ID A0A1I3Q2X3_9ACTN Unreviewed; 440 AA.
AC A0A1I3Q2X3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:SFJ27807.1};
GN ORFNames=SAMN05216561_12312 {ECO:0000313|EMBL:SFJ27807.1};
OS Nocardioides psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005945 {ECO:0000313|EMBL:SFJ27807.1, ECO:0000313|Proteomes:UP000198649};
RN [1] {ECO:0000313|EMBL:SFJ27807.1, ECO:0000313|Proteomes:UP000198649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11156 {ECO:0000313|EMBL:SFJ27807.1,
RC ECO:0000313|Proteomes:UP000198649};
RA de Groot N.N.;
RL Submitted (OCT-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; FOQG01000023; SFJ27807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3Q2X3; -.
DR STRING; 1005945.SAMN05216561_12312; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000198649; 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; 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:SFJ27807.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198649}.
FT DOMAIN 1..122
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 402..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 217..221
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 249
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 252..259
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 349..351
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 440 AA; 49137 MW; 3DF16E23AEF51829 CRC64;
MPSVMWFRRD LRLRDNPALV AAVADGDVLP LFVLDPALWD PAGAVRRAYL GASLRSLAED
LPLCVLHGDP VSQVVRAARE VGAARVHVAA DFGPYGHDRD LRVEAALADA GIELERTGSP
YAVAPGRVTN GSGAPYKVYT PFSRAWADHG WRGAVDAPSD VTWLRVEDTV DLPDDTAPEG
VELPEAGEAA AHARWSDFLD RVADYDEDRD KPGVEGTSRM SVHLKWGEIH PRSMLADLAP
LRSAGAATYR KELAWREFYA DVLAAQPHTA RDYLRPDYAR MRYDEPGAQL DAWREGRTGF
PVVDAGMRQL RATGWMHNRV RMIVASFLVK DLHLEWQHGA RHFMERLVDA DLASNQHGWQ
WTAGSGTDAS PYFRVFNPTS QGKKFDPRGD YVRRWVPELA DVADPHDPSA DDRDRVDYPS
PLVDHGAERQ EALARWEEIR
//
