ID F8MFH1_NEUT8 Unreviewed; 382 AA.
AC F8MFH1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN ORFNames=NEUTE1DRAFT_121702 {ECO:0000313|EMBL:EGO60025.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60025.1};
RN [1] {ECO:0000313|EMBL:EGO60025.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60025.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL891303; EGO60025.1; -; Genomic_DNA.
DR RefSeq; XP_009850203.1; XM_009851901.1.
DR AlphaFoldDB; F8MFH1; -.
DR GeneID; 20824169; -.
DR KEGG; nte:NEUTE1DRAFT121702; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_121702; -.
DR HOGENOM; CLU_012494_6_4_1; -.
DR OrthoDB; 1144477at2759; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT DOMAIN 136..226
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 229..290
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 41964 MW; FDAFB426F0B0AD2F CRC64;
MSNNSAFNFS PPGPQRPIIS PPPTTTASTL PNTATLASIG PRIPTVGSRA RDLHYSIRDF
LSTHPLLELG GQEHFSVERR RHQDVFGLHA LPKDKIHPID DVEFTAIRGP HGTIPVRVLY
PTSGKDNRNK GKAGALIYFH GGGYTVGSVD EFENGLRLVA EESGCQVYVV EYRLAPEFKY
PVQLDEYSAV IDWVQGEGGK TRGVHPEKVV GGGDSAGGNM TAAIYISPQN RYVSPGMQSV
EDLRGQPPAA VFTSGYDPLR DVGCEYASKL SQAGVPTRWR HYDNLTHGWL QMTAWSEVAE
QAVKDVSHEV KRLVFAAIDT HTLKGPQGQL PVDRLNVRDF TLANSQRGQS GDRPTTRAAR
TTRVTTPFKI NTFSKPRNRL VD
//
