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Database: UniProt
Entry: R4FZX0_9BACI
LinkDB: R4FZX0_9BACI
Original site: R4FZX0_9BACI 
ID   R4FZX0_9BACI            Unreviewed;       468 AA.
AC   R4FZX0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:GAC90493.1};
GN   ORFNames=KN10_0929 {ECO:0000313|EMBL:GAC90493.1};
OS   Anoxybacillus flavithermus NBRC 109594.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=1315967 {ECO:0000313|EMBL:GAC90493.1, ECO:0000313|Proteomes:UP000013057};
RN   [1] {ECO:0000313|Proteomes:UP000013057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 109594 {ECO:0000313|Proteomes:UP000013057};
RA   Matsutani M., Shirakihara Y., Imada K., Yakushi T., Matsushita K.;
RT   "Draft Genome Sequence of a Thermophilic Member of the Bacillaceae,
RT   Anoxybacillus flavithermus Strain Kn10, Isolated from the Kan-nawa Hot
RT   Spring in Japan.";
RL   Genome Announc.1:e00311-13(2013).
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:GAC90493.1}.
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DR   EMBL; BARH01000006; GAC90493.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4FZX0; -.
DR   Proteomes; UP000013057; 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:SF9; (6-4)-PHOTOLYASE, ISOFORM A; 1.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 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:GAC90493.1}.
FT   DOMAIN          5..136
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         276
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         279..286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         376..378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            310
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            363
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            386
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   468 AA;  56001 MW;  6ECA6596A805BF53 CRC64;
     MGYMHTAVVW FRRDFRLHDH TALIHALQWA KEREGKLLFF FHFDSHFAKE RTYHHEYFFQ
     TVEQFRQMLR HLYGIHVHIL HGDIDDVFVR LISRTHMNAI FFNKDEVGRG KERDDYVRTF
     LQKYGVDVYA YDDAHLHGAF EVLKADGTPY KVYTPYYRAW RKRPKRFPSS VDMALLREHM
     LHMTPISEDD ERAFTMWLAQ CTKHWERTSE QDALHVLQQF IDKALPYYHR KRDIPSVTGT
     SRLSPHIKTG TISIRTVFHA VAQQFGNGYD EAVETYIKEL AWRDFYHMIY AHFPFTKTEA
     FIEKYRHLPW SRDDEQFEAW KEGKTGFPFV DAGMRQLKKE GWMHNRLRMV VASFLAKDYL
     IDWRMGEQYF QHMLIDYDEA SNIGGWQWAA SVGTDAVPYF RVFNPIEQSK KFDPDGTYIR
     TYVQELASFP SLYIHEPWKS NIKIDYPAPT VDHQLQRQRA IALFQMNE
//
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