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Database: UniProt
Entry: A0A165J9V0_XYLHT
LinkDB: A0A165J9V0_XYLHT
Original site: A0A165J9V0_XYLHT 
ID   A0A165J9V0_XYLHT        Unreviewed;      2060 AA.
AC   A0A165J9V0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=BAH-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L228DRAFT_271943 {ECO:0000313|EMBL:KZF25948.1};
OS   Xylona heveae (strain CBS 132557 / TC161).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF25948.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF25948.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF25948.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA   Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal endophytism.";
RL   Fungal Biol. 120:26-42(2016).
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DR   EMBL; KV407454; KZF25948.1; -; Genomic_DNA.
DR   RefSeq; XP_018191503.1; XM_018335579.1.
DR   STRING; 1328760.A0A165J9V0; -.
DR   GeneID; 28900716; -.
DR   InParanoid; A0A165J9V0; -.
DR   OrthoDB; 1409291at2759; -.
DR   Proteomes; UP000076632; 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; 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); 2.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR034732; EPHD.
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   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          479..597
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          634..686
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          779..955
FT                   /note="ELM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51156"
FT   DOMAIN          1240..1290
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1346..1463
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          209..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1161..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1531..1583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1624..2060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..862
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1162..1187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1190..1204
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1236
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1539..1559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1563..1578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1642..1656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1721..1735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1736..1773
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1796..1830
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1831..1846
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1847..1872
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1901..1920
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1927..1947
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1948..1965
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1979..1999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2024..2060
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2060 AA;  224609 MW;  5FACFAE6D0DEC611 CRC64;
     MAFAFSTCQE KIARDAKESV LYKPSCEPKP DGQYVKSTSM CPVSYGLISY VATIEQIATL
     KMMYSSNSEQ FSSNYRLIAK YSIQNGQFKR IKSSLAWIII STVFQAAMTH KKGLAQEASL
     VGANMNVEIS LLSLTPFEVY QRPFWAPSLP HRASHSLGKA RGEHSAAPTC SIRKRGYDIE
     FATNLLLPSS AQIHQGILTL MAEINGQSSS EAASTPAPAT DLAGPAPHQA PATPDVRTQS
     SEPDGPDSAR HASTESPSAY EKPPESQPMT ASSSSSGSNA VSKGTTKELA APYGTRSRNR
     VGTARPNYAE DNEGDLDFEY STSAAPPSSS ARKSNANKES TAATTPQTTG SEGVRSRGPS
     SRRAPVAPDA QSNAAARPIP SAAPKEPAPK EHAMGNPGAT TVPASHNQAP SRKRKAGGAT
     STGQSTAAST PTSAHTSTRR GGAVTTSTTQ PALRETAMPS FELSQKYVKH GKLKADDGTL
     YGPNDHVYLV CEPPGEPYYL ARIMEFLHVD NNPSRPVEAI RVNWFYRPRD IQRKITDTRL
     VFASMHSDIS PVTSLRGKCQ IRHKNEVEDF EEYRKQRDSF WFEKMYDRYI QRHYEVIPVN
     QVINVPAKVK KVLQERWKFV IVEIGRGKEL TSAVKLCKRC GAYCASNNSV ECAVCHNTYH
     MNCVRPPLQK KPSRGFGWSC GPCSRAQERK LEARNTPIIG SINEHEEEEI FEEEEDEGPG
     LAGETGTSTP SLEDSQDLTL HPATADQIAQ TKLWPYRYLG VHCHVEDALD YDDRIYPRAS
     SRLGPRHQAN VIAWPGRPIE FVKPAEIRRK YGRGNTTKKD PKLPKDVAAA LEADKAAREK
     RPKWVLDEPP GYVPRGEDRP NGDPENTAQL LFKLPDEDDM EANQTYIRGD DEMAIDMKPE
     EREERVDSYM QKAKRLAKEV GVKEYNTNFL DKALQLFYEN RFSEGPALEK LKLVNRKKDL
     KEPELNREEL KRFEEAVLKY GSEHRNLREH VRTVKHPDIV RFYYTWKKTE RGKQVWGSYE
     GRKAKTGVKR GEAHPAKLVD ELADDHDDSA FDKDKAAGHK CGFECKFCGT RKSRQWRRAP
     GVAPGTKVPL DPNQKGKDKG PYLALALCLR CAGLWRRYGI QWENIDEVAK KVAQGGGKAW
     KRRIDEELYN ELLAANESAA RTKEVEASSS RASPATVASS QAGQEPAKKR ARTTAQEKQE
     KESAAAAEPG PVAAPAAPKK KAPPKPPSPP PAPELPKPRT LPCFVCNQVE PKGDQLLTCR
     ECRMSVHRNC YGVSEGRNAA KWVCDPCTND KNPQVSTSYE CVLCPVKFTE RDFVEPPKAA
     AGNKKKNDKE RLERELAIEA AKFYRQKQEE MHKPVDPCEP LKRTAGNNWV HVFCAVWTPE
     MRFGSAKALE PSEGIGTIPS ARYEQVCKIC KSSKGACVAC HYCHATVHIG CAHQAGYILG
     FDVTPVKGSR RDIVNTVTLG EESGLLTAAV WCKDHPVKTI MHPISEIDQE TGLNALQLFV
     RNYKQADLTL TGTVRKANLV NQSTKLLAHG MGASPLTHRG SVSHATNGIT ASGWSRRGSR
     PSPSEPIKSE DTDFPDRRSS GVDGSNAKKV ICVTCGIDVS PKWWPSEHAK PSKGLLVDGQ
     PKAKSVELSP AASDGLLRNG DMMSNADSNT STPDVEMKDD SVPPAAASLA AGKSTRRKSS
     AGTPMQCHKC HWKRLREPSP VAPPKTTPAS TAASPFRAQP LPPFVQSTTA TPPAATHQAP
     RPPPPAQLPW PPAPGPGLWR DHPQPPQQPP AASLPPAQNG LRPVNGFSPQ RPPAALAYSH
     SPPQPIPPPP AALPIVPPAV VPPPPPPPPP PTHHHHHHHP PPPVHHHHHA PPPPAQANGY
     SPRPPPPHAL PIFEQPHHGM PHLTHAGPGP ITGPGSIPVS HYTTAPPPPP LPPHPAASTQ
     HVHPPPHTVP IHHHHHHHHH HHRPHHPTAS PAGPPHIPPP PHDARSPHTV HLSPLAPPTR
     SLVSENSPFS STTAPSPRLA TFMTPGGGVA GQAGSPPIPK RETPTTPSMQ SVGPATTGSG
     SDSRAAGGAS ASPSLKNLLS
//
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