ID W9ZF37_9EURO Unreviewed; 500 AA.
AC W9ZF37;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O3_01676 {ECO:0000313|EMBL:EXJ93119.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ93119.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ93119.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ93119.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ93119.1}.
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DR EMBL; AMGY01000001; EXJ93119.1; -; Genomic_DNA.
DR RefSeq; XP_007730009.1; XM_007731819.1.
DR AlphaFoldDB; W9ZF37; -.
DR STRING; 1182542.W9ZF37; -.
DR GeneID; 19165809; -.
DR eggNOG; KOG3975; Eukaryota.
DR HOGENOM; CLU_018394_3_1_1; -.
DR OrthoDB; 5474978at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR GO; GO:0019915; P:lipid storage; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000019478}.
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 55031 MW; F46884C21E225C20 CRC64;
MDELLYPPVR FPCLSEGLGQ RQHSHSGSGS SRSQSQPQEQ SQDQDQDQDQ DESDKSQPKE
PKEQTAQPSP CEDDDNDDDK TNTRLYSLRE QIELSYARLE KLVDTLRNHN HNCKDGLSTA
KAASTGPGDG TAALETGEQE QEREREQDQE QDQEQQREQE PGRDPTQGQV PEPQPLVNVV
LVGHSVGAYI ALEIVRLRHE RHGFRQSSSS TTSSSSASNR ANSTSGINIS STSTDTTRTG
QSSTSSPPAA SVNASWTVTA CILLTPTIVD IHRSPSGRVA TPLLTSLQLA LPSASASRFI
LPVLAHTLVH SVLVKSLPST WLSWLVERVA GMKRGSHGSD ATLAFLRSPR GVKQALYMAA
DEMGQIRADG WGEEVWGAAA VDNDIGGATR FSPTPRLYFW FAKSDHWVAD ITREEIQRAR
GGGVVERDEI DILGHATDEV QFRLDATNHD KHAVDEAPMV RIYETDGLAH AWCLNQSEFV
ARRVIGWLRE ILGQECRESV
//