ID D1BDE7_SANKS Unreviewed; 450 AA.
AC D1BDE7;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase type I {ECO:0000313|EMBL:ACZ21009.1};
GN OrderedLocusNames=Sked_10630 {ECO:0000313|EMBL:ACZ21009.1};
OS Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=446469 {ECO:0000313|EMBL:ACZ21009.1, ECO:0000313|Proteomes:UP000000322};
RN [1] {ECO:0000313|EMBL:ACZ21009.1, ECO:0000313|Proteomes:UP000000322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74
RC {ECO:0000313|Proteomes:UP000000322};
RX PubMed=21304646;
RA Ivanova N., Sikorski J., Sims D., Brettin T., Detter J.C., Han C.,
RA Lapidus A., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Pati A.,
RA Mavromatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Goker M., Pukall R.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Sanguibacter keddieii type strain (ST-74).";
RL Stand. Genomic Sci. 1:110-118(2009).
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 ---------------------------------------------------------------------------
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; CP001819; ACZ21009.1; -; Genomic_DNA.
DR RefSeq; WP_012866078.1; NC_013521.1.
DR AlphaFoldDB; D1BDE7; -.
DR STRING; 446469.Sked_10630; -.
DR KEGG; ske:Sked_10630; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_11; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000000322; Chromosome.
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; 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:ACZ21009.1}.
FT DOMAIN 1..129
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 220..224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 355..357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 286
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 342
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 365
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 450 AA; 51125 MW; 54104B22F4C88CDB CRC64;
MTTIHWFRRD LRLADNPALN SAWEQAQADG SQVVGLFVLD DRLWGPSGSP RRDYLLASLR
ALDESMGGRL VVRRGAPTEV LPAVAREVGA RTVHVAESFE PFGRARDEEV ETALAEDDVE
LRRTGSAYAV SPGRVLTRTG TPYRVFTPFR TAWLDHGWCG PAQDPGEVDW AELPSEDLPE
ADGEPLRPAG EEAALERWHE FLEDVAGYDD DRNRPDLDLT SRLSVPLKWG EIHPRTLLAD
LKNLRDEGAA SFRSELAWRE FHADVLFHSP EAATLSIREV MPDDAWTPRS QADRWFEAWT
EGRTGYPMVD AGMRQLLAEG WMHGRVRMLV GSFLVKDLHI PWQRGARHFM QHLLDADRSQ
NQLNWQWVAG TGLDASPYFR IFNPVTQGLK FDPDGEYVRR WVPELRGIPG KAVHEPWKLP
TPPEDYPDQL VDHGRERKES LDAYARFKDG
//
