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Database: UniProt
Entry: A0A1Y2WP23_9PEZI
LinkDB: A0A1Y2WP23_9PEZI
Original site: A0A1Y2WP23_9PEZI 
ID   A0A1Y2WP23_9PEZI        Unreviewed;       648 AA.
AC   A0A1Y2WP23;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Endonuclease/exonuclease/phosphatase domain-containing protein {ECO:0000259|Pfam:PF14529};
GN   ORFNames=K445DRAFT_15753 {ECO:0000313|EMBL:OTB11493.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB11493.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB11493.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB11493.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR   EMBL; KZ112963; OTB11493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2WP23; -.
DR   STRING; 1001832.A0A1Y2WP23; -.
DR   OrthoDB; 2621451at2759; -.
DR   Proteomes; UP000243732; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   Pfam; PF14529; Exo_endo_phos_2; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732}.
FT   DOMAIN          408..520
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF14529"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   648 AA;  72911 MW;  759ABC774BBDB7D1 CRC64;
     MVNESKKEEA NEMKEQIIGT MDKEITRRIR DATATNTKRR CAESTAMEDI RHEMKKMKEE
     LLNKMESNRT TQGTGAPLRT WADVAATPAT QWNNNVAVPG RRLREITIRG NSDSPEIANR
     TPEETVKAVN LALGRQEAIA ARRLKSGGIT VTFREGADTY KEDGKQWIKK AFGEQATGAG
     KAFTLVAKSL KAGKLRDAHA NPERLLKEVR DENKQDIESL KPVYRKDKEA KCRNCGGPHP
     AWSKECKRVQ EAKEKAKEAY IHRPRQFEER EGTGFFPAAA HATYDGFKIV APRNRSRTRG
     QPQGETQNKT PVKGRPRKSI AQWNAGQGRG ILSQAVERRS DIDIIAVQEP QFVKRSPYNP
     TNSNYNLIWG GAGRAALYIS KTMDKKKWKG EAGHNWAACR LSTDKGPITV WSVYIEPPGE
     SRHSPLGEME LRKGQGRHIV VGDFNMHHPL WDAENRTAGN PGELLELTKR WNLSLATERG
     HATRLRQGNR DSTIDLTWID ARINHGKVTE LDWQGSDHVA LTTTVHIDES TNAPEKKRGG
     WVWKDLDPIL LKAEVEKLEI PRTFMGPGEL DLYVDYLVEE LQRIADAVAP QRKAPSPRAA
     KWWNGKVTRS RKEAIQRRRS NSQEKQLEAD PSGGINRPQV ALETGKVG
//
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