ID A0A0H2R6K9_9AGAM Unreviewed; 998 AA.
AC A0A0H2R6K9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE RecName: Full=BAH-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCHPADRAFT_945298 {ECO:0000313|EMBL:KLO07425.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO07425.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO07425.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO07425.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ086140; KLO07425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2R6K9; -.
DR STRING; 27342.A0A0H2R6K9; -.
DR InParanoid; A0A0H2R6K9; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000053477; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR029617; Snt2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013088; Znf_NHR/GATA.
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; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51293; SANT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053477};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 24..160
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 479..532
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 259..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 111733 MW; CDF137B97D522045 CRC64;
MSGTSASPTD SHSSEVHVTL KNGEQVRIND HVYCSPPWSI RDGTPYSVAR IMEFLPPEDK
RPRGTVKIDK GKGKSKEAFT RVRLAWYYRP SDVSDRAVAD SRLLLAAIYS EVCDINHLRS
KCYVMHKDKL ADLSGWKKKP DHFYFHRLFD PYIKKEFEVL LSTNVRNLPA HIKEVLVLRY
EYVVAEKEVT NELTDSLRLC QSCMEWCAHL ESVQCARCKE HFHMSCVSPP LIAKPARGYG
WTCAPCSRWH EDRVDSVDNV QTPQTQQSGS TGNRETTPKS TNVASAAPVI SANASAQPIS
AKPARGRGRP RKEKPGMKQS SNEEDLKVKH YRMWPFRYFG MYTVAEDTLD ADDLIFPRAA
IRTGPKNQVT ISPSADICRR QFKSASNAFP IELEERGGDS TIEVLGLIHE FNQPEVETLE
ALMLKLATRK DMTYSVDWLT EVIRRVSDAH KHGRGLETVN MRSSMRLEKW KKHDTRYTDR
EWNHDEIAAF EDGISQFGAE LRSVRDEVGT RTMPEVVRFY GKWKNGKLRE ENVRLREPEA
YTKSEIPRSG AASPANGAST QSTNDDDTSV VNIPASKPGS SSRTSTYCAA CRTRDSPRWW
KAPRSLSSEV LCEECGLNWR KYADLNARPT TREETALSGS AAPNGANGVG SGLAKLRPTE
KRPLSPQNGQ SGAKRIKISG ASPTGTTPPP TTTQLRCLSC YKHGPAGKVL KCRECGFQVH
AGVCGATVDR DDLDGWACEL CQNDKTQDAS LDSDCRLCPR PRPGSKPVPN PPSDTYLRAC
KPTEGHGWVH VLCAVFIPEV EFADTETLKP VEGLSTIPKH RWTTTDGGAV IRCANCPKEY
HVSCAWKMGH KFGFELQPVK SSRRDITTMV SFKHDYGLMN AVVCCKEHSS YRREMHNICD
TDDWGNTALE VYVRAYKQAG TAETHSLLRK ARRLDQILSS TNGDASGSDS ESNLSVDVEC
EDCHSQSSPS YHPHPKAGRG KYQCHRCFFK CADEKHRP
//
