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Database: UniProt
Entry: Q0FFF3_9RHOB
LinkDB: Q0FFF3_9RHOB
Original site: Q0FFF3_9RHOB 
ID   Q0FFF3_9RHOB            Unreviewed;       465 AA.
AC   Q0FFF3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=DNA photolyase, Cryptochrome 1 apoprotein (Blue light photoreceptor) {ECO:0000313|EMBL:EAU53036.1};
GN   ORFNames=OM2255_05890 {ECO:0000313|EMBL:EAU53036.1};
OS   Rhodobacterales bacterium HTCC2255.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU53036.1, ECO:0000313|Proteomes:UP000009381};
RN   [1] {ECO:0000313|EMBL:EAU53036.1, ECO:0000313|Proteomes:UP000009381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU53036.1,
RC   ECO:0000313|Proteomes:UP000009381};
RA   Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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}.
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:EAU53036.1}.
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DR   EMBL; AATR01000001; EAU53036.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0FFF3; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_2_2_5; -.
DR   OrthoDB; 9772484at2; -.
DR   BioCyc; RBAC367336:G1GNW-620-MONOMER; -.
DR   Proteomes; UP000009381; 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:EAU53036.1};
KW   Receptor {ECO:0000313|EMBL:EAU53036.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009381}.
FT   DOMAIN          5..126
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         220
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         232..236
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         267
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         367..369
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            301
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            354
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            377
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   465 AA;  53727 MW;  B0AC923E107503F6 CRC64;
     MVTQAPIIIW FRRDFRFSDH EALSAAHSSG RPIIPIFIFD EVFEALGAAP KWRLGLAIEC
     FKKKLERMGS NLILRRGNAC EILQELVNET GALDVYWSRA YDPVSIHRDT KVKSLLNGTS
     FKGHVLFEPW VPKTKSGENF KVYTPFWRHV SSQLTVNSTL SKISKLHSPH VWPKSDLLSN
     WGLGEEMNRG RNVVSKYINV GEEVALNKLE NFIVSKVNGY KIDRDFPMRH ATSGLSENLT
     YGEISPRLIF NSLRNTFDKN DLGAEHFLKE LVWREFAYHL LWHFPKLDTQ CWRGEWNDFP
     WKGINKNAKA WMQGRTGQSF VDAGMRELYT TGTMHNRLRM IVGSYLTKHL QTDWRIGLKW
     FEDCLIDWDP ASNAMGWQWI AGCGADAAPY FRIFNPNLQA EKFDSDGQYR KKWLEADKEL
     HAKAFFDAIP VAWKLSADKI NQNEIIDLSL GRKIALDAYA IFKKQ
//
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