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Database: UniProt
Entry: A0A1L9RXW0_ASPWE
LinkDB: A0A1L9RXW0_ASPWE
Original site: A0A1L9RXW0_ASPWE 
ID   A0A1L9RXW0_ASPWE        Unreviewed;      1691 AA.
AC   A0A1L9RXW0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=PHD finger and BAH domain protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPWEDRAFT_389751 {ECO:0000313|EMBL:OJJ39724.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ39724.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV878210; OJJ39724.1; -; Genomic_DNA.
DR   STRING; 1073089.A0A1L9RXW0; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_389751; -.
DR   OrthoDB; 1409291at2759; -.
DR   Proteomes; UP000184383; 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); 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; 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; PF00628; PHD; 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; 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:UP000184383};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          247..365
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          545..720
FT                   /note="ELM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51156"
FT   DOMAIN          733..776
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   DOMAIN          1006..1056
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1009..1045
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1114..1232
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          1..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          943..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1315..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1389..1691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..976
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1407..1421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1493
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1527
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1537..1589
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1590..1611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1667..1691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1691 AA;  185244 MW;  496814F8B1992FF8 CRC64;
     MSPVPSPPPK SQLNHVRPNS SASSPSQRRM PTPGHSSRPG SAGSSTPLPP TTVDEPNPQP
     MTTSASPSEV AGAEPPSSSA TPAPYGTRSR GRNAPRPNYA EDRDIDMDLE VANPGSKSSK
     RSSGVAPNNT INGSKPEGEK TTSSNTRKSL TAVNGATSTP SAKESIPGTS SFSAKPDDGN
     SSSNSSRKRK QPASTPNNSN TTNGNAAKKI FTTAPGIVQG QSETNMVTFE NSGARLKDGK
     LKADDGTTFA VNDHVYLICE PPGEPYYLAR IMEFLPSKDR PSGPIEALRV NWYYRPRDIQ
     RSVADTRLVF ASMHSDTCPL TSLRGKCEIR HQSEIEDFDD YRKTRDRFWY DKMFDRYIHR
     YYDVIPTKKV INVPANVKKV LDERWRYVLV EIGKRKELTS AVKTCKRCSL YAASTDSVDC
     AVCHHTYHMY CVRPVLTRKP ARGFAWACAA CSRAQERKLE ARNTPTMGES HHEPEEEIIE
     EEEEEPNGVG NGTGGSTPAL VEEEALRPAT EEQVAQARMW PYRYLGIHCR VEDALDYDDR
     IYPRASSRLG PRHQANILPW AGRPVEYVKP IDIKKKYMKS SGSRKDSKLG KEALAAIEAA
     KQEKANRPKW VMDEPTGYVR RGEDEPVPMG GKQVRTAELK FKMPTASQLP SRGEDDAPGA
     ELSPAEREKF IDDYMNRAKE LAPHIGVEKY STNFLDKALE LLYSESFNAD AALAKLKKAN
     KYKDLKEPHL RPEELKLFEQ GVAKYGSEWR NITKHVKTVP HYQIVRFYYM WKKTPRGRQV
     WGNFEGKRGK KEAKRHNTTA KLVDDVADDQ DDSAFDNDKA ADKKRGFQCK FCTTRNSRQW
     RRAPGVAPGS TVPAEPSSNK RDKGPQLQVA LCLRCALLWR KYGIQWENVD EVAKKIAQSG
     NKSWRRRVDE ELLAQLLVAT EIPISISSAT AATAASIGVP VNANPQVQQE SGKKTNNGNN
     KGRADNKDSA ATSAATSVEP APKKKTAPEK APEPAPIIPD PPKAKTLPCA ICNSMEPMGD
     QHVSCRDCRL TVHRSCYGVS PSRNCVKWLC DMCSNDRNPM ISTCYECVLC PVTWTEHELM
     EAPRVSHKKK TDRDREKERL EKEMVNEAIK LYRQRQEAVG KPIGPREPLK RTAGNNWVHV
     TCAVWTPEIK FGNAKELEPA EGFGFIPADK YRETCKICKT NKGACVSCHH SGCNAHFHVG
     CAFQAQYKFG FDITPVKSSR RDTVHSMRLG DEVGSAAPAI WCPHHTASPH SHDIGEATEQ
     EGLNALQRFA QTYKQADLTL TGTIRKAAYV QQTVGASQNV PVFGHRRPSA VNGVAALSPT
     KDGPKNSTTS PVDAPDEMDI DSEGPAPRPV TGTDAERKCA RCASAFSPRW WPLDRPRRLT
     GVSNRTPLLN GIGLGSPPFH GPSLTRPNGD YSPTGGEQQT SYECHKCHLK TLAAPPSPEP
     KPSPYSGQRP VLPAPRLPEY HPHPYGPHAH PTPAGVLPRP LGPAPPPPQY AGYDPRSPEA
     LRNGTISVPT YHGGPAPPPP PPPHHAPHHM NGYQQPSHHA PPPPPPAHYT NGAPPPPPQA
     YPTHHSPYGP VAVPSPHPSH TPGPRPFASS TSPPSVQATM VRHSPQHSLS ALNAGPPRVY
     SVDRVLSVPA QSPPVSQAQI DPRGPTPPSR LEDTPVPAPA VPMSSGRHAS VNGTSGGSGA
     SASPSLKNLL S
//
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