ID A0A453NWD6_AEGTS Unreviewed; 698 AA.
AC A0A453NWD6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET6Gv20511100.1, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET6Gv20511100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 AlphaFoldDB; A0A453NWD6; -.
DR EnsemblPlants; AET6Gv20511100.1; AET6Gv20511100.1; AET6Gv20511100.
DR Gramene; AET6Gv20511100.1; AET6Gv20511100.1; AET6Gv20511100.
DR OMA; KYFPWVV; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000015105; Chromosome 6D.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR GO; GO:0097159; F:organic cyclic compound binding; 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; IPR020978; Cryptochrome_C.
DR InterPro; IPR014134; Cryptochrome_pln.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02766; crypt_chrom_pln; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF58; OS02G0573200 PROTEIN; 1.
DR Pfam; PF12546; Cryptochrome_C; 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:UP000015105}.
FT DOMAIN 15..146
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 575..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 252..256
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 395..397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 329
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 382
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 405
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 698 AA; 79063 MW; 0E0BD4D347A07BFF CRC64;
MSASPSMSGG AGERTRTVVW FRRDLRVEDN PALAAAARTA GEVVPAYVWA PEEDGPYYPG
RVSRWWLSQS LKHLDASLRR LGATRLVTRR STDTVAALLE LVRSTGATHL FFNHLYDPLS
LVRDHRVKQV LGAEGITVQS FNSDLLYEPW EVLDDHGCPF TMFTPFWNKC LCMVDPPAPM
LPPKRINSGD LSRCCSSDDL IFEDESERGS NALLARAWSP GWQNADKAFT AFINGPLIDY
SVNRKKADSA NTSLLSPYLH FGELSVRKVF HQVRMKQLTW SNESNRDGEE GCSLFLRSIG
LREYSRYLAF NHPCSHEKPL LAHLRFFPWV VNEVYFKVWR QGRTGYPLVD AGMRELWATG
WLHDRIRVVV SSFFVKVLQL PWRWGMKYFW DTLLDADLES DALGWQYISG SLPDGRELDR
IDNPQFEGYK FDPYGEYVRR WLPELARLPT EWIHHPWDAP ESVLRAAGIE LGSNYPLPIV
ELDEAKSRLQ DALSEMWELE AASRAEIENG MEEGLGDSSD EPPIAFPQEL QHMEVDRATI
HTPATAGRRR ADQMVPSITS SLVRAETETE LSAAFESEVN RPEVPSQVHF QPQTRMEVRD
EGVSDGTAAR YNGVQQQQQY TLHRHRVQGG IAPSTSEASS SWTGREGGVV PVWSPPAASG
HSDPYAADET DISSRSYLDR HPQQSHRLMN WNQLSQSS
//
