ID A0A4S2MYT6_9PEZI Unreviewed; 1602 AA.
AC A0A4S2MYT6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=BAH-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EX30DRAFT_340360 {ECO:0000313|EMBL:TGZ81942.1};
OS Ascodesmis nigricans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascodesmidaceae; Ascodesmis.
OX NCBI_TaxID=341454 {ECO:0000313|EMBL:TGZ81942.1, ECO:0000313|Proteomes:UP000298138};
RN [1] {ECO:0000313|EMBL:TGZ81942.1, ECO:0000313|Proteomes:UP000298138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 389.68 {ECO:0000313|EMBL:TGZ81942.1,
RC ECO:0000313|Proteomes:UP000298138};
RG DOE Joint Genome Institute;
RA Lutkenhaus R., Traeger S., Breuer J., Kuo A., Lipzen A., Pangilinan J.,
RA Dilworth D., Sandor L., Poggeler S., Barry K., Grigoriev I.V.,
RA Nowrousian M.;
RT "Comparative genomics and transcriptomics to analyze fruiting body
RT development in filamentous ascomycetes.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; ML220117; TGZ81942.1; -; Genomic_DNA.
DR STRING; 341454.A0A4S2MYT6; -.
DR InParanoid; A0A4S2MYT6; -.
DR Proteomes; UP000298138; 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; 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); 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; IPR001005; SANT/Myb.
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 SMART; SM00717; SANT; 1.
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; 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:UP000298138};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 190..308
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 490..639
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 652..695
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 922..972
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1030..1164
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 176638 MW; A96D949407F454D6 CRC64;
MTDRKGLGAQ RASQASPGEG LSPSIPATSA AASKVRSTSP YGTRSRNRGA RVNYAEDKDS
EMDFEYTTPP APASTAAPAK AQGTSEGSSR HQSTVTNNNK DASAGAVARE SSTYTQAAAP
VVGSTTTAGK KRKGASTLAA AAPAASAASQ SQAAAAAMMR PLPKDYSLTN MLAFSSPTLQ
DGKLVADDGT VLQVHDHIYM ICEPPGEPYY LARIMEFLHQ GNDSSRPIDS VRVNWYYRPK
DIQRKVTDTR MLFASMHSDC CPLNSIRGKC YIAHRSEIEN LDEYRKLRDH FYFERMFDRY
IHRYYDVIPT HKVRNVPEHI RKVLVQRWKY LLVEPQRGKE LCAQMKECRR CSGYCANNDS
VHCAVCDSTY HMNCVRPPLL KKPSRGFAWA CGPCNRAQER KLQARNGTAN TSSDGHPNGE
TEEEHLDDDE EEMPNCVGTE TPSEAAAELL LQEPTPEQRK LASMWTMRYL GQHCKIEDAL
DYDDRIYPRA SSRLGPKHQA VVTPWPGRPF ELVKPAEGKR KYAKGPGGRT KLVEVAPAKA
QRPPWVIDEP PGYIERGGDD GKTSTLMFKV PVEGFDDSAQ KERKERVEEL DRYMDKTQKI
AEGMKMKFYA TNFVDKAAEL LFANGWDEEK ALEQLSKVTP VKDLKEPRLK PDEVKRFEEG
VAKYGSELHL VCKHVKTRKE ADIVRFYYQW KKTDKGREIW GNYEGRRSKK EGKKKDSEAN
GTTTGPKLAD DVADDEDDSA FDVEKANTKK RGFQCKFCHT KHSRQWRRAP GVPPGTLVSP
NDKGNSKKKQ TDDRPLISAL CRRCAELWRR YGIVWEDPDE IQKKVNQGGG RAWKRRIDEE
LLRELYSAQQ DAKAENFYAS SATPQPGSRT ATPDDKKEPP RKKAKTETNG VKKAKASEKH
VDVVKETPAP PPPPPEPPKP KLITCRVCAV VQEAGKDHAT CRECKMTVHK KCYGVEETRI
PSKWLCDMCS NDKNPVVSTN YECVLCPHPC HLPNYEPEKK PSHKKKKVAA PPGTDSLVRG
SPDVDGRRIK DSEKYKPNRP REPMKKTANN NWAHVLCAVW TPEIKFSDAA NFQVVEGIGL
IPQTRWLQQC KICGAGNGMN GACVQCAQPS CHAFVHVWCA RQAGWTLGFD VQPVKGSRRD
AINTVKFNNE IGHMIAGVWC PEHGKAQSVH QMSEVSEESG QTALEVYVRA YKQADLALTG
TVRKANLVSL STKANNAGRR NSLIGNTTKE GPDPSTVVYI KSEGSIPDRI GGITGLLPGH
VGGDGPKECV SCKVTVSPLW WKVLVGEPAL TNGSGPEPHT NGATPENRVV GLRCNRCHIK
KTSVMNGEGP QPKENPFLPL PPLQTFLEQQ HMPPAPQMGP APPAALPPLA VPLPTPTTTM
GIPVSSVISQ PIIVPPLGGP LTHHVPMGAP IMAHGPSHHH PPSRSILHHI PPPSHAIPLP
QISPTARTFH HVSPPPPRGM HHPPPPTSSS SPLVATIQTH LPPHPTHHQH LNPISPHKPP
PPPHHPSHSS PPQMYSHPPP PMLMSRRTSS AGLPPPTTSM PPAPQISAPT APMSHLPPHH
IPPPPPQLHP QGMQTPQMQR QEEPKRVLSA ASGSPALANL LS
//