ID B7HWR4_BACC7 Unreviewed; 476 AA.
AC B7HWR4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Deoxyribodipyrimidine photolyase family protein {ECO:0000313|EMBL:ACJ77256.1};
GN OrderedLocusNames=BCAH187_A3193 {ECO:0000313|EMBL:ACJ77256.1};
OS Bacillus cereus (strain AH187).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ77256.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ77256.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ77256.1,
RC ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001177; ACJ77256.1; -; Genomic_DNA.
DR AlphaFoldDB; B7HWR4; -.
DR KEGG; bcr:BCAH187_A3193; -.
DR HOGENOM; CLU_010348_2_2_9; -.
DR Proteomes; UP000002214; Chromosome.
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}.
FT DOMAIN 3..127
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 219
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 371..373
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 358
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 381
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 476 AA; 55821 MW; 3274DCE633E29353 CRC64;
MQNKIIVMFQ KDFRLYDNPA LFEAAQSGEV LPLYVYDETF SIGSASKWWL HHTIIDVKRQ
LEALGSTLII RKGNTMEEIL SLIEQLGITA VYWNICYDPD RLQSNQKMKM MLEDKGITCK
EFNSHLLLEP WIIKKKDNTE YKVFTPFYNA FQKQVISKPI SKVQSIKWGS SLPASLSVSE
LHLLPTIPWT SHMESIWEPT EEGAYKTCKK FFSSKLVSYS EGRDFPNQNA HSMLAPYLSF
GQISVKLMYH YLINKSNEKQ CSLFEQQVNS FIRQFIWREF SYYLLYHYPF TVYKPLNKSF
EYFPWNNEKK LLRVWQKGKT GYPFIDAGMR ELWQTGFMHN RARMAVASFL VKHLLIPWQE
GAKWFMDTLL DADIANNTMG WQWVAGSGAD ASPYFRIFNP ITQGEKFDKD GEYIRKWVPE
LRDMPNKYIH KPWEAPEHIL QKANIKLGDT YPLPVVDHKA ARERALCAYK SMKESI
//
