ID   A0A177CVA5_9PLEO        Unreviewed;       890 AA.
AC   A0A177CVA5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=MHD domain-containing protein {ECO:0000259|PROSITE:PS51072};
GN   ORFNames=CC84DRAFT_1159018 {ECO:0000313|EMBL:OAG11494.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG11494.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG11494.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG11494.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV441548; OAG11494.1; -; Genomic_DNA.
DR   RefSeq; XP_018041859.1; XM_018177115.1.
DR   AlphaFoldDB; A0A177CVA5; -.
DR   STRING; 1460663.A0A177CVA5; -.
DR   GeneID; 28760601; -.
DR   InParanoid; A0A177CVA5; -.
DR   OrthoDB; 2056337at2759; -.
DR   Proteomes; UP000077069; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT   DOMAIN          608..866
FT                   /note="MHD"
FT                   /evidence="ECO:0000259|PROSITE:PS51072"
FT   REGION          237..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..154
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        258..272
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   890 AA;  96363 MW;  8AA27979FB578851 CRC64;
     MELQRKEYPG LLDALPPQQA VDVLNGRMKH VSALNAHIAD WLQERRRVEE AYVQGLRKLA
     NKRPPDDSSD LGVFSTPWQK IVSATEAVAE SHHTLAQKIE VDVERPLREF ATTNREVQGM
     STISGNLASM AREIDTAKKK AEKLREKGAK AKASAVASAV ADVENATLQW ESQAPYVFEK
     LQAVDESRLN HLRDALTQFQ THEVDQVERN RISAEETLNV LLNIETADEI QTWALRMRSG
     EKPPPANRKG SSVGTPSRSL APPPPMPPPP MIQADDDRSQ KSGSVPEEKG KHSSNPLKRF
     GTVLNRRRQS MHPYGRQSSP ERKSNSNLGS GFPGFGKIKS KDRDTASSSI DRPGSSATGA
     TPRPSDASAS PKHTRKSSAD PDRPNGASPE PFEERAASPT PAPAAVNGTT HDTIPELIEP
     LAPPHHEEPR AEPEKDDEGF SKPLSAIDAI TQAENEAREA GLSGNELGNP PPQFKLDIKN
     APIQEEEGDV NAAMADMANT LRAQAVPPRR SGTLRGRRDV RNTIFVPNPA TPELTSIGEM
     PPVPSASSEN TTFPPPAVPP QPASPVFKLP HRSLATDDHP ASDTQSIRSG RSLSSSTSTT
     MKHPDMHEPG LNASLVETVS AWFEQGHVTK SLVIGQVALA FNPVDISSGP FGTENIRLEN
     FPVLEKVAPN PAFVEQVTDT PGEYTVDLSR ITKTSVAFHY QVHLETENLA SFAPILLSPV
     WKSEPTQTSV LLNYGLNPKF NIGDQTSITL QNVVLVLRLE PGSKATSCQS KPAGTFSREK
     GLIYWRLGEV TFSRDQPAQT MRVRFFTDGE AKPGNSEARW ELTGAHSLAF GSGLAVSQVA
     AAAGESKTEE KEADPFADAE ENVPPAGGAA PSWKPVTCVK RISSGTYLGV
//