(data stored in SCRATCH zone)

SWISSPROT: B7UKY1_ECO27

ID   B7UKY1_ECO27            Unreviewed;       472 AA.
AC   B7UKY1;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   SubName: Full=Deoxyribodipyrimidine photolyase, FAD-binding {ECO:0000313|EMBL:CAS08139.1};
GN   Name=phr {ECO:0000313|EMBL:CAS08139.1};
GN   OrderedLocusNames=E2348C_0591 {ECO:0000313|EMBL:CAS08139.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08139.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08139.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- SIMILARITY: Belongs to the DNA photolyase family.
CC       {ECO:0000256|RuleBase:RU004182}.
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DR   EMBL; FM180568; CAS08139.1; -; Genomic_DNA.
DR   RefSeq; WP_000207175.1; NC_011601.1.
DR   EnsemblBacteria; CAS08139; CAS08139; E2348C_0591.
DR   KEGG; ecg:E2348C_0591; -.
DR   HOGENOM; HOG000245621; -.
DR   KO; K01669; -.
DR   OMA; NTQGWEP; -.
DR   BioCyc; ECOL574521:E2348C_RS03135-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKY1.
DR   SWISS-2DPAGE; B7UKY1.
KW   Chromophore {ECO:0000256|RuleBase:RU004182};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   FAD {ECO:0000256|RuleBase:RU004182};
KW   Flavoprotein {ECO:0000256|RuleBase:RU004182};
KW   Lyase {ECO:0000313|EMBL:CAS08139.1}.
FT   DOMAIN        2    134       Photolyase/cryptochrome alpha/beta.
FT                                {ECO:0000259|PROSITE:PS51645}.
SQ   SEQUENCE   472 AA;  53761 MW;  FF8D0F19FC087EB7 CRC64;
     MTTHLVWFRQ DLRQHDNLAL AAACRNSSAR VLALYIATPR QWAVHNVSPR QAELINTQLN
     ALQNALAEKG IPLLFREVDD FAASVEIVKQ VCAENRVTHL FYNYQYEVNE RARDVQAERA
     LRNVVCEGFD DGVILPPGAV MTGNHEMYKV FTPFKNAWLK RLREGMPECV AAPKVRSSGS
     IDPAPSITLN YPRQPFDTAH FPVEEKAAIA QLRQFCQNGA GEYEQQRDFP AVEGTSRLSA
     SLATGGLSPR QCLHRLLAEQ PQALDGGAGS IWLNELIWRE FYRHLITYYP SLCKHRPFIV
     WTDRVQWQSN SAHLKAWQEG KTGYPIVDAA MRQLNSTGWM HNRLRMITAS FLVKDLLIDW
     REGERYFMSQ LIDGDLAANN GGWQWAASTG TDAAPYFRIF NPTTQGEKFD REGEFIRQWL
     PELRDVPGKV VHEPWKWAQK AGVTLDYPQP IVDHKEARLR TLAAYEEARK GA
//

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