(data stored in SCRATCH zone)

SWISSPROT: D6XVT1_BACIE

ID   D6XVT1_BACIE            Unreviewed;       512 AA.
AC   D6XVT1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 54.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ADH97704.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:ADH97704.1};
GN   OrderedLocusNames=Bsel_0155 {ECO:0000313|EMBL:ADH97704.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97704.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97704.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DNA photolyase family.
CC       {ECO:0000256|RuleBase:RU004182}.
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DR   EMBL; CP001791; ADH97704.1; -; Genomic_DNA.
DR   RefSeq; WP_013171133.1; NC_014219.1.
DR   STRING; 439292.Bsel_0155; -.
DR   EnsemblBacteria; ADH97704; ADH97704; Bsel_0155.
DR   KEGG; bse:Bsel_0155; -.
DR   eggNOG; ENOG4105CVP; Bacteria.
DR   eggNOG; COG0415; LUCA.
DR   HOGENOM; HOG000245621; -.
DR   KO; K01669; -.
DR   OrthoDB; 184000at2; -.
DR   BioCyc; BSEL439292:G1GLR-180-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 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   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XVT1.
DR   SWISS-2DPAGE; D6XVT1.
KW   Chromophore {ECO:0000256|RuleBase:RU004182};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   FAD {ECO:0000256|RuleBase:RU004182};
KW   Flavoprotein {ECO:0000256|RuleBase:RU004182};
KW   Lyase {ECO:0000313|EMBL:ADH97704.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        1    130       Photolyase/cryptochrome alpha/beta.
FT                                {ECO:0000259|PROSITE:PS51645}.
SQ   SEQUENCE   512 AA;  58012 MW;  445E30905168BDF6 CRC64;
     MVNVVWLKRD LRIFDHRPLK EAAEQGEVLP LFVWEASVWA HGDLSVRHRD FVLQSLAELD
     RRLDQRGARL YTAVGEVIDV LTRLEADLGP FQLFAHEENG TPLTFERDIA VRNWMKARGC
     TMKEWPHFGV TRGLKSRDDF QKGYERYVNA PVVPAPEAVR GIRHAPAWLT KGAGEPGGIA
     LPGTAITRGQ QGGERLAHGV LKGFLEERFK AYQVRISKPF ASAESCSRLS PYLAWGNLSV
     RYTYQETVAR LGELGSGFHK KQLSAFLSRL HWHCHFIQRL EDEPEIAHRT MNPVFDTVRQ
     TWSEEAYQRW LHGRTGIPLI DAAMRCLHET GWLNFRSRAM VISFVCNTLM LDWRRPAEDL
     SRLFLDYEPG IHYSQVQMQA GTTGFNTIRI YNPVKQGQEH DPSGAFVRRF VPELSAVSDA
     FIHEPWKLPA GPPKGYPMPM VDVAKANGEA RRILWGLKAS KEAKAAAGEQ LNKHGSRAHR
     KKGKKKPGAG VEQLDLFELA DPHDHKEKEK GG
//

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