ID A0A2J6TF53_9HELO Unreviewed; 595 AA.
AC A0A2J6TF53;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN ORFNames=K444DRAFT_525843 {ECO:0000313|EMBL:PMD61640.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD61640.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD61640.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD61640.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR EMBL; KZ613786; PMD61640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TF53; -.
DR STRING; 1095630.A0A2J6TF53; -.
DR InParanoid; A0A2J6TF53; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000235371; 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; 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:UP000235371}.
FT DOMAIN 100..237
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 352..356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 395..402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 493..495
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 427
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 480
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 503
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 595 AA; 67777 MW; 4E6CF5D0696F3F8D CRC64;
MPPKKAITNG KRKASTSAEP TSNGMKKSKL DGTNDHIKEP HPKAQEAEEN GIVLRKYYPH
EMSNARALAY NNGEITRPIE LLNAALSGTK EQREKIQVKD AVVHWFKCDL RTKDNKSLHL
ASEKAKEKGV PLIGMYIVSP QDFEAHLTAP VRVDFILRTL EVLKSDLAKL DIPLYVETVE
KRKKIPDRIL ELLDVWGASH LFANVEYEVD ELRREASLVR ACLERGIAMD VVPDTCVVSP
GELASGTGRQ YSIYTPWFRA WVAYIHGHAD VLNLFDEPGK NPESARKKLR KLFESNIPSA
PENKKLTEEE KERFRSMWPS GEHEAHERLK RFCDERIGGY SDNRNFPAKG ATSSLSVHLA
SGTLSSRTCV RTARDHNSTK KLDGGNQGIQ TWISEVAWRD FYKHVMAHWP YVCMNTPFKP
EYTNIDWEYN NEHFKAWCDG KTGYPIVDAA MRQLKHCGYM HNRCRMIVGS FLAKHLLLDW
RMGERYFMEH LIDGDFASNN GGWGFSASTG VDPQPYFRIF NPLLQSEKFD AGGEYIRKWV
PELEGIQGNA IHDPHARGKG NEAKRKGYPE RIVDHKESRD RALARYKQGL GRDAA
//
