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Database: UniProt
Entry: A0A1L9NP78_ASPTC
LinkDB: A0A1L9NP78_ASPTC
Original site: A0A1L9NP78_ASPTC 
ID   A0A1L9NP78_ASPTC        Unreviewed;       859 AA.
AC   A0A1L9NP78;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=MHD domain-containing protein {ECO:0000259|PROSITE:PS51072};
GN   ORFNames=ASPTUDRAFT_291171 {ECO:0000313|EMBL:OJI91095.1};
OS   Aspergillus tubingensis (strain CBS 134.48).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI91095.1, ECO:0000313|Proteomes:UP000184304};
RN   [1] {ECO:0000313|Proteomes:UP000184304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
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; KV878176; OJI91095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9NP78; -.
DR   STRING; 767770.A0A1L9NP78; -.
DR   VEuPathDB; FungiDB:ASPTUDRAFT_291171; -.
DR   OMA; FQTHEVD; -.
DR   Proteomes; UP000184304; Unassembled WGS sequence.
DR   CDD; cd09264; AP_Syp1_MHD; 1.
DR   CDD; cd07650; F-BAR_Syp1p_like; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR028565; MHD.
DR   InterPro; IPR018808; Muniscin_C.
DR   InterPro; IPR049609; Syp1-like_MHD.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR23065:SF54; SUPPRESSOR OF YEAST PROFILIN DELETION; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF10291; muHD; 1.
DR   SMART; SM00055; FCH; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184304}.
FT   DOMAIN          569..839
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          240..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..261
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  93640 MW;  34EA9DEBC72E20B0 CRC64;
     MELSRQEYPA LLASLQPGQA TSVLNDRIRI INKVNADIAD WLQERRRIEE LYAQGLRKLA
     HRPQLDNGAA LGVFQIPWQR IITATESIAS SHETFAHKIE EDVERPLREY STKNRELSSM
     TGIQSDLAGL AKNYEASQKK VEKAREKGPK GADKLASAVA AAEEISQQWD SRAPFVFEQL
     QAADEGRLNH LRDALTQLET HETDQVERCR QAAESCLNVL LNVETADEIK TFAAKINGGR
     PVVPRRQQTT SPPPVAPLSP PPRLQDDAAS QRSEHSGPVR TPPAPEPRHN TPLGGLKRLG
     TVMNRRRSIV QPSSAGPFFS DKKHRSPFAS FKRGDSRELQ IPETPTEGME RPSTAMTTQD
     TEPPAISNES HDHEGFAGAT STAMPQSAPA TANGATSHEA PSEEITAAAG VSRNEPRVDS
     EGFTERPETI DEITRAQREA AGLEEPGMNL TIRDQPIFED EDQAKQAMDD MANQLRMQSG
     VRRNAGTLRG RRDVRNTVFI PTPAPGNDLP AIPSTLDTSA PTSPSLQARH VASPSTATDD
     HAMSDTTSIR SSHTLHSAPG PVLHPDLHEP GLNASIIDTV SAWFTEGAVS KSFVVGELAL
     AYNATPDVTP GSTRVRLDNF QILEKVAANP HFVTEDKGKD QFDEKRGEYE VNLASIARSS
     PTVAFKYQIH MEPSVAAAYC PVIFKPVWNL EEHQASAIIY YSLNSSFTSA PGGSITLRNL
     VLTVNLDTSP VEGREVAHAT AAVMYPNTGA TFRRKQSAVT WKIPEFEVKA GSDAKLLVRF
     STTASWPRQG KVDAKFEVHT LDDGSRLGIS TASPTNLAKG SDPFADEEAG SQTPELQPSV
     EWKNVPTARK LLGGKYVSS
//
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