ID A0A1Q5SZQ3_9EURO Unreviewed; 1316 AA.
AC A0A1Q5SZQ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 02-APR-2025, entry version 22.
DE SubName: Full=DNA damage-responsive transcriptional repressor RPH1 {ECO:0000313|EMBL:OKO93420.1};
GN ORFNames=PENSUB_12483 {ECO:0000313|EMBL:OKO93420.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO93420.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKO93420.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO93420.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKO93420.1}.
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DR EMBL; MNBE01000725; OKO93420.1; -; Genomic_DNA.
DR STRING; 1316194.A0A1Q5SZQ3; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR CDD; cd15571; ePHD; 1.
DR FunFam; 2.60.120.650:FF:000024; Putative jumonji family transcription factor; 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; IPR055500; DUF7072.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF23258; DUF7072; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 238..401
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 481..606
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 64..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..884
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..908
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1316 AA; 146124 MW; 8E371FFF003F06D0 CRC64;
MMWMVVLMSP SSRSESLPPL DEQVKTIRVK NPIMQEFHGS HGTYTQANIE RQRTYNLPQW
KGLCEESSHQ PPARRGERRR NQERVNRPAP TPRPQASRPE GQKRRPGRPP KRGNQVKVKD
EPTDDDTEKS RPEGPPTPVS PESLPVETKS EDLSDGESLP AAKPKGRQAK SVTARRKNNR
GETVDLVDEE AFKEFDYRIH DNEDYTAERC EELETAYWKS LMFNNPMYGA DMPGSLFDDS
TTTWNVAKLP NLLDVLGQKV PGVNTAYLYL GMWKATFAWH LEDVDLYSIN YIHFGAPKQW
YSISQEDAPK FEAAMRSIWS SDAKNCDQFL RHKTYLVSPS LLKSQYGITV NRLVHYEGEF
VITFPYGYHS GYNIGYNCAE SVNFATERWL DYGRIAKKCN CEADSVWIDV DEIERKLRGE
ATPDYYGDYD SEFEGFDGAS DMLTPPRSVP DKPSTRGRKR KNAGDGPRTK RLKLHLDGPR
KIPCLLCPNN LDYEDLLPTE GGKGHVHRRC ALFIEETTIL HDASGNEVVC DIDKIPKARL
GLKCLFCREV RGACFQCNFG KCTRAYHATC ALLAGVQVEH GAIAVIADDS QQYSLPSVDL
KCKFHRQKRP TGLLVESSDL DRRVIEAACR LVQGDLIQFQ ADKEINGAIV LENRPEERSL
LLKVLPRGDV IEMPYRWMLV VRKSNFVPLA PGIQPLPAHL ARKADSRREL EAAVPVAGSA
FGDSRSPYQW AEFETVDGAR NAFAPPVRVN LDKLEQVWHY LGTQSTESRA QYTHNPSVPV
HNPRANFLDS VKSLGVAGGF NARASKIPPH RPFHYAATAP APPYQQNLYA QHRPPLLQQN
QHLLPPTLNA VNLAPHLHSS SSSSLRPPSA AVASSSASSS LQHLAPPPPP APAAPTGAAA
AGPAMPSAFR TLPNSSIRHA PYPTVTKSHA QQQHHLTSTN TFANVRDLIA RRRLAQITEH
ANVFAGYTIV SPEMVVETLL GPMGSIPPIN GLEKLELAMA QQRVQPRAAD GTLLPPQTLN
MRADEVARLL QMLRFSLVSH RERLDVIQKK ESEGVKQEIV DQGSVAAARM PGKYAFLDQQ
RAKAPNVYQS PYNMPSGLSE YAKTTYGLVP SPDDPPKSTL ANDFFASLSQ ADKEKIMKTC
GSFVQRAIER STSHSRHSST ASNLRLSSAL AQQTENPTID ITTVDDPPLS GLDLPLHADS
PCSSFGRSHM RFPSPNDFPT HGPDPQPDHH DLFGDQQANT RFWQNGPWVA GDGNTPNEEN
RPFFGPHLFG PHERLKHDYA SSDMSLGKGP GSLHSVDMAG FGPDVADDLL TGGLSP
//
