ID D2QBC1_SPILD Unreviewed; 438 AA.
AC D2QBC1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ADB36103.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ADB36103.1};
GN OrderedLocusNames=Slin_0029 {ECO:0000313|EMBL:ADB36103.1};
OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896 / Claus 1).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB36103.1, ECO:0000313|Proteomes:UP000002028};
RN [1] {ECO:0000313|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC {ECO:0000313|Proteomes:UP000002028};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA Goker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Spirosoma linguale DSM 74.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB36103.1, ECO:0000313|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC {ECO:0000313|Proteomes:UP000002028};
RX PubMed=21304700;
RA Lail K., Sikorski J., Saunders E., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.D., Chain P., Brettin T., Detter J.C., Schuetze A., Rohde M.,
RA Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.-P., Chen F.;
RT "Complete genome sequence of Spirosoma linguale type strain (1).";
RL Stand. Genomic Sci. 2:176-185(2010).
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}.
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DR EMBL; CP001769; ADB36103.1; -; Genomic_DNA.
DR AlphaFoldDB; D2QBC1; -.
DR STRING; 504472.Slin_0029; -.
DR KEGG; sli:Slin_0029; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_10; -.
DR Proteomes; UP000002028; Chromosome.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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:ADB36103.1}.
FT DOMAIN 4..134
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 228..232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 260..267
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 357..359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 291
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 344
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 367
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 438 AA; 51289 MW; 53ACF1FF686E8245 CRC64;
MSEPLSLVWL RRDLRLHDNA ALYYALKSGR PVIPVFIFDR VILDALDDRL DRRVEFLVQE
VNRLHDELAK LGSTIIVRYG KPVDVWKELI ETYTIGDVFT NHDYEGYAKE RDKAIGELLA
ERGIGFHTSK DQAIFERDEV LSGKKTPYTV FTPYSRKWKD TLTDFYLKSY PTENYSSHYW
QTKPEPAITL ADMGFQPVGE PFPAETVSDK LLDTYNETRD FPALPHSTSQ LSIHLRFGTI
SIRELARQAK AADDQTFLNE LCWRDFYFQV LDHFPHVEQY SFRREYDQIE WRNNEDEFDK
WCRGETGYPI VDAGMRQLNT IGWMHNRVRM ITASFLCKHL LIDWRWGEAY FGKKLRDYDL
SANNGGWQWA AGSGTDAAPY FRVFNPTAQA QRFDPKSVYI RQWVPEVDKP SYPKPMVDHA
MARQRAIDTY RKALAKVK
//
