ID A0A4S3JKZ2_9EURO Unreviewed; 1688 AA.
AC A0A4S3JKZ2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=PHD type zinc finger protein with BAH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EYZ11_004270 {ECO:0000313|EMBL:THC96236.1};
OS Aspergillus tanneri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1220188 {ECO:0000313|EMBL:THC96236.1, ECO:0000313|Proteomes:UP000308092};
RN [1] {ECO:0000313|EMBL:THC96236.1, ECO:0000313|Proteomes:UP000308092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH1004 {ECO:0000313|EMBL:THC96236.1,
RC ECO:0000313|Proteomes:UP000308092};
RA Mounaud S., Singh I., Joardar V., Pakala S., Pakala S., Venepally P.,
RA Hoover J., Nierman W., Chung J., Losada L.;
RT "The genome sequence of a newly discovered highly antifungal drug resistant
RT Aspergillus species, Aspergillus tanneri NIH 1004.";
RL Submitted (MAR-2019) 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:THC96236.1}.
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DR EMBL; SOSA01000122; THC96236.1; -; Genomic_DNA.
DR STRING; 1220188.A0A4S3JKZ2; -.
DR VEuPathDB; FungiDB:EYZ11_004270; -.
DR Proteomes; UP000308092; 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; cd04710; BAH_fungalPHD; 1.
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); 2.
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; IPR002219; PE/DAG-bd.
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; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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; PS50081; ZF_DAG_PE_2; 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:UP000308092};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 251..369
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 518..693
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 706..749
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 972..1022
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 975..1011
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1080..1196
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1688 AA; 185128 MW; F3202DA71BB2BC40 CRC64;
MASDRSPPQK SQQHVRADSP SSSAVTAVSQ RRMPTPTQPS RTGSPTPQGA ATVNDPQSQP
MTASASPSEA AGTEPPSTST TPAPYGTRSR GRNAAPRPNY AEDRDIDMDL EIAQPAHKLG
KRTSGVTPNS ISATNGSKHE SEKPSSSSSS AKKNQTAVNG SSSLVSAAKD AIPGTSSFSA
KLDEANGPFN SRKRKQPASS TNSNFTNGNS TKKVFTTAPS SSQAQSDSNM VSFENCGAYL
ENGKLKADDG TTFGIDDHVY LICEPPGEPY YLARIMEFIP SKNVPSGPIE ALRVNWYYRP
RDIQRKVADT RLVFASMHSD TCPLTSLRGK CQITHLSEIE DFDEYRKTRD CFWYDKMFDR
YIHRYYEVIP TKKVINVPAN VKKVLDGRWR YVLVEIGKRK ELTSAVKTFL TKKPARGFAW
ACAACSRAQE RKLEARNTPI LGDSQPEAEE EIVEEEEEEP NVANGTAGST PIPAEEEAVR
PATEEQVAQA RMWPYRYLGI HCRVEDALDY DDRIYPRASS RLGPRHQAIV NPWHGHPVEY
VKPTDIKKKY LKSSGGRKDS KLSKEAHAAI EAAKQERANR PKWVMDEPVG YVPRGEDEPV
NVNGKQVRTA EISFKMPTVG QLSSRGEDDI PGADLSPTGR EKFIDEYMTR AKEMAPSLGV
ETYSTNFLDK ALGLLYSNSF DTETALAKLK QMNKYKDLKE PHLRPEEVKL FEQGVSKYGS
ELRNVTKHVG TVPHYQIVRF YYMWKKTDRG RQIWGVFEGR RGKREARRSS SSKLVDDVAD
DHDDSAYDND KAVEKKRGFQ CKFCSTRTSR QWRRAPGIPP GTTTPNEPSS RQRDKGLQLT
VALCLRCALL WRKYGIQWES VDEVAKKIAQ SGNKSWRRRV DEELLTQLLV STETPISINP
ATAATAAAIG VPVNANPQVQ QESTKKKGRV NEKDSAATST ATSVEPAPKK KAATEKVPEP
PPIVPDPPKA KTLPCAICNK MEPAGNQHLS CRDCRLTVHR SCYGISPSRN CVKWLCDMCS
NDRNPMISTC YECILCPVTW TEHELMEAPR STHKKKSERD REKERLEKEM VNEAIKLYRQ
RQEAVGKPVG PREPLKRTAG NNWVHVTCAV WTPEIKFGNA KELEPAEAFG LIPMDRHREV
CKVCNSTNGA CVPCQFNGCN AQFHVGCALQ ANYLFGFSVT PIKGSKKDTV NSIKLGNETG
VATAGIWCAH HTVPSVVHEI NEPTEEEGVN ALTRFVETYK QADLSLTGTV RRAAYVQQSI
GASHHGGSVV SRRSACANGV LASQSVPIKD SQKNATVSRE EAPDEMEVDS ESHRPAQIIG
ADLTKKCVRC ATAYSPRWWP IDKSRRATIV DHRAPLLNGV GLNESAGSRY PNTASASPPY
LHRHPSQPPL PKVNGEYGPA DWSGPASSID GPGGPQSQTL YECHKCHLKK IAAQPSPEPR
PSPYSAQRPV LPAPRLPEYH SHPYGPHAHP PQPQSGVLPR PIGAAHSGPE WYPGYEQRTS
DYGDSKIRNN IPIPSYRGGP APPPAHHMNG YQPSSSHHPP PHYTGGAHPP HPPPQSYPAH
QSPYGPVSMP SPHPSHTAGP RAYAPSASPP DVQATIVGHS PPHSLSALNG GPPPRVYSVD
RVLKAPTQSP PISQAHVDPR GPTPAKLEET PVLATPAPTS SNRPTSTMNG TSGGSGASAS
PSLKNLLS
//
