ID A0A139IDS4_9PEZI Unreviewed; 1867 AA.
AC A0A139IDS4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=PLU-1-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_10464 {ECO:0000313|EMBL:KXT12888.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12888.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT12888.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12888.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT12888.1}.
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DR EMBL; LFZO01000136; KXT12888.1; -; Genomic_DNA.
DR STRING; 113226.A0A139IDS4; -.
DR Proteomes; UP000073492; 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 CDD; cd15543; PHD_RSF1; 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); 1.
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:UP000073492};
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 104..145
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 169..262
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 473..523
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 616..782
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1340..1389
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1867 AA; 209525 MW; 5E40005AC16CCDB0 CRC64;
MVVPPSTGGG PATAVLQMQH FPPPSPTPGP PSDAQSAKSI KAKQVAPSSA PGTLHGPPSG
NNHAIPLSAR RAEPLDLSTV ERRGQPSMRP ERPRKSRVFD IPNAPIYRPT DEEFRDPMEY
MRKIAPEGSK YGIVKVVPPH TWNPTFAINT ERFHFRTRRQ ELNSVEGGNR VNNDYLDQLA
KFHKQNGHNL NRFPSVDKRP LDLYRLKKTV ERKGGFDQVC KGKRWAEVGR DLGYSGKIMS
SLSTSLKNSY QKWLLPYEDY LRMAKPGVQQ HLEMMNGGPY TPSPGPSPAK KPFGASPQEH
APTMQASAAL HATMNGHSPQ PPQLTPFQQE TPQHTPQPQV PPPSTGGFTP VNAGGFTPVN
AHPPPPQPAP TPSFTSVNGM NGLPPSNNGT PLRSVEGTPS SMGSQFIAPH PNGVAALKRQ
HSELTPEEVE LMNRRSKRLR KDVPTVVGSN MHHSRMSAGR YREARDRGNY KPGEVCENCL
RPDEPHKWLK CESCDNVYHM YCLEPPLKQP PDHEWHCPRC LVGTNEYGFE EGDVYSLSGF
QRKANEFKNH HFSTVPRQYS PFNEQKHHLE EEDVEREFWR LVEDMSDSTE VEYGADIHST
THGSGFPTIE KHPRDPYSTD PWNLNIMPLD KESLFRHIKS DVSGMTVPWL YVGMIFSTFC
WHNEDHYTYS ANYQHFGETK TWYGIPGEDS YKFEDAMKQE VPELFETQPD LLFQLVTLAK
PEKLRKAGVR VYAIDQHAGE FVITFPRAYH AGFNHGFNFN EAVNFAPHDW EPFGDEGVKR
LRDYRKQPCF SHDEMLLTAA SRDHSIKTAK WLAPALERMR EDEIATRQHF ISPPEAEPDN
QAQIPYNGPR YKQEAQLIDP STEDEEVICT FCKAYCYLSR FVCKKTNKVL CLLHAGSYEC
CDAMDFERYS GQNGEHVLYH RMTDDVLALT VQKVVDKANI PEAWAAKVDK ELEDTARPNL
KHLRTLLAEG EKIQYDLPQL ADLRRFVERC NEWVEEATSY ITRKQVNRRK SEKPWRKGTK
AAELEERDKE LRKISNIYNL LSTAEQIGFD CQEIATLRER AQKIEEFQKD ANAALSNIHA
KATSDFEELL DRGKEFHVDM PEMENLEKVL KRLRWNDEAK AKRPNTETNK QEQTLSDIER
FIASGAEIGV PDTNPDMEFF RAHKAQGELW EQKTQELMAV DQIHYQQLDA LSKQASTLPV
TPETLAKVDA ILKKQREIQD KIASLVERSK DPEFRNRPQY REMKEVMDAL DELQSKPTGT
IDLEKESKRH EDWMRRGKKL FGKANAPLHI LHQHMQAVDN RNRSCFDLED KPRGPIEPSS
RAGTPEDGVV HTEGSSSSRD VFCICRKPEA GMMIECELCH EWYHGKCLKI ARGKVKEDDK
YTCPICDWRV KIPRDAARPK LEDLQTWQDE LETLPFQPEE EKTLASLCEY GQAFREFIKP
YVEPAMEPTT EEVGVLRFYL RKIEGADLLL APETNYLRQH LHRLAKVAPE PPPIMDVSQS
TRKPRPTKQQ KLMAQLGITN PDDLPTQYKL KPHIAKRKAS EVYGVGDKPL QPAGSSASPG
GSMTPGLPPG SSSSHQPYPS GMTPTPAEPR KKHLTALSLQ VLGPLAGEPI VDDFLAQEPH
ANRDRLLKVR AVLELARDTN DTSFTTDLET FKAKVNSLPT PAAHTPGLGY ETPQERMSMV
TSGYRDPSLF ATAPSNPYPI TSQASRLGSP ANFSRGYGTQ GHSPPPPGFG PHVFGDTSPD
NMFQTPSATR PEAHSGIPSG MPAGMFDSPK QPDVTSAGHA GFTTSAGLNS PGFGGSQQSA
GGAMDSVFAE LVHQEDDGIP GLDGANDVRE SKELVPSSTS GAEKADIDMS DAPTTAGDAL
KAEAQQT
//
