ID E3RIQ1_PYRTT Unreviewed; 632 AA.
AC E3RIQ1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN ORFNames=PTT_07932 {ECO:0000313|EMBL:EFQ94400.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94400.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94400.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR EMBL; GL533345; EFQ94400.1; -; Genomic_DNA.
DR RefSeq; XP_003297506.1; XM_003297458.1.
DR AlphaFoldDB; E3RIQ1; -.
DR STRING; 861557.E3RIQ1; -.
DR EnsemblFungi; EFQ94400; EFQ94400; PTT_07932.
DR KEGG; pte:PTT_07932; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_2_1_1; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
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:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 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};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 135..272
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 387..391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 427
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 430..437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 528..530
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 462
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 515
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 538
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 632 AA; 72133 MW; C2EDDA73840FA14F CRC64;
MPTKRKAGIP PNAESAIKYT DVSGNAPNKR SRIANPIQKA FTESTSPIED TAKVTENGAP
GEAVKEKAGQ FDHSRSEERA GIVDRRYYPA EISNERCAMY NANEIPRPIE ILEKTLHTTS
QAREKIRLGK DGSGDAVVHW FKRDLRIRDN TGLSKAAELA KERGVGLIGI WLMSPQDWEA
HLVSPPKCDF ELRSVELLQK ELSELDIPLY IETIPERKNV TKRLVELAQE WNVKNVFCNL
EYEPDELRRE ERLVRMMLEK GIGFDPYHDD CVVPPGSLKT GAGKQYAVYS PWCRAWIAHL
HAHPDLLIER PMPGRNPTNF RDKFSKLFEF SVPSLPECKA LTPEEKERFS RLWPAGEAAA
VDRLERFLVE KIVKYKDTRN FPALNSTGRV SVHHAAGTLA ARTSIRMARD INSAQKLDGG
KDGVKTWIGE VAWRDFYRHV LVNWPYVCMN KPFKYEYTNI HWEYNTAHFT AWTRGLTGYP
IVDAAMRCLN HTGYMHNRLR MITASFLSKH LLLDWRLGEQ YFLTHLIDGD FASNNGGWGF
SASTGVDPQP YFRIFNPWIQ SEKFDADGEF IRMWVEELSG VQGKEVHNPY AAGGKAAEVA
RRMGYPEPVV EHRVARERCL KRYKEGIGRD TA
//
