ID A0A2N5N044_9BACL Unreviewed; 503 AA.
AC A0A2N5N044;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:PLT43717.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:PLT43717.1};
GN ORFNames=B8V81_2148 {ECO:0000313|EMBL:PLT43717.1};
OS Paenibacillus pasadenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=217090 {ECO:0000313|EMBL:PLT43717.1, ECO:0000313|Proteomes:UP000234789};
RN [1] {ECO:0000313|EMBL:PLT43717.1, ECO:0000313|Proteomes:UP000234789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R16 {ECO:0000313|EMBL:PLT43717.1,
RC ECO:0000313|Proteomes:UP000234789};
RA Passera A., Marcolungo L., Casati P., Brasca M., Quaglino F.,
RA Delledonne M.;
RT "Functional genome analysis of Paenibacillus pasadenensis strain R16:
RT insights on endophytic life style and antifungal activity.";
RL Submitted (MAY-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:PLT43717.1}.
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DR EMBL; NFEZ01000004; PLT43717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5N044; -.
DR Proteomes; UP000234789; 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 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:PLT43717.1}.
FT DOMAIN 1..129
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 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 315..322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 408..410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 503 AA; 55884 MW; B3DEA2627C5C67F7 CRC64;
MYLFIHRKDL RAGDLRAFDY AASLGMPGIH ALILDPAQLG DGRAESHPGR HFLRAAGLLL
RDYAAQGAEL QLLHGNPALV LDELLEREPI REVVVTADHT PYARRRDERL AAVCRSRGVR
WTALEDVPLA DLDAFQEQTG RKEPYRVFTP FYRAWNGYVR SRLAPPPAVA AGGLPIARLS
GGGSWSVPGE LAGLLAAPVP EDERPERQLE RFLGGSLQAY EELRDRYALD AGSGLSRWLN
VGALSARRAY GLALDAARTE DGREPLAFGG AADWRADAAG QLELALPGSG EGPGSAPRDP
SAAAARSGAE SWIRQLAWRE FYLYQARFDA DFFRYEEQVD LSGLTERHAE AWRQGRTGIP
LIDAAMTQLR TTGELPNRLR MIAAMFLCKN LLAPFTAGER WFREQLLDYD ATLNRGGWLW
SSSLGFDAAP YFRIMNPVVQ SKRWDPDGAY IRRWLPERAG WSAAAVHEPS PQAVVDLKAS
RARAIETYKR LLAKPSRPLD RLH
//
