ID W2SE12_9EURO Unreviewed; 1734 AA.
AC W2SE12;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=PHD finger protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_00472 {ECO:0000313|EMBL:ETN46288.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN46288.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN46288.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN46288.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB822711; ETN46288.1; -; Genomic_DNA.
DR RefSeq; XP_008711000.1; XM_008712778.1.
DR STRING; 1220924.W2SE12; -.
DR GeneID; 19967811; -.
DR VEuPathDB; FungiDB:HMPREF1541_00472; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_001514_0_0_1; -.
DR InParanoid; W2SE12; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR029617; Snt2.
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; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 231..349
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 386..438
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 526..697
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 708..753
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 1083..1203
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1514
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1563
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1734 AA; 190834 MW; BD4BC9B36E5E8D1F CRC64;
MSTADADPIH SVDSDAPPPL PPTSRPLDLL PPRTNSHHAQ PAPTPDPAGP EDLPQSQPMT
TTHSASSQNP DTDNVDINAA GPYGTRSRNR GPRINYADDK ELDMEIEAAG RIGKGASRKA
AAVAAASTPT GSGTNVSNGF STINSVSIPN GELAAQNNTV NPNHAPAPAP SKKRKQPGGS
ATASGTTTPF APGSRHQPAQ SAHYVASNMM SFTKSGGRLN SKKQLVADDG TTLEADDHTY
LVCEPPGEAY YLARIMEFLH VNNDPTAPID AVRVNWYYRP KDIGRRVQET RLVFASMHSD
TCPLASLRGK CHIEHIASID SLETYRKQKD CFWFDKLYDR YMQRYYEVVP TSRVVNVPQR
VKDVLDERWK FVLIEVGRSR DLTSASKRCI RCEQFAANHD SVDCAVCKNT YHMRCVRPPL
LKKPARGFAW ACAACSRKQE LRLEARNTPT ASESAQTPDD EAMDEDEDDN IRLAADTRDS
SAAPEEHPPP TAAQIAQANL WPWRYLGVHS RVEDALDYDD RIYPRASSRL GPRHQANVNV
WHGRPVQLVK PAEIKKKYQK HTTSKKDGKL SKDTLAQMEA EKDSRQKRPK WVLDEPVGYV
ARGEDEMVEI RGKKEYTAQL TFKMPDPSKF TERGLDEPAK AVDGEKLVDD YITQVKKLAG
QYDIEETSVD LLTKAVEKLQ ANDYDAEKAL AAMRSLSKRS DLKLPDLNRE EVKRFEEGVQ
KYGSELHLVA RHVGTVKESR VVRFYYMWKK SERGRQIWGN YEGRRSKKES RRADKSDGKI
DDVADDADDS AYDNDKAAAK KRGFECKFCM TRQSRIWRRA PGTSPGTLVP GDSAAKNSKD
KSGWLVLALC GKCAYLWRRY AIQYENIEEI SRKIAAAGGR AAKRKIDEEL LQIHYEAHFE
AGDPISLHTA NEVHKAGVEV PQNLVQHEEP PKKKAKADKD VSAAATPEII PEKKKPAEKI
PEAPLEPEAP RVKIHPCAVC HVIEVPGQRL LKCRDCRLHV HGACYGVAPN VSTVPWFCDM
CRNDHNLQVS TIYECLLCPV THTPQELMEP LKVSHKKKTD REREKERMEK EMVQEASRRW
RQEQESAGRP VNPREALKRT AWNNWVHIVC ALWTPEMKFA DADLLDAAEG VGFIPPESYE
NVCKVCKTAG TKPTHQCHLP GCTATFHIGC AHQSGYIFGF DVTPVKSSRR DAVSLIKFAS
ETGVAVPGIW CPNHAPPTYV HSMVELTEGD VTALQVYARA YKQADNSITG TVRRAKQFAA
NAPIPASAVQ QPQRQATITN GVASGSGQPD RSIPRARTSR SLSPTAAEDG MELEAGDAAE
QKGSVNKLST RKECCTCRIK ATPKWWPVRL DSAQDERSSS PTRDAEDRYR LNGIDTTSHR
DDTFMTNGIV KKEPRDQSGI SGALPADRTM WQCHRCHVRK IAPPSSPSQV RRSEPTPSEP
VQEPPAPEPQ PYVQPPGYNY TPRPPPADAA PPPHSHPPGP PAVAQHAPWP PTPTQWGDPI
LRNNPPPPSV VYGPAPPRSD GQQPSSLWGG HRDGPYGVPP PPPPPSSSGP PQHSPPPAGP
YSFPHQHGSP AHGGPPPPMP ALARPRSPPR ASYDYSRTGL GIGGPSHLGR PFPEHSPSHV
NGYGSSQGSW GPAPPQPGLA PPPRPPSIHG QPLTQMAQAA EQINSSQHMR SMSNEGATRL
GQPVNPVGGF PSPHMMGGAQ PRPITPADAR AEEMRAERDR PGASASPSVR NLLS
//
