ID   A0A395HPH8_ASPHC        Unreviewed;      1175 AA.
AC   A0A395HPH8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=DUF726-domain-containing protein {ECO:0000313|EMBL:RAL09862.1};
GN   ORFNames=BO97DRAFT_479732 {ECO:0000313|EMBL:RAL09862.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL09862.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL09862.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL09862.1,
RC   ECO:0000313|Proteomes:UP000248961};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TMCO4 family.
CC       {ECO:0000256|ARBA:ARBA00009824}.
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DR   EMBL; KZ824300; RAL09862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HPH8; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_479732; -.
DR   OrthoDB; 8526at2759; -.
DR   Proteomes; UP000248961; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR007941; DUF726.
DR   PANTHER; PTHR17920:SF24; LIPASE MIL1-RELATED; 1.
DR   PANTHER; PTHR17920; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4 TMCO4; 1.
DR   Pfam; PF05277; DUF726; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        595..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        638..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1175 AA;  128795 MW;  84A1EC5BAA3C76A5 CRC64;
     MSAVSSPSPV DQSVDDDAAD LSHHSHTSKP SANATVSPSA TTDITLNGNV NVNAVHSERG
     EVTLDKTTAL SSESGKPAAA NPEPQQPQEE LDDFGLPIRV RPKRESSESE ETFHDVSQQG
     QGRDGDEGDG LSHTEVTVAE KLGSDEQTTE KSRVVSNDES EGATPPSPKP VVQEKEVSTR
     APTEPPVAPE NRELPRDEEP PPPYTKTPSH DDTRHSTDLR KTKRKSLEAS EWSHQHLNTT
     IDSEEESEEE DDDGGWKDMP ALGDMDVYDD YGRLVAKGSK NVESDEAVYS GMGGAGKGYT
     RVQLDEDAQS ATSMDEDTSY LFKDSHANSA GVEEELRDPT SQMQATKDLL TESQRIAYVG
     VTRLTLWQMA LEMNRIPSIK GCRKARQGGI DSMRKWGQTM MARLYSHMEI DAAEQVMIEQ
     LAEHGVQPAD LVRPLMSNAR VKNPLAEATD TPKRSLSSPS SPPLREEYRS SISTELDQSS
     RSTSPPPYET HEGEDLPEVR TPSQLPTSAK IDIDLRWTVL CDLFLVLIAD SAYDARSRTL
     LERVGESMEV PWLQIARFEK RVIDALEMQE SADKENWDET EHMEKRRKMA LKHKYMIMGL
     ATVGGGLVIG LSAGLLAPVI GAGLAAGFTT VGITGTSAFL GGVGGTALIA SGATLTGSTI
     GLRASQRRMG AVQTFEYRPL HNNKRVNLII TVSGWMTGKV DDVRLPFSTV DPIMGDLYSV
     LWEPEMLRSM GDTINILATE ALTQGLQQVL GQTVLVALMA SLQLPLVLTK LSYLIDNPWN
     VSLTRANAAG LILADSLMVH NLGKRPVTLV GYSLGARVIF SCLKELADKG AYGLVQNVYL
     FGSPMVANRD EYLKARSVVS GRFVNGYASN DWILGYLFRA TSGGIMKVAG LAPIEGIPGL
     ENFDLTKLVN GHMDYRTAIP RLLKEVGWEV LSEEFAEIED PDPENHAERQ RELIREIDEA
     RRDAEQKPEK KRFGLFKRGK LAQKKKWETY DVDRNNATAR SSTDTNNGTG SVLFDIDAIR
     AELASENLEV KQLESTLPPM KLDLSAPASP SPAPSPPKTQ ETKFYEPTSP PPQTLPEKQP
     SYSPSRQAPP YSPHHEEEVE MTFDTSFHEP LPRSHSSFGA SNSYDAQPTR PELRSTVTMP
     ALGASTMGAM ALEPNAWAEH DIGDGDESEI QMTFE
//