GenomeNet

Database: UniProt
Entry: A0A257FIY2_9BURK
LinkDB: A0A257FIY2_9BURK
Original site: A0A257FIY2_9BURK 
ID   A0A257FIY2_9BURK        Unreviewed;       499 AA.
AC   A0A257FIY2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:OYU26093.1};
GN   ORFNames=CFE41_17885 {ECO:0000313|EMBL:OYU26093.1};
OS   Burkholderiales bacterium PBB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015564 {ECO:0000313|EMBL:OYU26093.1, ECO:0000313|Proteomes:UP000215624};
RN   [1] {ECO:0000313|EMBL:OYU26093.1, ECO:0000313|Proteomes:UP000215624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB2 {ECO:0000313|EMBL:OYU26093.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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:OYU26093.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NKIM01000032; OYU26093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257FIY2; -.
DR   Proteomes; UP000215624; 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; 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}; Lyase {ECO:0000313|EMBL:OYU26093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215624}.
FT   DOMAIN          19..150
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         242
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         289
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         292..299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         392..394
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            323
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            379
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            402
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   499 AA;  56075 MW;  BEA31A88AD23D8CC CRC64;
     MTRPINASDP SPAPSSRVPR ALVWFRRDLR VDDQAALYRA LRAAQQVFCV FVLDRDILDA
     LPRSDRRVDF ILRSLVELDA GLRALCPGGG LIVRHGRAAE DIPRLAAELE VQAVFCNHDD
     EPAALARDAQ VAEALASFAC QLRSFKDHVV FERNEVLTGA GKPYGVFTPY KNAWLRQINE
     FYLSSYPVAR HAAGLAPTAL ARGVPSLAEI GFEPTDLSPH LGAGASGAEA LFEEFLDRMD
     QYEASRNFPA VKGPSYLSLH LRFGTISIRR LAREAWQRAQ GGDRGAEVWL SELIWRDFYH
     QVMHHHPHAM VRAFRPEYDA ITWDSGPAAD HLFKAWCEGR TGYPLVDAAM LQLNQSGYMH
     NRLRMVTACF LIKDLGIDWR RGEAYFAEKL LDFDLAANNG GWQWASSSGC DAQPYFRIFN
     PVTQSEKFDP EGKFIKRYLP QLAKLPPKLI HAPWLAKPLE LEACRLVLGR DYPTPVVRHD
     EARAATLARY AVVKSRAIE
//
DBGET integrated database retrieval system