ID A0A395NXF5_TRIAR Unreviewed; 626 AA.
AC A0A395NXF5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Cryptochrome {ECO:0000313|EMBL:RFU80790.1};
GN ORFNames=TARUN_1447 {ECO:0000313|EMBL:RFU80790.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU80790.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU80790.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU80790.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU80790.1}.
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DR EMBL; PXOA01000093; RFU80790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NXF5; -.
DR STRING; 490622.A0A395NXF5; -.
DR Proteomes; UP000266272; 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:UP000266272}.
FT DOMAIN 4..136
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 576..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..596
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 276..280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 350
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 425
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 448
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 626 AA; 71037 MW; C5A6AE811A3B5FD4 CRC64;
MAKPRVIYWF RTDLRLHDSP ALQAALDLEP EVLWPIFTWD PHYVYKSRVG VNRWQFLLDC
QNDLSQSITK LNKKSKLFVL REGPQTLFPK LFKAWKPTHL VFEKDTDAYG RFRDEAITKA
AKAAGVQVII QPGRTLWDSD DIVKQHGGKP TMSITQLQAA GKKQGPVAKP IPAPESLPDP
GDMPVDFEQD PPETKPDFNA NYRSEKDTGY KDIAGPHGDF AIETLEELGF PPATTPHRGG
ETIALQALDK LIKNADYTAT FQKPKTSPAQ FSPQSTTLLS PFFHFGALSV RLFYWRVHQV
VSSYGKGASS PPESLIGQVL FRDMYFAAQA ALGQSFSQTA TNPCCRFIPW HLPSKRDPKT
GFTTGEYHID KEEPEVWFQR WKYGVTGFPW IDALMRQLKE EGWIHHLGRH SVACFLTRGG
CYVDWERGAE VFEEWLIDHE PACNIGNWQW LACVAFFTQY YRCYSPVSFG QKWDKNGDLI
RRWIPELKKV SAKYIYEPWK MPLPDQKEAG VRVTGDGLSD PQKGTYPKPM FDFSERRGIC
MSAMKKAYAV GLYGNDEKVL DGSWRSLFPS PDEAEVMGEY ESDFGENADN GDDGSQEEAN
NETSRNKRGA KSNGAESKPK KQKIEL
//
