ID A0A0Q7ZDL0_9ACTN Unreviewed; 456 AA.
AC A0A0Q7ZDL0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KQZ67023.1};
GN ORFNames=ASD66_18695 {ECO:0000313|EMBL:KQZ67023.1};
OS Nocardioides sp. Root151.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ67023.1, ECO:0000313|Proteomes:UP000051274};
RN [1] {ECO:0000313|EMBL:KQZ67023.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ67023.1,
RC ECO:0000313|Proteomes:UP000051274};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ67023.1, ECO:0000313|Proteomes:UP000051274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root151 {ECO:0000313|EMBL:KQZ67023.1,
RC ECO:0000313|Proteomes:UP000051274};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ67023.1}.
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DR EMBL; LMGG01000007; KQZ67023.1; -; Genomic_DNA.
DR RefSeq; WP_056682224.1; NZ_LMGG01000007.1.
DR AlphaFoldDB; A0A0Q7ZDL0; -.
DR Proteomes; UP000051274; 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:KQZ67023.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051274}.
FT DOMAIN 4..134
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 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 297
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 350
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 373
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 456 AA; 51197 MW; B3AEC88C2C25B553 CRC64;
MTTRTAIVLF TRDLRVHDNP TLQAAADQAD HVLPLFVFDD AIAGSTYLAP NRAAFLTDSL
SDLDESLRGC GSDGLVVRRG DPADEVAALA REVGASSVHL SGDWSRHAQR RLERLRNAVD
GSAVDVVVHD ETLTVSPPGV VTPDKSDHFA VFTPYHRRWS DRPLRPVLGQ GPRLVSPRVR
RGRIPTADTL SPGDSLARHL PVGGETAGRR RMSAWLDSSV TDYEDRHDDL PGDATSRLSP
YLHFGCVSPV ELVANAGRSQ GAQAFVRQLA WRDFHLQVLA ARPDAAHTDY RDRGDRWRQD
ADDLRAWQEG RTGFPIIDAA MRQLREEGWM HNRARLLVGS FLTKTLYLDW REGARHFLHH
LVDGEVSNNQ LNWQWVAGTG TDSRPNRVLN PLTQADRHDP DGDYVRHYVP ELADVEGGAV
HRPWRLPDEV RSRLDYPEPI VDLAEGRRRF LEARDR
//
