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Database: UniProt
Entry: B8M8B8_TALSN
LinkDB: B8M8B8_TALSN
Original site: B8M8B8_TALSN 
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
//
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