ID A0A1J4QCU6_9GAMM Unreviewed; 469 AA.
AC A0A1J4QCU6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:OIN08154.1};
GN ORFNames=BFR47_15560 {ECO:0000313|EMBL:OIN08154.1};
OS Oceanisphaera psychrotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanisphaera.
OX NCBI_TaxID=1414654 {ECO:0000313|EMBL:OIN08154.1, ECO:0000313|Proteomes:UP000243073};
RN [1] {ECO:0000313|EMBL:OIN08154.1, ECO:0000313|Proteomes:UP000243073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM-WHM-ZC {ECO:0000313|EMBL:OIN08154.1,
RC ECO:0000313|Proteomes:UP000243073};
RA Zhuo S., Ruan Z.;
RT "Draft Genome Sequence of Oceanisphaera psychrotolerans, isolated from
RT coastal sediment samples.";
RL Submitted (JUL-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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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:OIN08154.1}.
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DR EMBL; MDKE01000028; OIN08154.1; -; Genomic_DNA.
DR RefSeq; WP_071473081.1; NZ_MDKE01000028.1.
DR AlphaFoldDB; A0A1J4QCU6; -.
DR STRING; 1414654.BFR47_15560; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000243073; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
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; IPR018394; DNA_photolyase_1_CS_C.
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; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, 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:OIN08154.1}.
FT DOMAIN 1..131
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 228..232
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 270..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 302
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 355
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 378
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 469 AA; 53317 MW; 9E812A69A02FC15D CRC64;
MRHLVWFRTD LRVADNPALY EAAADDAEVE AVYVDCPGQW QEHGKSAMQR DFLSRNLQAL
NEQLAGLGIP LTVLTADTFS ETPDLLVRWL EGRHFDALYA NREIGIDERR RDKELQRRLS
IPCRVYNGDC VLDHGSLTTR SGDMYKVFTP FSKTWLAKLR AGGYRLLPVP AAQAEALSSE
PLSLSGERVS SDDWPAGEAD AAQRLSQFCQ RSLREYGERR DYPAQDGTSS LSPYLALGVL
SPNQCLSAME SELGQLPFSR GEPGFVWLNE LIWREFYRHL LVAFPRLSMD RAFRPETEAL
QWSRDDEGFR AWCEGHTGYP IVDAAMRCLN QTGWMHNRLR MIVASFLTKD LHIDWRRGER
YFMSRLIDGE LAANNGGWQW AAGTGADAAP YFRVFNPTTQ GERFDAEGDF LRCWLPELAE
VPARVIHSPH DWLDNHSPGH GYAKPIVDHG RARLHAIAMF DALKDRETV
//
