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Database: UniProt
Entry: C3GKY1_BACTU
LinkDB: C3GKY1_BACTU
Original site: C3GKY1_BACTU 
ID   C3GKY1_BACTU            Unreviewed;       476 AA.
AC   C3GKY1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:EEM76858.1};
GN   ORFNames=bthur0010_29140 {ECO:0000313|EMBL:EEM76858.1};
OS   Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM76858.1};
RN   [1] {ECO:0000313|EMBL:EEM76858.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM76858.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
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:EEM76858.1}.
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DR   EMBL; ACNH01000059; EEM76858.1; -; Genomic_DNA.
DR   RefSeq; WP_001179957.1; NZ_CM000755.1.
DR   AlphaFoldDB; C3GKY1; -.
DR   HOGENOM; CLU_010348_2_2_9; -.
DR   Proteomes; UP000006660; Chromosome.
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:EEM76858.1}.
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;  55643 MW;  DB2293B78E47D347 CRC64;
     MQNKIIVMFQ KDFRLYDNPA LFEAAQSGEV VPVYVHDETF SMGSASKWWL HHAIIDVKKQ
     LEALGSTLII RKGSTQEKIL SLVEQLGITA VYWNICYDPD RLQSNQKMKM MLEDKGMICK
     EFNSHLLLEP WIIKKKDNTE YKVFTPFYNA FQKQVIHKPI SKVQSIKGGN SLPVSLSVSE
     LHLLPTIPWT SHMESIWEPT EEGAYKTWKE FFSSKLASYS EGRDFPNQNA HSMLAPYLSF
     GQISVKLIYH YLINKSTESQ CSLFEKQVNS FIRQLIWREF SYYLLYHYPF TAYKPLNKSF
     EHFPWNNEEE LLRVWQKGDT GYPFIDAGMR ELWQTGFMHN RTRMAVASFL VKHLLIPWQE
     GAKWFMDTLL DADIANNTMG WQWVAGSGAD ASPYFRIFNP ITQGEKFDKN GEYIREWVPE
     LKDMPNKYIH KPWEAPEHIL QKANIQLGHT YPLPVVDHKA ARERALCAYK SMKEFV
//
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