DR   EMBL; FXYF01000013; SMX48504.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238L090; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000207598; Unassembled WGS sequence.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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:SMX48504.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000207598}.
FT   DOMAIN          5..131
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         236..240
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         373..375
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            305
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"
FT   SITE            383
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   473 AA;  53636 MW;  8DE3327F7D8A98E1 CRC64;
     MSDRSPILVW FRRDLRLSDH AALSAAAESG RPVIPVCLRD GLVDGLGAAP KWRWGLGVGH
     LAGRLEGMGS RLVLRSGEAV EVLTALAQET GAGAVHWMRA YDPDSVARDT DVKAALKEAG
     IEARSFAGHV MFEPWTVETG QGGYYKVYTP YWKSVRGRDV ATPLAAPSRL PAPDTWPKSE
     ALDDWHLGRA MQRGAAVVRP WVRLGEEAAQ DRLGHFLEDI VARYDETRDL PWTDGTSCLS
     ENLAVGEISP AQCWHAGRRA LEDGKQGAET FLKELVWREF AYHLMWHTPR ILDANWREEW
     EAFPWNTDER LKEVRDWKRG RTGMSFVDAG LREMYVTGRM HNRARMITAS YLTKHLLCHW
     KIGQKWFEDC LIDWDPASNA MGWQWSAGSG PDATPYFRVF NPVSQREKFD PKRRYVDRWI
     AEGHRAPSDE ALSYFEAIPK SWGMSPKDPY PEPVVGADTG RKRALEAYRN RGF
//
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