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Database: UniProt
Entry: A0A2A3XC63_9GAMM
LinkDB: A0A2A3XC63_9GAMM
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ID   A0A2A3XC63_9GAMM        Unreviewed;       525 AA.
AC   A0A2A3XC63;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:PCC21385.1};
GN   ORFNames=CIK78_04445 {ECO:0000313|EMBL:PCC21385.1};
OS   Halomonas sp. JB37.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=2024405 {ECO:0000313|EMBL:PCC21385.1, ECO:0000313|Proteomes:UP000217454};
RN   [1] {ECO:0000313|EMBL:PCC21385.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB37 {ECO:0000313|EMBL:PCC21385.1};
RX   PubMed=28644126;
RA   Bonham K.S., Wolfe B.E., Dutton R.J.;
RT   "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL   Elife 6:e22144-e22144(2017).
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   -!- 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:PCC21385.1}.
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DR   EMBL; NRGW01000001; PCC21385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3XC63; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000217454; 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   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};
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:PCC21385.1}.
FT   DOMAIN          5..134
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          492..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         277
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ   SEQUENCE   525 AA;  60092 MW;  4F3F119FA2E50599 CRC64;
     MAKAPIQVVW FKRDLRIHDN APLTNAAAAG PVLPLFAIEP EQWHAPDSAL RHWQFAADSL
     IDLSNALEKL GLPLCIWQGD MIDLLNALKT HYGEFALHSH EETGNAWSFA RDLSVKAWCQ
     QHDTPWHEAR QHGVVRGLKS RVADRSAWET QWETLMTAPT ATAPSNAQAA PDWQAFHHIN
     VDHLHRLTLG FDTTPCPERQ PGGRSEGRAI WRSFISQRGR RYRGSLSKPL LAWEFGSRLS
     PHLAWGTLSM REVVQSLRRQ RKKHAEDTAW SRSLRAFASR LHWHCHFIQK LESEPSIESQ
     TLHPALRGLR ERDPEPPNLI AWKRGQTGVP LVDACMRSLI NTGWINFRMR AMLISHATFG
     LGLHWYEPAL HLARLFTDFE PGIHYPQVQM QAGATGINAL RVYNPIKQAE DNDPTGEFVA
     RWVPELTVLP LEWRAKPWAL PESLQKRFDF QPGVNYPIPN DFETEARHWK KMLYELRRTP
     DAREASQAIV DKLASQRRPS KQHVKKAKPA NRQQLSLFDE GGLEE
//
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