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Database: UniProt
Entry: A0A166J320_9AGAM
LinkDB: A0A166J320_9AGAM
Original site: A0A166J320_9AGAM 
ID   A0A166J320_9AGAM        Unreviewed;      1060 AA.
AC   A0A166J320;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=DUF726-domain-containing protein {ECO:0000313|EMBL:KZV74103.1};
GN   ORFNames=PENSPDRAFT_648301 {ECO:0000313|EMBL:KZV74103.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV74103.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV74103.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV74103.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the TMCO4 family.
CC       {ECO:0000256|ARBA:ARBA00009824}.
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DR   EMBL; KV424483; KZV74103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166J320; -.
DR   STRING; 1314672.A0A166J320; -.
DR   InParanoid; A0A166J320; -.
DR   OrthoDB; 8526at2759; -.
DR   Proteomes; UP000077086; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR007941; DUF726.
DR   InterPro; IPR029024; TerB-like.
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.
DR   SUPFAM; SSF158682; TerB-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        387..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          29..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1008..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..915
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1043
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  114983 MW;  493CE80AE0846A99 CRC64;
     MSKFTPQDAA FFDLDDDEGW EDMPVVRQDE FAGGLDDEDQ KKYHYKPQDK REDVSKGSGN
     ALGEVLDVDA FGKEWRANTA AANESEYTRL RIREEDEADE VHLRTRYLFD EDQAMTPLSQ
     MQQTKNLLTE AQRVAYVGLC ALVIKEMTDA LRKLENRDVK PAIQNLELWG LKILGRLYYH
     MELATPEQKM IQNLSLHGVI PEDLVPALMT THTVANPEYD PAEAQRQQQE REDDVVATLS
     DDISEITLVA EPESSNADEG PSTPTTASKA AEFQTTARVL DETTAAQIPG VSTTLSAADE
     LVTLDIRWTV LCDLFLILIA DSVYDARSRV LLEQVAKRLG LGWLDVVKFE QRVTEALEIQ
     EGVEKMEQKE IIDGNVKKSR KRRYMMMGLA TLGGGLVIGL SAGLLAPVIG AGIGAALTTV
     GVGGTSAFLT GTAGAAIITT GGVLTGANIG GRGMARRVQS VRTFDILPLH NNKRVNAILT
     VSGFMTGELD DVRLPFSVLD PVVGDVYSVL WEPEMIRETG SALKILTSEV LSQVGQTVLQ
     ATVMTALMSA LQWPILLTKL GYLIDNPWNN ALDRAKAAGA VLADVLIQRH LGVRPITLIG
     FSLGSRLIFY CLLELHRQKA FGIVQDVIIL GTTVTAPQKT WYQARSVVSG RFINCFARND
     WLLNYLFRAT SSGLNTIAGL RPIENVPGIE NIDVTDKISG HMSYRTFMPL ILDQLGFPVS
     ADYFDEPEEP DFEGERVVIR EGEEMPKKRG WFGRAKSGSV GRSSSGSVSR PPTAYTPPPR
     KSKDGDVKSA IDDELPPREV ASPPPGAAPR EPKTLDEAGD MGAPELPPAK AGFNISAIKA
     VIDNTAPADH PLPAGGREPP PPPLDLAAAM QTASSSRPQS APPPHDDDDH TPTREKPEPT
     MPLRESIDEL DEHASIKLNT PMTRSLSLND VSRADESAED EDEGRFAATS SSSSRAGPSN
     SFAPPPSFVE DNAIWAPPPL PEKDGLYRSG MSFGSPFNVG APAFGESTTS FGAPPSSGVQ
     LSFGDRDGDI TSAATSSSDR DPWAIPSTKA PPSYLSNPWG
//
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