ID G4US26_NEUT9 Unreviewed; 836 AA.
AC G4US26;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:EGZ70402.1};
GN ORFNames=NEUTE2DRAFT_151175 {ECO:0000313|EMBL:EGZ70402.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ70402.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ70402.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., 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 Genetics 189:55-69(2011).
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DR EMBL; GL891247; EGZ70402.1; -; Genomic_DNA.
DR AlphaFoldDB; G4US26; -.
DR STRING; 510952.G4US26; -.
DR eggNOG; KOG4388; Eukaryota.
DR HOGENOM; CLU_003590_1_0_1; -.
DR Proteomes; UP000008513; 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 Hydrolase {ECO:0000313|EMBL:EGZ70402.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513}.
FT DOMAIN 221..366
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 481..565
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 367..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 91989 MW; DD15A825202F5787 CRC64;
MIDHLLGRPS AKSRRLQVLA VLGFWSAYLI KGHKHGPPGF RIFSRLLSRR LTTWQTVILT
MIYLYAARNF STLVGLASPE PMANMYDAAY FRATWVLTAL DAGFWTAMKI KQKWLRDISS
IAFSLFYLVA AEKADEKVRK VRGNLTVEHL RVSWNKGVTS PYLRFVQNLM RPRFTRWPPR
QIRIPRPATS DYKDPVAAWL YYDGPLADLE YHNKIILDIP GGGFVAMDPR CNDDKLFSWA
AKTGLPILSL DYKKAPEFPY PYALNECYDV YSTIIKTKGR CIGLSGREVP KIVVTGDSAG
GTLATSMTLM IVESGSSPVR RFQGEANLKV PDGLILFYPA LDMNIGSWMS DEQMALIKDR
RMRGTNKRIV QRKTSQYNDL VGTPAPSDDE DDGPSSGPNP EPSLVKEKEP LSAARSAPEY
AHSGPSTWSH ADIPSLSSSR SEKSKTTEKQ PKAKSSAVVT TTTPSPTAAP HSHHPQPMRT
RLAMSSMISY FADRVLTPEM MRAMIILYVG PHNRPDFSSD YLLCPILAPD ILLSKFPKTY
FLTGERDPLV DDTVIFAGRL KRVKAAMVAS DGTRTQYREE DVDEAIRKTN GKWDGKQAAE
VALVPGISHG FLQFAGVYPP AWGLFGKIAG WMGEVFAEAE RKEREEERAR RKMGVAGGAK
LEEKAETGAA GRGTNEKGVG FGAVEEHSAE ERTGRHHRRR GTGGTESSAD EDKPLEMGGK
ARTRGRVALK NAGSISEGNA STSADAMEGM VNEDGIHVVE GAEGDEEAGS DTATEAAIAA
NTKVKAKKAP RRMKLRRVKV GDEDGALLVR LDSSDDILGR RMQGLAGGLT GLQEAE
//
