GenomeNet

Database: UniProt
Entry: A0A0C1DRQ5_9SPHI
LinkDB: A0A0C1DRQ5_9SPHI
Original site: A0A0C1DRQ5_9SPHI 
ID   A0A0C1DRQ5_9SPHI        Unreviewed;       434 AA.
AC   A0A0C1DRQ5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KIA96725.1};
GN   ORFNames=OC25_03140 {ECO:0000313|EMBL:KIA96725.1};
OS   Pedobacter kyungheensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA96725.1, ECO:0000313|Proteomes:UP000031246};
RN   [1] {ECO:0000313|EMBL:KIA96725.1, ECO:0000313|Proteomes:UP000031246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA96725.1,
RC   ECO:0000313|Proteomes:UP000031246};
RA   Anderson B.M., Newman J.D.;
RT   "Pedobacter Kyungheensis.";
RL   Submitted (OCT-2014) 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}.
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:KIA96725.1}.
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; JSYN01000002; KIA96725.1; -; Genomic_DNA.
DR   RefSeq; WP_039471547.1; NZ_JSYN01000002.1.
DR   AlphaFoldDB; A0A0C1DRQ5; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000031246; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
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; IPR018394; DNA_photolyase_1_CS_C.
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; 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;
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991, 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:KIA96725.1}.
FT   DOMAIN          4..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         213
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         254
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         257..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            288
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            341
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            364
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   434 AA;  51023 MW;  6FE894F23E8F9D2B CRC64;
     MKKAISIFWF RRDLRLTDNA GFYHALKSGH PVLSLFIFDK NILDKLPEDD ARVTFNYQTI
     EDLKKDLQAH GSDLLVKYGK PEKIWSEILG DYEVAAVYTN HDYEPYARER DDNMAEFLTS
     EKIAFKTYKD QVIFEKNEIL KADQTPYTVF TPFYKQWHAK LNSFYTKAYP TQKYYKNLLP
     AKNLPLPSLK EMGFEKSKLN FPKLSYKSKL DSYAKERDFP ALDSTTHIGL HLRFGTLSIR
     KAVRDAIEAK SNIWLSELAW REFYMSILWH FPYSAADSFK KQYDKIKWRN NEDEFKAWCE
     GNTGYPIVDA GMRQLNQTGW MHNRVRMVVA SFLTKHLLID WRWGETYFAE KLLDYEMASN
     VGGWQWAAGS GNDAAPYFRV FNPELQTKKF DPKLEYIKKW VPEFGTKKYA QPIVEHTFAR
     ERVLKVFKAA LANS
//
DBGET integrated database retrieval system