ID A0A0P7Y0K4_9RHOB Unreviewed; 511 AA.
AC A0A0P7Y0K4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:KPQ13792.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:KPQ13792.1};
GN Name=phrB-3 {ECO:0000313|EMBL:KPQ13792.1};
GN ORFNames=HLUCCO18_16885 {ECO:0000313|EMBL:KPQ13792.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ13792.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ13792.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ13792.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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 -!- 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:KPQ13792.1}.
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DR EMBL; LJSY01000056; KPQ13792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7Y0K4; -.
DR STRING; 1666917.HLUCCO18_16885; -.
DR PATRIC; fig|1666917.4.peg.3156; -.
DR Proteomes; UP000050333; Unassembled WGS sequence.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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 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 4: Predicted;
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:KPQ13792.1}.
FT DOMAIN 3..133
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 480..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211
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"
SQ SEQUENCE 511 AA; 56388 MW; 2B68EBC03893D18B CRC64;
MGDGVLLWFK RDLRVRDNPA LHLAAARGGP VLPLFIVEPG AWAQPDASAR QYRFMAECLA
ALRADLAVMG APLVVRVGEA VAVLETLCAQ FGIREIVSAE ETGNAWSYAR DRAVGALARA
QGLAWTEVPQ PGVVRRLQGR DGWAARRERA MRQPRLGVPA AIEGFAIDPG AIPEARDLRL
AFDPCPGRQR GGRPEAEALL ASFLDNRGQT YRRAMSSPLE GETACSRLSA HLAWGTLGPR
EAVQAAAARK ASANGTRAGW RGAMRSFEAR LAWRDHFMQK LEDEPAIETH CLHPAYEGLR
PRGSDAARLA AWEKGETGIP FVDACMRYLD HGGWLNFRMR AMLVAVASYH LWLDWRDTGP
HLARMFTDYE PGIHWPQMQM QSGTTGMNTV RIYNPLKQGT DQDPGGVFTR RWVPELAEIP
DAFLQAPWGW EGAGRVLGKR YPEPIVDVAG AARAARDRVW AVRRGAAFRG EAARIVEKHA
SRKDGGPGRH FVNDRDARGR QGDARQLKLD L
//
