ID A0A166KV56_9AGAM Unreviewed; 599 AA.
AC A0A166KV56;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645};
GN ORFNames=PENSPDRAFT_741498 {ECO:0000313|EMBL:KZV76131.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76131.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV76131.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV76131.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV424467; KZV76131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166KV56; -.
DR STRING; 1314672.A0A166KV56; -.
DR InParanoid; A0A166KV56; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000077086; 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: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}; Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT DOMAIN 86..223
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 14..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 362..366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 403
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 406..413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 504..506
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 438
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 491
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 514
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 599 AA; 67749 MW; 5BA7DC199B867D3B CRC64;
MILFRLAHRP RLLTTTMAKR ARTSSPASPS TERQGSPSKK PKSDAHFVHN KIALADAAAN
AEKDPPFKKL MEAVEHTAKS PKKGECVVYW MKMEDIRVYD NRALAAASEQ AQKDGISLVV
LFTISPQDYV AHDRSPRRID FMLRNLRDVK AKFSALNIPL AVITHSPRRT IPERIMSFVM
EVGATHLVGT IEYAVDELRR DIKICELAKD ANICVNFVHD KLIIEPGTLF TKQGKPYTVY
SPFQKQWIQV LNSDVNKHLA EAPEPAANSK AIKSDSKFGK LFESDIPDHV DGFECEDADV
MRELWPAGSD AGREMLRLFM HTKSQGSHVG LSDPLAKADE STKHSRVLAY KENRDRCDRN
TTSRLSPYLA SGVISVRDCV RATLDVLNVK KVQADSNSGV GVWVKEVAWH DFYTHILATF
PRVSMGRNFL EKYDDVQWET NQEHVDAWKA GKTGVPIVDA AMRQANTMGW MHNRGRMIAA
MYLVKDLMLD WRLGERYFMQ QFIDGDLAAN NGGWQWCAST GCDPQPYFRI MNPYLQSEKA
DPTGEYIRTF VPELSKVFGK DVHNPPAALA DKLGYPRPLV DHHKARERAI HRYKNIGEK
//
