ID A8P1A3_COPC7 Unreviewed; 560 AA.
AC A8P1A3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Fungal lipase-like domain-containing protein {ECO:0000259|Pfam:PF01764};
GN ORFNames=CC1G_07550 {ECO:0000313|EMBL:EAU83815.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU83815.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU83815.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043831};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC Class 3 subfamily. {ECO:0000256|ARBA:ARBA00043996}.
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:EAU83815.2}.
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DR EMBL; AACS02000006; EAU83815.2; -; Genomic_DNA.
DR RefSeq; XP_001838060.2; XM_001838008.2.
DR AlphaFoldDB; A8P1A3; -.
DR GeneID; 6014629; -.
DR KEGG; cci:CC1G_07550; -.
DR VEuPathDB; FungiDB:CC1G_07550; -.
DR eggNOG; ENOG502S209; Eukaryota.
DR HOGENOM; CLU_035620_0_0_1; -.
DR InParanoid; A8P1A3; -.
DR OMA; VAFMESA; -.
DR OrthoDB; 91669at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR45856; ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR45856:SF11; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 173..333
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
SQ SEQUENCE 560 AA; 60796 MW; 6F54F8D5EC7A38D4 CRC64;
MPDTSLGFKI IKDVVRQRHL DQLSAHPKLY AEPLKTMPVF ATREDIVQWS EESKAQIAQG
QADRVYGGPI GSPLNLNNAF MAFMESATVY LRDTSKVLDA VQKYQAGHVE EALRLLEDST
RIIDEIAEMW GMEFVQICDL PERHPDGHSF LVGPYCGAFF PKDFSGHNPF IGIAYKGTSN
FGEFLNDLLA ASTIKASGRL WNTEVCSGFY YPLFSTYSAK TLTTTAAVTS TMPFVMVQQA
VQDLITRATT TVITHVTGHS LGGAYATLTH GQLCIEGFGA AGAAVGDLYT FGGPRAGRGD
FATLFKASVA PPTDQGSTWR IVNYKDYIPK VPASKPLIPV SNPFVHIDAG VMVYPDKQPE
SLPSEIGTKP TWSIPTAISP HYTTEYYKSL VFATTGKPPV SATLARAPHS PSLSTYNTTQ
VTAKLEPETR NALPGAEVTF EPGHGGFVVG KVRYGHFLGE IVALGTLSEV SQNPQFFCDS
MEALYGKENH AVFSVKDGKT LEVRFIVDDQ EVAVARASTS EDIDQVPTRG VCRFYDDGTL
EAVEQSVAQS AAAVFQHASA
//
