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Database: UniProt
Entry: A0A0C1RLS7_9ACTN
LinkDB: A0A0C1RLS7_9ACTN
Original site: A0A0C1RLS7_9ACTN 
ID   A0A0C1RLS7_9ACTN        Unreviewed;       449 AA.
AC   A0A0C1RLS7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN   ORFNames=MB52_01520 {ECO:0000313|EMBL:KIE51761.1};
OS   marine actinobacterium MedAcidi-G1.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550399 {ECO:0000313|EMBL:KIE51761.1, ECO:0000313|Proteomes:UP000031399};
RN   [1] {ECO:0000313|EMBL:KIE51761.1, ECO:0000313|Proteomes:UP000031399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-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:KIE51761.1}.
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DR   EMBL; JUEM01000003; KIE51761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1RLS7; -.
DR   Proteomes; UP000031399; Unassembled WGS sequence.
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}.
FT   DOMAIN          3..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         231..235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         260
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         263..270
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         358..360
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            292
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            345
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            368
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   449 AA;  51752 MW;  FE3B2DE29E0AD23C CRC64;
     MDSPNIIVFT RDLRVRDNPA LDAAVSMPGP TVALFVFDEL ITDKKSPSPN RFQFLIDSLR
     DLDASLKKIG SQLIIRQGKW VDEITKVALE TQSKQIHVSN DFSLLAKTRL EALIERGEST
     GFKISVHPGV SLVEPGHLTP ADGREYKVFT PYYRRWLETS WREPVKTPKF IQSIDTDGDH
     IEILEKYDQK NLSPFLLKGG ETEGISRLND WMTKEISDYE KGRDDIEGDR TSRLSPYLHF
     GCLSPLEVAL QALEFGGDAF VRQLCWRDFY LQILHHRPDS SRSDYRDRKY DWNKNPEAFR
     LWKEGKTGFP IVDAGMRQLL AEGFMHNRVR MIVASFLTKD LHLDWRIGAE HFMNYLIDGD
     VASNQLNWQW VAGTGTDSNP HRIFNPVRQS ERFDADGKYI HKWVPELKDI LGNDVHNPDR
     KSRLEASYPE AMLDHHEAIA IYKSKYSGK
//
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