ID A0A2B7YEA3_9EURO Unreviewed; 1733 AA.
AC A0A2B7YEA3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=PHD finger and BAH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ80_04183 {ECO:0000313|EMBL:PGH19212.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH19212.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH19212.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH19212.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH19212.1}.
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DR EMBL; PDNA01000051; PGH19212.1; -; Genomic_DNA.
DR STRING; 1447883.A0A2B7YEA3; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000224634; 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 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; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
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:UP000224634};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 257..375
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 554..728
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 740..784
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 1008..1058
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1116..1235
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1733 AA; 188418 MW; B1F9F2FF4EAC3EFA CRC64;
MSSSQAIAAA ADGNHPTPGK TSENSPLAST QNTPSQDKAI ASITLKGVAS ANGTPSQSMT
ATTTSSSTSS PVPAAQTSTA SPAVPPVYGT RSRNRGGAPR PNYAEDPDID GDLELVSTST
RGGASKKASP HANTATASPS AENDKASGVS TRRSQTNTNN SNTPGSTKDA IPGTSSFSAN
PNGAGTTTAS KKRKQPGSSN TVASSSTTTH SSTSTKKFVA PANLPPGSQG ANGRSMMTFI
NCRGYLKNGK LKADDGTTLS ANDHVYLVCE PPGEPYYLAR IMEFLPSKNN PTGPIESIRV
NWYYRSRDLH RKTVDMRVVF ASMHSDTCPL TSLRGKCQIL HQSEVKDMDE FRKSRDCFWF
DKMYDRYIQR YYDVIPTSLI INVPEHVKKV LRERWRYVLV EVGRRKELLS DVKTCKKCCL
YAANVDSVDC AVCHSTYHMD CVRPKLLKKP ARGFAWACAP CSRAQERKLE ARNTPIVGEI
PPEAESEIVE EEEEDPTAAA DVTRRSTPAA NEHVPKPATA EQIAQAKLWP FRYLGIHCRV
EDALDYDDRI YPRASSRLGT RHQANVLPWY GHPVRYVKAP STKKKYLKSG SKKDLKLSKE
TLAAIEAERA ERAQRPKWVM DEPTGYISRG KDEPVTVGAK QIRTLEPQFI MPDASQLPVR
GEDDAPGASL TDADREKFID DYMTQAKEVA TSKGIEKYST NFLDKALKIL YDESFNVETA
LAKLKQVNRY ADLKEPHLRA DEVKLFESGV AKYGSELRLI TKHVGTVPHR HIVRYYYMWK
KTPKGRQIWG NFEGRRGKKA AKKTDNMAKL VDDVADDHDD SAFDAEKAIE KKRGFTCKFC
STRSSRQWRR APATAPGTTV PAESSSKRDK GAALSVALCQ RCAVLWRKYG LQWEDVDEVA
KKVAQGGHKS SRRRYEEELL IQLLMSSESE IRLSNATATT ATAIGIPVTA EATPQPPPEP
PKKKAKASDR DSSAATSQAP VEPPPKKKVV EKPPEPPALV PEPPRAKTLP CAVCNKMEPM
GDQHLSCRDC RLTVHRGCYG VSPSRSFTKW YCDMCANDRN PMISTNYECI LCPVTWTEHE
LMEPPKITHK KKTDREREKE RLEKEMVTEA IKLYRQRQEA VGKPIGPREP LKRTAGNNWV
HVTCAIWNPE IKFGNAKELE PAEGFGLVPQ DRFQATCKIC KTKKGACVSC QNPSCNAKFH
VECAHQNGYI FGFDVTPVKS SRRDTVNTMK LGEEAGAVTP GIWCFNHDVT TVVHEMSEPS
EVEGLNALQL YAQTTKQADL TLTGTVRKAA HVQQSVGASI QNGLVPTNRR ISLINGSTSQ
QQKDNSPRGS LSPKTDGTKA LPDADDRGTS TLEGSGNKKC SRCQSSCSPK WWRIESSVEG
PATGGAGHKL INGVGSKEPG DPSGPPLHTP PLRAANPATI ATNGDVPMTD IDRSTSLGRD
SAKSQPSPRV TYECHKCHFR KQSASLPVSD VRPSPSSVPR DPSLPAPRAP EFAPRPFVAS
PHGHPPQLPM PPIVPVHSHG PSDWRPEYDQ RPAEYGAPLM RPSLSSGGHP PNGIPLVPPS
FHPGPPPPSH MNGYHPSIQP AYPNGAPPPP PPHSYPAHHS PYAPVSLPLP GGHPPPPPPP
ARPYSTAGSP PVHFSTPSTM SGMPPGPPRM YSVERSMAPN LASPSSTHRS LEPQRPSTPA
TTEGHGGRQL GGVGPPGTGP NNSERYSGAN GTGPGASAAS GASASPSLKN LLS
//
