ID A0A1L2ZPA5_9MICC Unreviewed; 442 AA.
AC A0A1L2ZPA5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:APF41204.1};
GN ORFNames=BHE16_09625 {ECO:0000313|EMBL:APF41204.1};
OS Neomicrococcus aestuarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Neomicrococcus.
OX NCBI_TaxID=556325 {ECO:0000313|EMBL:APF41204.1, ECO:0000313|Proteomes:UP000183530};
RN [1] {ECO:0000313|EMBL:APF41204.1, ECO:0000313|Proteomes:UP000183530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18 {ECO:0000313|EMBL:APF41204.1,
RC ECO:0000313|Proteomes:UP000183530};
RA Luo Y.;
RT "Genome sequencing of Zhihengliuella aestuarii B18 antagonistic to
RT Plasmodiophora brassicae.";
RL Submitted (NOV-2016) 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}.
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DR EMBL; CP018135; APF41204.1; -; Genomic_DNA.
DR RefSeq; WP_071894673.1; NZ_CP018135.1.
DR AlphaFoldDB; A0A1L2ZPA5; -.
DR STRING; 556325.BHE16_09625; -.
DR KEGG; nae:BHE16_09625; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000183530; Chromosome.
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; 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:APF41204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183530}.
FT DOMAIN 1..129
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 235..239
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 367..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 300
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 354
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 377
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 442 AA; 50426 MW; E9DCFD68C77D738F CRC64;
MVAITWFRDD LRLADNAALS AAAKDPDGIV ALYVLDDETA EVRPLGSAAR WWLHESLQQL
ERSLATYSIP LILRRGPAEQ VLTEVVSEVG ATAVHWNRRY GAARALDARL KESLTARGIT
AHSYPGNLLF EPWTVANSSG DPYAVYSAFW RACLSSPEPD HPLPIPTTLI PGGQQPYSED
LTAWNLQPVT PRWWNGFHDR WVPGEAKALE KLTHFLERAV TRYHEERDFP ARSATSELSP
HLRFGEISPR TIWHISRAAN QEVEVFLSEL GWREFAWHTA YAFPDLHQRS LNQKYQDFPW
RKGAGDEVQA WQRGNTGYGI VDAGMRELWQ TGFMHNRVRM VAASFLTKNL LVDWRVGEEW
FWDTLVDADE ASNPFNWQWV AGCGRDASPY FRIFNPQTQQ KKFDHDGLYV NCWAPESANL
EPVVDLSHSR SEALAAYESI RH
//
