ID S7ZVS2_PENO1 Unreviewed; 1693 AA.
AC S7ZVS2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS34534.1};
GN ORFNames=PDE_09498 {ECO:0000313|EMBL:EPS34534.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34534.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS34534.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; KB644415; EPS34534.1; -; Genomic_DNA.
DR STRING; 933388.S7ZVS2; -.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_0_0_1; -.
DR OrthoDB; 48111at2759; -.
DR PhylomeDB; S7ZVS2; -.
DR Proteomes; UP000019376; 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:UP000019376};
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 75..116
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 145..238
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 443..493
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 585..751
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1309..1358
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1693 AA; 189681 MW; CDAB4F864E531806 CRC64;
MVAPASTGPT SMAAQPSMGR QSTRSASTHP SHSHNVPLSA RRSAPLDLAT VERRGQTNSP
REPSKRVRPH GLPEAPTFRP TEEEFKDPVA YIQKIAPEGR KYGICRVIPP ENWQPPFAID
TEAPPKQRFH FKTRRQELNS VEGGNRANMN YIDGLAMFHK QHGTNYSRLP SVDKRPLDLY
KLKKAVEVRG GFESVCKTKK WAEIGRDLGY SGKIMSSLST SLKNSYQRYL QPYEEYLARA
KPGVQHQLEL EHGGPYTPSP RQSPMTKKPG AEENGTPSKA GYGTPTMSAG LPAGNSYSRP
TDKPASSVEP TPPPPPRPAP SGFTPVNAGA GGFTAVNHSP AFTPVNQGPL IKHEGENGAS
TPKSVSEHSS NFTPVPNGHP APASKRAISH DENSSQAENG DDGGSGRRSK RLKKDMPPTV
AGSHMSLLRP APPKGRNGTQ KIGDKCESCG KSDNRSAILV CDSCELGYHT TCLDPSTTSS
SDHDWHCPKC LVGTGEFGFE DGGVYSLKQF QEKANEFKKR YFASKMPFDP VLNTHRRETE
DDVEAEFWKL VVDLHETVEV EYGADIHSTT HGSGFPTIER NPLDQYSSDP WNLNVLPFYG
DSLFRHIKSD ISGMTVPWVY VGMCFSTFCW HNEDHYAYSA NYQHFGATKT WYGIPGADAE
AFENAMREAI PELFEGQPDL LFQLVTLMPP DKLRKAGVNV YAVDQRAGQF VLTFPQAYHA
GFNHGFNFNE AVNFAPADWE PFGAAGVERL QTFRRHPCFS HDELLFTAAA RDTSITTAKW
LAPALERTIN RELHDRASFL SRHKDIAPHS CSLGGNPPKS GCQLELVVEE EDVPEDDYQC
QHCKAYTYLS QFRCHKSGKT LCLLHADAFD CCGESLSQKL LGSGHSLRYR MSDDSLKSAA
QKVYERARIP EMWQEKLDKT LEDEPKPQLK ALHNLLSEGE KIPYHLPGLQ DLAAFVQRCD
KWVEEANNYI TRKQQNRRKN EKAWRKPGSK AAQLDDRDRE VRRVENIYAL LAEADKLSFD
CPQMAALEEK TREIEKFRQD LNVALINPHT RSAQEIEELV EAGRNFNVEI PEVEHLERIH
QQMKWSDEAA RKRQLYLTLQ ECQDLVASGE QLGLKDNNEQ LLHFKEMARL GQAWEAKAKE
LMAVEAVHYQ QLEALSAQAS RFPVSRETLA AVDAILIKQR EAQKRIQTLY ERSQDPDFKN
RPRYKEVREL TESLEQLNSR PIGAIDLERE QKRHEDWMRK GKKLFGKANA PLHILKSHME
YVEKRNSYCF DLEDSYRPPV EPSSRDNTPD GLLENPASSM WGPKSRKRDV FCICRHSEAG
MMIECEVCHE WYHGKCLKIA RGKVKEFDKY TCPICDWRQK IPRDAARPKL EDLLDWQAEM
ANLPFQPDEE EVLDRIINQA TAFRDFLQSF TNAACTTTEE VPTLIFYLRK IEGAEVLLAY
ETNFFRQEIH KWAPVAPEAP PILEQSLSTR KPRPTKQQKI MAQLGVERPE DLPEHLRTKQ
IAANKRKSID AQTPRPTSLH SATSPSSSGM PATTGPMLTP MPDANGASYP FSANFSLTAS
ESLPAFAPTT TSAFLPGAAA SQSPSFLPRS PSPERGMEPL FSPPRFGRDA QFASSSPRQN
LDDVFADLTN QEEVEPETED MENLHANEAL EALNASNGSS RAPSPTDDIS APKEVQVNGA
SRAESAENVG PEL
//