ID A0A0D2DSD0_9EURO Unreviewed; 1759 AA.
AC A0A0D2DSD0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW45918.1};
GN ORFNames=PV06_01624 {ECO:0000313|EMBL:KIW45918.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW45918.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW45918.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW45918.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; KN847333; KIW45918.1; -; Genomic_DNA.
DR RefSeq; XP_016266134.1; XM_016402237.1.
DR STRING; 215243.A0A0D2DSD0; -.
DR GeneID; 27353698; -.
DR VEuPathDB; FungiDB:PV06_01624; -.
DR HOGENOM; CLU_000991_0_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000053342; 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); 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; 1.
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; SSF81995; beta-sandwich domain of Sec23/24; 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; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
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 140..233
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 458..507
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 599..765
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1187..1214
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 257..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1722..1740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1759 AA; 196852 MW; 2B0CA60E17F067FB CRC64;
MVAPPSTGGV APATAAAKPS PATRMNGVGP NIATPAFPYS ARHAQALDMR TVERKGDPAS
RDPPARSRQY GLLEAPTYRP TEAEFRDPME YIRSIAPSAS KFGICKIIPP DSWNPDFAVD
TERFHFRTRR QEINLVEGGN RTNLNYLDQL AKYHKQYGQH LNRFPSVDKR PLDLFKLKKA
VEIRGGFERV CKDKKWAEIG RDLGYSGKIM SSLSTSLKNS YQRWLHPYEE YLKWAKPGVQ
QQLENEQGGS YSPAMAPYQS PIPPPPPSQS APPAMSLGDP SQPHTTTANG PLHPVPPPVQ
QQPSIAPVAP APQPRPVSSS GFTAVNSGFA AVNAPSGFTA VNTLPPPIVK NEVNGTTTPP
PNHTPSFMPV NGPTLSAVPP GAHLHNGGSN PLKRTMSHDS LTGESGSEAM HGDEDGPNGR
RSKRPKKDGM PTIPGNHIPA MRPSTPQVRS KSTPRRQGDR CEKCGKSDNK ESILLCDSCD
LGYHMHCAEP PLTQAPTEWH CPKCLVGTND YGFEEGSIYS LKQFQEKANN FKDHYFAARM
PFDPVTNTQR RPNEDDVERE FWRLVEDITE QVEVEYGADI HSTTHGSGFP TIEKQPLNPY
SKDPWNLNVM PFLEDSLFRH IKGDISGMTV PWLYVGMCFS TFCWHNEDHY AYSANYQHFG
ATKTWYGIPG SHAGLFEDAM RKAVPELFET QPDLLFQLVT ILPPNQLRKA GVDVYACDQR
AGQFVITFPQ AYHAGFNHGF NFNEAVNFAP ADWEPFGEAG VRRLQEFRRQ PCFSHDELLV
TAALSDTTIK TAKWLGPALE RTRDRELLER TNFVNTHRTL CPHDDCAFDS LAPEPPEACG
LTVKIDSSDL EEDEYQCCYC KAFSYLSQFR CHRSGKVSCL LHPLRADCCD DSDEERMKGP
NHSLVLRFTN QELSNIVQKV VDKAHVPEMW EAKLEALLSE EARPPLKAMH TLLSEGEKIP
APLNGLDDLS EFVRRCDQWV DEANLYLTRK QQNRRKNEKA WRRSSLRTGK GDEKDNEPQL
TLDRMKELID DGEQLGFSTP QLEGLQEKVT VIDAWRANAK RILSGINPAR LEELESLLEE
GRGFSAAMPE LTSLEKIYAR TQWLEESRQL QNDITSKSLD ECRSLLERIT ELDILPQAPE
ATFVNEMVKQ GEFWEHKAKE LMAAQDVHYP QLESLHSQVH LQMFPVNKEV LDKMDQILAK
NREAKRQIIT LVERSHDPDL RKRPLYAHVR DVVKGFEDLN GKPHGAAELE KELRRHEDWM
RRGKKLFGKA NAPLHILEQH MKFVEEKNSF CFDLNDTFRP PVEPASREAS PTDDRGRGQL
GEDEKPVFCI CRQPEAGLMI ECEICHDWYH AKCLKLARGK VKECEMFTCP ICDWRVKIPR
DAARPKLEDL QGWQDEIADL PFQPEEEELL KRIIDKAQAF REFLSQYTNG NALCRTIEEM
PEMLFYLRKI EGAEVLLAYE TNLFRQELHK WQPIAPEPPP ILDQSLSTRK PRPTKQQKLM
KELGVEKPED LPPHLRTKSY VRRKTQESFM TGPLLPKPST QSPSAPGSAA SPSQSQSAGN
AETPGPGQRQ GSAGAAGAGG TIEPGYIAGS ASYGNAFGND RPESFPPNSP SPMFSPTREQ
PAQGMKDPMM PAFAGGTSSS TARNHDPSFP MFQPNTGLDA DDDLRNGLAN ASPGGTQPGR
EGTPPGGEYD NIFMDITNQD GDGSNDTVPS LEHETSHASE ALDMIRTASN DSANNNAELE
DGDNVSKHFD DFLTGDEQH
//
