ID   A0A1I1ZH78_9BACT        Unreviewed;       559 AA.
AC   A0A1I1ZH78;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase family protein (Cryptochrome) {ECO:0000313|EMBL:SFE29690.1};
GN   ORFNames=SAMN05216167_11287 {ECO:0000313|EMBL:SFE29690.1};
OS   Spirosoma endophyticum.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=662367 {ECO:0000313|EMBL:SFE29690.1, ECO:0000313|Proteomes:UP000198598};
RN   [1] {ECO:0000313|EMBL:SFE29690.1, ECO:0000313|Proteomes:UP000198598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26130 {ECO:0000313|EMBL:SFE29690.1,
RC   ECO:0000313|Proteomes:UP000198598};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
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; FOLQ01000012; SFE29690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1ZH78; -.
DR   STRING; 662367.SAMN05216167_11287; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000198598; 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; 2.
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:SFE29690.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198598}.
FT   DOMAIN          6..173
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          515..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         255
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         309
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   559 AA;  64427 MW;  3F17ACF5432EB1A7 CRC64;
     MPDQPTINIL WFKRDLRLRD HAPLQAAIAR GQRVPKRPLL LLYCFEPSVM ADPNYELRHW
     RFVHECLADL QQQLATMPPA AVSETSPLVH EWLPFDFEDP ADEPTPETGP PAVWIFHREV
     TDVLTALQTQ FTIGSLFSHE ETGLAVTYDR DKAVARFCRQ QGIPWHEYQN NGVIRRLKNR
     DTWATDWQQT MQAPQQQPDL TRWLPAPVPL TWYEAERGPE LPIEWQTPHP SYQPGGEYNG
     HRYLTSFLTE RIARYAASIS KPLESRRGCS RLSPYLAWGC LSIRQVYQAQ REAARKPALV
     GLGRQLAAFA SRLRWHCHFI QKFEDEDRME FENVNRAFET LPKNTNPDHY AAWRDGRTGY
     PLIDACMRCL AATGYINFRM RAMLTSFLTH HLFQHWQEGG WHLARLYTDF EPGIHYAQIQ
     MQSGMTGTNT IRIYNPVKQS QDHDPQGVFI RQWVPELVNC PLAYIHHPWT MPPLEQAMDH
     FQVGVDYPAP IIDAAVMARQ ARLLLHQPRQ SEVGQAEQAR ILEKHSLPVS DRPKKTARKP
     GKKGKKTTTG PEGVGPLLP
//