ID C6HSU9_AJECH Unreviewed; 415 AA.
AC C6HSU9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DUF676 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCDG_09280 {ECO:0000313|EMBL:EER36624.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER36624.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. LDAH family.
CC {ECO:0000256|ARBA:ARBA00008300}.
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DR EMBL; GG692439; EER36624.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HSU9; -.
DR STRING; 544712.C6HSU9; -.
DR ESTHER; ajecg-c0ndw0; LIDHydrolase.
DR VEuPathDB; FungiDB:HCDG_09280; -.
DR HOGENOM; CLU_018394_3_0_1; -.
DR OMA; LIGYYHT; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0019915; P:lipid storage; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR019363; LDAH.
DR PANTHER; PTHR13390; LIPASE; 1.
DR PANTHER; PTHR13390:SF0; LIPID DROPLET-ASSOCIATED HYDROLASE; 1.
DR Pfam; PF10230; LIDHydrolase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45317 MW; B3052D607D44E407 CRC64;
MNQLATPHIT TNSFLTFTGT SCTADEPESI LLYFIPGNPG LIAYYHTFLS LLSSTLISSA
EYSDYDDGSA ENNSSTASSS HMGKVPQYII HGKSMGGFEI VENGKHVSCC SPPLTNIKAN
GGMETQSQSQ PQAHHHPTTK TNKLYSLSEQ IEHVERNLNN FVDAWHARKL AQTRGKDLSD
DQGRWRHFGG VKVILIGHSV GAYIAMEILR RHREGIRQNG AFADTGVAGI GATMDIVGGI
LLFPTVVDIA QSSSGRKLTK LLYVPYLAFL TSLLVKFLIF ILPGSWLRSI VGRVMGSPSD
NAIDTTVAFL KSARGVEQAI HMSADEMRDI TYDKWSDEIW GIASSSSAPS PMSAPSSEES
PLNLVLYFAK QDHWVADRTR DEIIRVRGGV GSSSGSNGPR MQNIVTSWQR RPPDG
//
