ID   A0A0B7FNT9_THACB        Unreviewed;       649 AA.
AC   A0A0B7FNT9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Cryptochrome-2 {ECO:0000313|EMBL:CEL59601.1};
GN   ORFNames=RSOLAG1IB_03534 {ECO:0000313|EMBL:CEL59601.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL59601.1, ECO:0000313|Proteomes:UP000059188};
RN   [1] {ECO:0000313|EMBL:CEL59601.1, ECO:0000313|Proteomes:UP000059188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL59601.1};
RA   Wibberg Daniel;
RL   Submitted (NOV-2014) 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; LN679103; CEL59601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7FNT9; -.
DR   STRING; 1108050.A0A0B7FNT9; -.
DR   Proteomes; UP000059188; Unassembled WGS sequence.
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; 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   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
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:UP000059188}.
FT   DOMAIN          5..137
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          166..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         316..320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         357..364
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         479..481
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            390
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            466
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            489
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   649 AA;  73708 MW;  5584F1B8AFA421DA CRC64;
     MTPRPRVLHW FRTDLRVHDA PALQAGLALK PEVWYPVWCW DPEYVYSHRV GVNRFNFLIE
     SMNDLSQSLT RINDKSKLLV VRGSPYTVLP KLFRDWKITH LVYELDTGGY AQERDKRVQE
     IATQNKVQVV DVLGHSLYHP AEVIEKNGGK PTTTITQWQK AASKLGSVPR PTAAPKKLIP
     PGDLHLGSLS REDHPVNREH DLNEKTRISP VTCFDTLTGP KGDFAVPTLE ELGYPNPTTT
     IRGGEKEGRA RLFAFNKDDN GNRAALFEKP KTSPTIPGPF KASRTNNGHE DTLQEDGDEF
     EDLPEGAQID VTKPSTTLMS PYLKFGCVGV RECYWSWHDI LVNAPKSAKK PENLLGQLEF
     RDMYYAAELA VGGTAFARVQ GNPICRYIPW RCPTVYSDDT NQIIPRPKDE QHPRAEEWLA
     AWTEGRTGFP WIDALMRQLR EEGWMHHLGR HSVACFLTRG QCYISWERGA EVFDEYLIDW
     DPASNYGNWM WLSCSAFFSQ FMRVYGVATW PSKFDKTGAL VRKYIPELQN FPNQYIYEPW
     LAPKSVQKEA GCIIGKDYPS PMLDEKEEKG RNIERMKAAY QAGLYGDSPK VLDGTATIEV
     PNKPEDDDSN KAGTKRKADK SGGSKTRSTR TRKVSDDGQK SLDAYMKKK
//