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Database: UniProt
Entry: A0A074JU80_9RHOB
LinkDB: A0A074JU80_9RHOB
Original site: A0A074JU80_9RHOB 
ID   A0A074JU80_9RHOB        Unreviewed;       472 AA.
AC   A0A074JU80;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN   ORFNames=DT23_09995 {ECO:0000313|EMBL:KEO61226.1};
OS   Thioclava indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO61226.1, ECO:0000313|Proteomes:UP000027471};
RN   [1] {ECO:0000313|EMBL:KEO61226.1, ECO:0000313|Proteomes:UP000027471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DT23-4 {ECO:0000313|EMBL:KEO61226.1,
RC   ECO:0000313|Proteomes:UP000027471};
RX   PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA   Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT   "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT   Ocean.";
RL   Antonie Van Leeuwenhoek 107:297-304(2015).
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 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:KEO61226.1}.
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DR   EMBL; AUNB01000009; KEO61226.1; -; Genomic_DNA.
DR   RefSeq; WP_038128129.1; NZ_AUNB01000009.1.
DR   AlphaFoldDB; A0A074JU80; -.
DR   STRING; 1353528.DT23_09995; -.
DR   eggNOG; COG0415; Bacteria.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000027471; Unassembled WGS sequence.
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; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {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}; Reference proteome {ECO:0000313|Proteomes:UP000027471}.
FT   DOMAIN          4..130
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         235..239
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         270
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         370..372
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            304
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            357
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            380
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   472 AA;  53345 MW;  76CECDE71EAEE112 CRC64;
     MSADVTLLWL RRDFRFYDHP AMVAAAANGA AVIPVFIYDD QVAALGAAPK WRLGEAVDHF
     ADALAEKGSR LILRKGDPLE VLRALIAQTG ARAVHWSRAY DPASVARDKA VKAALKEDGI
     TAESQAGHLL FEPWSVQTGK GEPYKVYSPY WRAVKGRDIA APLKTVSELR APSNWPDSET
     LSDWQMGDAM NRGAEVVAKY AHIGEARAQG RLSTFLRDHI EHYKTERDFP ASGATSGLSE
     NLTYGEISPR AVWHAGWRHV QEGAAGAEHF LKELVWREFA WHLLYHFPDL AEANWRKEWN
     GFPWRPDNND AKAWRRGMTG EPFVDAAMRE MYVTGTMHNR ARMIVASYLT KHLMTDWRVG
     RRWFEDCLID WDPASNAMGW QWVAGSGPDA APYFRVFNPE TQLKKFDKTK DYRDKFILEG
     QSNPPQTARD FFDAIPRSWG LTPDQSYPAQ IADLKGGREC ALAAYHAHRD TD
//
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