ID A0A1V6QTS2_9EURO Unreviewed; 1714 AA.
AC A0A1V6QTS2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD92615.1};
GN ORFNames=PENSOL_c039G03619 {ECO:0000313|EMBL:OQD92615.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD92615.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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:OQD92615.1}.
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DR EMBL; MDYO01000039; OQD92615.1; -; Genomic_DNA.
DR STRING; 60172.A0A1V6QTS2; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16100; ARID; 1.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF133; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 71..112
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 136..229
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 453..503
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 595..761
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1321..1370
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1714 AA; 192346 MW; C7A531750989A840 CRC64;
MGAPASAGAT STAAAAQPTR SSSTHPSHSH NVPLSARRST PLDLSTVERR GQPNNPREPS
KRIRPHGIPE APTFRPTEEE FKDPVAYIQK IAPEGRKYGI CRVVPPEGWQ PTFAIDTERF
HFKTRRQELN SVEGGNRANM NYVDGLAMFH KQHGTNYSRL PSVDKRPLDL YKLKKAVESR
GGFESVCKTK KWAEIGRDLG YSGKIMSSLS TSLKNSYQRY LQPYEEYLAR AKPGVQQQLE
LEHGGPYTPS PLQSPMTHKP MFDENGTPSK VRDETPSLPR MAASHTPMAY TPVAHTPMAH
TPMEKSPEKP TPPVEPTPPP PSRPAAAGFT PVNSGLGGFT AVNHSPFTPG SNTPANNGPP
IKREGENGAS TPKVVSEHAS VSTPINSQDE ESLKRAISRE DSSQCENGDD DDGSGRRSKR
LKKDSFPTIA GSHMSLLRPA PVRSRKDGSQ PAGEKCETCG KSDDQGSILV CDGCELGYHK
ACLDPSTTTP SEHDWHCPKC LVGTGEFGFE DGGVYSLKQF QEKANEFKKK YFAAKMPFDP
VLNTHRRETE DDVEAEFWKL VVDLHETVEV EYGADIHSTT HGSGFPTIER NPLDPFSSDP
WNLNVLPFYG DSLFRYIKSD ISGMTVPWVY VGMCFSTFCW HNEDHYAYSA NYQHFGATKT
WYGIPGADAE AFEAAMRDAV PELFEGQPDL LFQLVTLMPP DKLRKAGVNV YAVDQRAGQF
VLTFPQAYHA GFNHGFNFNE AVNFAPTDWE PYGAAGVERL QNFRRHPCFS HDELLLTAAA
RDTSIATAKW LAPALARTCT RELGERAAFL YRQKEVSART PGFGPDSMTD DAQPKFVVEN
EDLPEDDYQC QHCKAYAYLT QFRCHKSGKT VCLSHVDTYD CCGETFAQKL CGSGHTLRYR
MSDDELQALV QKVQERARIP EAWSEKLDKT LEDEPKPQLK ALHNLLNEGE KIPYHLPGLQ
DLAAFVQRCD KWVEEANNYI TRKQQNRRKN EKAWRRASTK AAQLDDRDRE VRRIEHIYAL
QAEADKLSFD CPQMAALEGK TREIEKFQQD INNALMHPHT RPLQEIEELI ERGKNFNVEV
PELEHLEQVS HQIKWIEQAV RKRDQYMTLT DCRELVAGAE KLGLSDTNEH LVHFKELARH
GDAWEMKAKE LMSVEAVHYQ QLEALSAQAS RFPVSPDTLA AVDAILTKQR EAQKRIQTLY
EKSKDVEMKN RPKYKDIRDL MESLEHLTSR PIGAIDLERE QKRHEDWMRK GKKLFGKANA
PLHILRSHME YVEKRNSYCF DLEDSYRPPV EPSSRDNSPE GLLENPGNPT NMWGPKSRKR
DVFCICRHSE AGMMIECEVC HEWYHGKCLK IARGKVKEFD KYTCPICDWR QKIPRDAARP
KLEDLQDWHA EIATLPFQPE EEEVLESIIN QATAFRDFLH GFTNAACTTT EEVPTLIFYL
RKIEGAEVLL TFETNFFRQE IHKWAPVAPE PPPILEQSLS TRKPRPTKQQ KIMAQLGVNR
PEDLPEHLRP KHIGATKRKS VDAQPQPGPG QPASMQPAPP TSSSGQPPST GPTLAQMTEP
NAAPYPFSAN YSLPASDSTP AFAPTSSSAF LPHAAASQSP SFLPRSPPPQ PDLETSLFSP
PRFGHDPQFA SSSPRQNLDD VFADLTNQEI DPEADNQPME NTHANEALEA LVVSNGSSRA
ASVQDESVQN GDHGEPQDEP KLDGTNGDLE DEEL
//
