ID   F6D9K1_THICA            Unreviewed;       478 AA.
AC   F6D9K1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:AEG30958.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:AEG30958.1};
GN   OrderedLocusNames=Thicy_0182 {ECO:0000313|EMBL:AEG30958.1};
OS   Thiomicrospira cyclica (strain DSM 14477 / JCM 11371 / ALM1)
OS   (Thioalkalimicrobium cyclicum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=717773 {ECO:0000313|EMBL:AEG30958.1, ECO:0000313|Proteomes:UP000009232};
RN   [1] {ECO:0000313|EMBL:AEG30958.1, ECO:0000313|Proteomes:UP000009232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14477 / JCM 11371 / ALM1
RC   {ECO:0000313|Proteomes:UP000009232};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Kappler U., Woyke T.;
RT   "Complete sequence of Thioalkalimicrobium cyclicum ALM1.";
RL   Submitted (MAY-2011) 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 class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase family.
CC       {ECO:0000256|RuleBase:RU004182}.
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DR   EMBL; CP002776; AEG30958.1; -; Genomic_DNA.
DR   RefSeq; WP_013834741.1; NC_015581.1.
DR   AlphaFoldDB; F6D9K1; -.
DR   STRING; 717773.Thicy_0182; -.
DR   KEGG; tcy:Thicy_0182; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_2_2_6; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000009232; 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; 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:AEG30958.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009232}.
FT   DOMAIN          1..129
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         234..238
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         272
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         372..374
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            306
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            359
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            382
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   478 AA;  54998 MW;  D716FF62567AB714 CRC64;
     MNQLIWFQRD LRLNDHTPIH RALSQNEPTL FAYFHDPQQA QGEANQVWLA ASLSKLQTAL
     QAKNADLLVA EGEFSQAFER VLTTYNVKNV LYHFELGEPY QTIQQQALAV CQRLKVRLTP
     FDQAWLPPES VLTQQGNPYG VYTPFSKKVF SMLDGVPKPE GEANWSNFQP VTLENHDRQL
     PSRLKAIANT DWAKPLISQW KVGEQAAINQ ATHFLTTHIQ HYPERRDFPA INGTSQLSIH
     LHFGEISSTR LLESCRQAQA NQPGHSEAIQ SFIRQLIWRE FSRYLLFFNP GLINQAYQSK
     FNQIDWPEPD DQVVAWQRGL TGVPIIDAGM RQLWHTGWMH NRVRMLVGSW LTKNLNQHWL
     VGQAWFENTL LDADIANNVM GWQWVAGCGV DAAPYFRLFN PVVQSEKFDP QGHYIRQWLP
     ELAPLPNQLI HAPWDAAGKI KQQFPTLAAN YPLHDPNLKQ VRLDHQQRVQ ALKMMTNA
//