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Database: UniProt
Entry: A0A1H9TBC3_9RHOB
LinkDB: A0A1H9TBC3_9RHOB
Original site: A0A1H9TBC3_9RHOB 
ID   A0A1H9TBC3_9RHOB        Unreviewed;       473 AA.
AC   A0A1H9TBC3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:SER94522.1};
GN   ORFNames=SAMN04490244_10477 {ECO:0000313|EMBL:SER94522.1};
OS   Tranquillimonas rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=641238 {ECO:0000313|EMBL:SER94522.1, ECO:0000313|Proteomes:UP000198885};
RN   [1] {ECO:0000313|EMBL:SER94522.1, ECO:0000313|Proteomes:UP000198885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23042 {ECO:0000313|EMBL:SER94522.1,
RC   ECO:0000313|Proteomes:UP000198885};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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 family.
CC       {ECO:0000256|RuleBase:RU004182}.
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DR   EMBL; FOGU01000004; SER94522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9TBC3; -.
DR   STRING; 641238.SAMN04490244_10477; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000198885; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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}; Lyase {ECO:0000313|EMBL:SER94522.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198885}.
FT   DOMAIN          5..131
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         236..240
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         373..375
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            305
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            360
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            383
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   473 AA;  53232 MW;  63D5654423F35875 CRC64;
     MTDDSPILFW HRRDLRLTDN PGLAAAALTG RPVIPVFILD EVFDSHGAAP KWRLGLGLEA
     FGAALAERGA RLVLRRGGAL QTLAALVRET GAGAVWWNRL YDPDSVERDT GVKADLKADG
     IDAQSFAGHI LHEPWEVETK QGDYYKVFTP FWRAVKDREV PDPVTAPSDL TAPDSWPDSD
     ALEDWQLGAA MDRGAPIVGK HVVVGERAAQ GRLAAFIGQR VQDYGDARDL PSVDGTSRLS
     ENLTLGEISI RSCWHAGLRA QADGKDGAGT FLQELVWRDF GHHLAYNTPR LTSENWREEW
     DAFPWNEDER KAEVIAWKRG RTGIRFVDAA MRELYVTGHM HNRSRMIVAS YLCKHLMCHW
     KIGKAWFEEH LTDWDPASNA LGWQWSAGSG PDATPYFRVF NPVTQLDRFD KKRTYVGHWI
     AEGQSQPSRD ALDYFEAIPR RWGLSPDDDY PEPVVGADEG RKRALEAYEN RSF
//
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