ID A0A1V3RGV5_9FLAO Unreviewed; 494 AA.
AC A0A1V3RGV5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:OOG76110.1};
GN ORFNames=B0E44_04300 {ECO:0000313|EMBL:OOG76110.1};
OS Flavobacterium sp. A45.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1945862 {ECO:0000313|EMBL:OOG76110.1, ECO:0000313|Proteomes:UP000188437};
RN [1] {ECO:0000313|EMBL:OOG76110.1, ECO:0000313|Proteomes:UP000188437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A45 {ECO:0000313|EMBL:OOG76110.1,
RC ECO:0000313|Proteomes:UP000188437};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:OOG76110.1}.
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DR EMBL; MUNX01000058; OOG76110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3RGV5; -.
DR STRING; 1945862.B0E44_04300; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000188437; 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; 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:OOG76110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188437}.
FT DOMAIN 7..137
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 494 AA; 58187 MW; 3AE4543E31023ABC CRC64;
MNTYKSHINI VWFKRDLRLQ DNEAIFNAIQ SNKPTLLLYV FENSLQNDGH YSERHWDFIK
QSIKDINQQL APLNTKVLSV SGEVISIINS IQEIYKIDTV FSHQETGIKI TYERDKSFKR
FCKNNLIIWK ENINNGIFRA LENRKNWIKL WEDYMNSKQF PFEAASQNFL SLESILFLEN
SFETVSLQTI PNDVFQKGGT NMGNKYLESF FYDRYQDYNR NISKPLLARK SCSRLSPYIA
WGNLSSRQVL QQAANFRLTS NNKKQIDSFV SRLTWQAHFI QKFEMEEIME FESVNKGFHT
LKKKTNHSYI QAWQTGQTGF PIIDACMRCL NQTGYLNFRM RAMVVSFFTH NLWQPWQEAA
PHLSQMFLDF EPGIHYPQLQ MQAGETGINM LRIYNPLKNS LEHDPNGEFI KKWVSELQNL
PIPFIHNPSK MTFLDQKFSN FDLGVDYPKP IVNIERTRKH ASDFLWNMKK NPLVKEENNR
ILKLHTMADV GDSD
//
