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Database: UniProt
Entry: E6ZVN9_SPORE
LinkDB: E6ZVN9_SPORE
Original site: E6ZVN9_SPORE 
ID   E6ZVN9_SPORE            Unreviewed;       651 AA.
AC   E6ZVN9;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Related to deoxyribodipyrimidine photo-lyase PHR {ECO:0000313|EMBL:CBQ71357.1};
GN   ORFNames=sr16705 {ECO:0000313|EMBL:CBQ71357.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71357.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ71357.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
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; FQ311443; CBQ71357.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZVN9; -.
DR   EnsemblFungi; CBQ71357; CBQ71357; sr16705.
DR   VEuPathDB; FungiDB:sr16705; -.
DR   eggNOG; KOG0133; Eukaryota.
DR   HOGENOM; CLU_010348_2_1_1; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000008867; Chromosome 21.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 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}; Lyase {ECO:0000313|EMBL:CBQ71357.1}.
FT   DOMAIN          120..263
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         399
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         411..415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         451
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         454..461
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         552..554
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            486
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            539
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            562
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   651 AA;  72655 MW;  633A3981F50246AC CRC64;
     MAASKRKDVS PKPEDHDEDE KALDPKLAEH PDEDEAETSK PPTKRKQTKG DRSAVINGGA
     KADKQYGASA YAKSGDGWHR SDFNPSPCGR TDSQTPLDDL EAALKAHAPN KANDEGDGKN
     VLYWMRMHDL RVHDNRALAH ASALAAARRA KGKGGNLIAL FVITPADYSA HDRGARRIDF
     VLRTLASLKT QFDELDIPFV VYTHSGARTK VGEKVFDLCA KYSVSQLTAN IEYEVDELWR
     DIGMLKAASA QNVAFSLFHD CYVVPPGRVR TNDGRPYSVF SPWNRRWTDC IAKDLSLIEA
     SPDPEPNPKS IHKDSALSAL FDLSSLGAGY GIPTELPGFE CKDRAYMAKL WPVDGDAPQQ
     VLDNFMAGKG GETALDRPAN EPSTAHVGGN AKDSRLGRYA EGRNLMDENG TSRISPYLAA
     GLVSARECLR RTKALTKNRL TVGRDSGAAM WNTEISFRDF YGHVLAAWPK VCMGHAFITK
     YEDVVWETDP KTLQAWKEGR TGYPIVDAAQ RQCIQQGYIH NRGRMISAMF LTKHLLHDWR
     EGERHFSLNF IDQDFASNNG GWQWSASTGT DPQPYFRIFN LLSQSEKSDP QGDYIRHFVP
     ELKNVKGKAI HDPFHRLSKP EFDKLGYPKP IVEHAEARQR ALRRYKSPGD K
//
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