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Database: UniProt
Entry: A0A2N4YDV3_9RHOB
LinkDB: A0A2N4YDV3_9RHOB
Original site: A0A2N4YDV3_9RHOB 
ID   A0A2N4YDV3_9RHOB        Unreviewed;       473 AA.
AC   A0A2N4YDV3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:PLL11373.1};
GN   ORFNames=C0V75_15160 {ECO:0000313|EMBL:PLL11373.1};
OS   Tabrizicola sp. TH137.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tabrizicola.
OX   NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL11373.1, ECO:0000313|Proteomes:UP000234539};
RN   [1] {ECO:0000313|EMBL:PLL11373.1, ECO:0000313|Proteomes:UP000234539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH137 {ECO:0000313|EMBL:PLL11373.1,
RC   ECO:0000313|Proteomes:UP000234539};
RA   Cai h.;
RT   "genomes of bacteria within cyanobacterial aggregates.";
RL   Submitted (DEC-2017) 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:PLL11373.1}.
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DR   EMBL; PKRQ01000005; PLL11373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N4YDV3; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000234539; 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:PLL11373.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234539}.
FT   DOMAIN          3..129
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         234..238
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"
FT   BINDING         369..371
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            303
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            356
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            379
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   473 AA;  52253 MW;  A7ED360101B27249 CRC64;
     MTPPLILWFR RDLRLDDLPM LSAALDSGQP VIPVFILDPE TEALGAAPKW RLGLGLQTFA
     ARLEAMGARI ILRRGPALAV LESLLAETGA TGVLWSRLYD PAAKARDSAV KAALKARGLR
     AESFAGHLMH EPWTVQTGQG GFYRVYTPYW RAVRGLPVAA PDPAPARLPV PEVWPASDRL
     EDWHLGAAMR RGAPVVAAHV RVGEAAALAR MEAFLSGPVH RYAEARDLPA EPGTSRLSEN
     LTYGEIGIRR LWHAALTAFE QGSPGAETFL KELVWREFSY HLLHHTPHIA TANWKADWDS
     FPWASQGPQL TAWQRGMTGE PFVDAALREL YVTGTMHNRG RMIVASYLTK HLMTHWKAGL
     DWFADCLVDW DPAANAMGWQ WAAGSGPDAA PYFRIFNPAT QVEKFDPSGL YRRRFLAELS
     RNPGPEALAF FDAAPRSWNL DPARPYPRPI VDLATGRARA LAAYAARGGQ EPD
//
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