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
//