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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//