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Database: UniProt
Entry: A0A2H3IML7_9EURO
LinkDB: A0A2H3IML7_9EURO
Original site: A0A2H3IML7_9EURO 
ID   A0A2H3IML7_9EURO        Unreviewed;       897 AA.
AC   A0A2H3IML7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-NOV-2023, entry version 19.
DE   SubName: Full=Zinc finger, FYVE/PHD-type {ECO:0000313|EMBL:PCH05846.1};
GN   ORFNames=PENO1_020370 {ECO:0000313|EMBL:PCH05846.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH05846.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH05846.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH05846.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCH05846.1}.
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DR   EMBL; NPFK01000035; PCH05846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IML7; -.
DR   STRING; 290292.A0A2H3IML7; -.
DR   OrthoDB; 124870at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46462; UPSET, ISOFORM A; 1.
DR   PANTHER; PTHR46462:SF3; UPSET, ISOFORM A; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT   DOMAIN          272..402
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          96..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..136
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   897 AA;  98220 MW;  E7BDE54C65181F13 CRC64;
     MTDTSLLATT HSTGDSYPVT ASIHSPALNG AISDSVPLED EEPYTIKCIC AFEDDDGNTV
     FCEKCETWQH IECYYHGQEV PDVHFCTDCS PSPLYLDGKR ATERQRRLRE QNDSGDRKAK
     RSGSKSHKKK HHKEELVNGH HRSESTSRDQ LGTLKKPKSS HRPSASVSSV NVPPKLQPDP
     RKRSGSMTTS MSPTKFSSTS PQIPLYSHEF LHLYENDRGY QDIKSNLVNN IHLMNDIGSW
     VKDPSTIPPD GTGRPPQDVF TYADVLDSSE WPQLSLDTQI DKEIEMEGVH PTWKLLRTQT
     AVHKDQIVGE VTGKIGALRD YCLDPANRWP DLHHPQPFVF FHPQLPIYID CRQEGSILRY
     VRRSCRPNVT LKTYITNGIE YHFCFVANQD IPADSEVTAM WYIDRQFSGD SDQEEARAIS
     MSNLLANFGG CACSPPQPCL LAAVDRRRHP SLKQMNGKRK KAKSKSAVSP TSVGRSNTSR
     AGSEVAIEDD NADNRSTSGS VRGQTRSRDL TPTHPPPEWA LQDTELSARD RRKIAAVEKK
     FEQLEHDQHG QRKKKRGSAT SAHPNLPAPL PKQSSVPASG KSLKVDTATS RTLSRKVSDP
     TNTRSPLSRA SYVDESQQTR PPTFNFSPLG RRLMKRCLED SAKTQWPVKR QQLSAGISVA
     DVANSPSSVT HSQSWGSGVR PSSSHSEDVD MKDGPSDTAS VKSASHEVMA KPPLPSTAAH
     NTLVPGMSPL NIRMSNLHVQ LPPNHFAVPS TPGAAPPGSL QSPSDTVSQP PQTPGGSLTA
     PSPVKKKMSL GDYMGRRGTM ATPTTEKTQA QATTSALAPP NKPASQAQST TPPLSTDGES
     QPQSQSQPAQ GADTIKNEAS PTDPDITMKD VPSKPPISPP YVSSLEMQDD SKVPPTT
//
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