ID A0A0D1Z629_9EURO Unreviewed; 698 AA.
AC A0A0D1Z629;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Partial AB-hydrolase lipase domain-containing protein {ECO:0000259|Pfam:PF04083};
GN ORFNames=PV07_11241 {ECO:0000313|EMBL:KIW23006.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23006.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23006.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23006.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847046; KIW23006.1; -; Genomic_DNA.
DR RefSeq; XP_016243222.1; XM_016398660.1.
DR AlphaFoldDB; A0A0D1Z629; -.
DR STRING; 569365.A0A0D1Z629; -.
DR GeneID; 27350435; -.
DR VEuPathDB; FungiDB:PV07_11241; -.
DR HOGENOM; CLU_024238_0_0_1; -.
DR OrthoDB; 5471104at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006693; AB_hydrolase_lipase.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF160; STEROL ESTERASE 1-RELATED; 1.
DR Pfam; PF04083; Abhydro_lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 166..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..351
FT /note="Partial AB-hydrolase lipase"
FT /evidence="ECO:0000259|Pfam:PF04083"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 79950 MW; 041AE59A7EC831C2 CRC64;
MSQTQLRTRA HAAVEYEQQA EKLSLESSSQ TDDNGDRAGH AVEAKFITSL DPVIETTDGN
RLPAVPVQEA HKINLLKSRS EGRPYRPGRP RGLSRFDRQR AGAGAVDRSE LMKDDHESES
SRLDEAIPVL HTHPLFPPLP LYGAPSLLRD LQCTVLRTTS AVLSTAFLTV IVLGALFTSI
PHFVNYAWLW LTFRDPYKQR PFYDEERRRL TIRKEQEEEW ERRTSKQDAT IQNGTIEPAA
SSQERLVALE GGPDKLVCDI RYYARRVGLD AEEFKVQTED GFILTLWHIY SPSEYTPRPS
MERQPDEPSV FTDSKEGFQQ HIPKQYSDGN RRYPVLLVHG LLQSAGAYCA NDDDSLAFYL
CKSGYDVWLG NNRCGFSPEH SLLKYHDPRM WAWNIRQMGV MDLPAFMSRV LVETGFEKLG
LVCHSQGTTE AFVALAKEQR PDLGDRISVF CALAPAVYAG PLIGKMYFKF MRVISPSMFR
VFFGIHSFIP LMMTMHRMLP GKLYGALGYR VFSFLFNWTD TRWDRGLRDR LFQFSPVYVS
AESMRWWLGR ECFAKQKCIL ATREDGQNEE VEDGDGEESS ERASSDEDDR GRTAWYDEHV
PPLALWVAGS DDLVDGRRLL RRFQRGREPF VQVVHSKVIE EYEHLDVLWA MDAVEQVGSE
VRQVLWKTMP EEARRICRKI SGVVDDDRGD SQSSDQQE
//