ID B8M8B8_TALSN Unreviewed; 771 AA.
AC B8M8B8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 28-JUN-2023, entry version 51.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase Phr1, putative {ECO:0000313|EMBL:EED20431.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:EED20431.1};
GN ORFNames=TSTA_036560 {ECO:0000313|EMBL:EED20431.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20431.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20431.1; -; Genomic_DNA.
DR RefSeq; XP_002480865.1; XM_002480820.1.
DR AlphaFoldDB; B8M8B8; -.
DR STRING; 441959.B8M8B8; -.
DR GeneID; 8101927; -.
DR VEuPathDB; FungiDB:TSTA_036560; -.
DR eggNOG; KOG0133; Eukaryota.
DR InParanoid; B8M8B8; -.
DR OrthoDB; 124765at2759; -.
DR PhylomeDB; B8M8B8; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; 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; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF18; SI:CH1073-390K14.1; 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}; Lyase {ECO:0000313|EMBL:EED20431.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 275..412
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 528..532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 567
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 570..577
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 668..670
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 602
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 655
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 678
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 771 AA; 88571 MW; E0B1A46EA7B13713 CRC64;
MNPKRERIIP HKRGLLPLST SSSTSTSSSS LTRSKVHKAI NPSAVPAIIQ LQKPVFSSLN
ATIEKEEEHK QENKRKRYAT TLEDNNENTN KVIRIEFDSS QAPQPFLEPE LAQRIIEARR
KKRIEEESEK EDVNKDATAD LNTEREVRRR AAQRDYGRLR SSLRLRKYHY RSIPQDTQMA
PQKRKAPNGA EVSSARRNNV SQPNGQRQNN DINAPHPGAQ QAENFGIVLR EFYPPEMSNA
RCEAYNNGTL ERPVDTLNRA YAETDPIRKE IKPRNAVVHW FKGDLRLNDN RALKMASELA
AKNEIPLVCM YIMSPQDLTA HCSSPARVDF TLRNLRVLQR ELGTLDIPLY IETQERRRNI
PERIGELCEQ WGASHLFANI EYEVDELRRE AKLVRLLADK GIAFETAHDS CVVTPGALQS
QQGKQYAVYS PWYRAWMGYL HQHGDHNLRV LEPPGKNHES ARSHFGDLFD SQIPGASENR
RLSDEEKQRF EKMYPEGEQE ARKRLDEFIT TRVKEYSKKR SMVDGQYTAI LSPYLASGVL
SARTAVSKAK DANGGYLDGK NASLASWISE VAWRDFYKHV LVHWPFICMN KCFKPEFTNV
TWEYDTDLFT RWTEGQTGYP IVDAAMRQLR HDAWLHNRNR MIVSSFLSKD LMIDWRRGER
YFMETLIDGD FASNHGGWGF GSSTGVDPQP YFRIFNPLLQ SEKFDPNGDF IRKWVPELSD
IKDSKAIHDP YGRGAGAIAQ KAGYPRPIVE HAASRVRALK RYKEGIARDK P
//