ID A0A317Y0Q4_9BASI Unreviewed; 812 AA.
AC A0A317Y0Q4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=Cryptochrome {ECO:0000313|EMBL:PWZ03131.1};
GN ORFNames=BCV70DRAFT_12038 {ECO:0000313|EMBL:PWZ03131.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWZ03131.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWZ03131.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWZ03131.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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; KZ819188; PWZ03131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317Y0Q4; -.
DR STRING; 1882483.A0A317Y0Q4; -.
DR InParanoid; A0A317Y0Q4; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR014133; Cry_DASH.
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 NCBIfam; TIGR02765; crypto_DASH; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF22; CRYPTOCHROME DASH; 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; 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:UP000246740}.
FT DOMAIN 30..210
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 382..386
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 422..430
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 537..539
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 464
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 524
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 547
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 812 AA; 90605 MW; 9F33C43C43936592 CRC64;
MEGTASSSSA GTSQGGSGNP SRPSSDSGRS VLICLLRLDL RIHDNPLFHY AHESPKPIVS
SADKTVNLSK VEDEALLGST ADYLLPVFVF DEREMELSGL PGYQRKGPEA RTKEYGFWKT
GGFRTRFISE TVYDLRSRLR AVGSDLLIRF GIPEVVVANL VSAFQAEGTH VEGVWLQKEM
THPEIEVENH ILQKLSGTGV PVHFVHSKTM IHPADLPFES SETPDVFTPF RKKVEALGRK
MVRPVKPSPA KFKPLPPQIP STPDYALDVS YEVDVDGLAP RSLETRDKQE GQVSFHDILR
FLLTPLNDSQ LPPTLEANAL LQQRHPASAF PLRGGESSAL DRLDWYFVRG KSADSSRWGK
ADPPPVARYK QTRNNLIGHA YSTKMSPFLA YGSISPRQIW EALDQHEQKF GEDQNTYWVR
FELLWRDYFF FVAEKFGKML YELGGFEQAT DPRQAAQKME DGWWRKWDPL NDGPEHEMTR
LLEGRTGIPF IDANILELRE SGFMSNRGRQ NVASFLSKDL GYDWRIGAEF FQSHLIDYDP
TSNYGNWQYV AGVGNDPRAS RQFNTIKQAK DYDSHGEYVK MWIPALRNLH PDYVHTPWLL
TSEERRRYGL KTTAMDVTID GYPASPLYEH EGWHRHYERK QGVGSKMHGN PQEKVKDGKA
PRRHRPGPYR NHAAMYGALS DRLNTDQLSA SAGTLYHSSY EGGPSRNVIP PLRGASGSIG
PGYTSRPNAG YMNHGGNGNG YGHGPGLERT HSPFGSSGPR YSRPPPPPMG GPGAPVMPAP
VGRAPGNAFD FGPGRTGSAG SADGNNRTRR LK
//
