ID A0A150G4J4_GONPE Unreviewed; 1138 AA.
AC A0A150G4J4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Fungal lipase-like domain-containing protein {ECO:0000259|Pfam:PF01764};
GN ORFNames=GPECTOR_63g30 {ECO:0000313|EMBL:KXZ44703.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ44703.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
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:KXZ44703.1}.
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DR EMBL; LSYV01000064; KXZ44703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150G4J4; -.
DR OrthoDB; 373802at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd00519; Lipase_3; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR PANTHER; PTHR46023; LIPASE CLASS 3 PROTEIN-LIKE; 1.
DR PANTHER; PTHR46023:SF5; OS02G0780700 PROTEIN; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT DOMAIN 182..313
FT /note="Fungal lipase-like"
FT /evidence="ECO:0000259|Pfam:PF01764"
FT REGION 575..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..877
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 113290 MW; 894ECC2F63BCBEE9 CRC64;
MSSGVVAAGA AAVALYVYLK QKGLQDGEDG AMEPVLPIEA CRTDQAPSNW SEALFHVKEV
LRYMYNETLG RWHTIDLFVG LAYLSHREAP EYPALDIAAR GVPAEVGLGT SEQLKLLLEL
QEARRYMLYC KGLKLRREEM QARFWKEHMG ADTLTIVKQQ PTAGVLRPAY VLVSDRELRA
VVLCIRGTHS MKDLFTSLAG TAKPHHVVDT NGGGLVLGYS HLGMLAAARW LARHVTPLLR
EARWTAYPGY SLRVVGHSRG AGAGGASVCD RLREARCVSI ACPSVVTLEL AAACRDYVTS
IVNGTDIVPT FCAASVDRLR EDVTRSSWFS EFSRDMRSGV MRALQGGVRG VGTATQWTSR
NIFQPAVVAP FRACYTTTAA AATRRTKRRA AAASILTGAA AGAGGSMAAA AAAAAAAAEQ
QEQLLLGAGA GGGAAAAAAA AAAAAALSEV AGGAGGGAGT LSPTSTAVLA AMSRGAAGMG
AGVGAGRPPL AQSMGVAASG SGLGSSGLVH GGGQPGGAGP HGARLDERAM AEAVQSCMYA
VGSAVSAQAE HGDSPPDPAL AEALELLDSL PQALGAGRAA GRPHGVRRSH PGSGGAADAA
SPSSADVDGA EPAGNLLTGG GAAVSVLSGG GVSTALSYGS SLRRRLWPWG QGPQAAGGGG
GEWGPGGDDV DGGGGGGGSA AAGSAFTSAP PGIRRNNSGA CLPMSTAAAG DSGAPSRASG
GGAGSGGGGL QGDAMTPPHL IAFDSPGKAK AASAALGRPG GGGGSGGGGG DGAAATPGRG
LGDWLWRGSG LLFTSCTTPR RPGGGLGPVP VLRGPGGGLG LGLGVGRAAA ANGGLDAAAG
RRSLRMDTGV AYDDETDDEG STGEGEEEDD YSGNDEEDEE ALARGLPGPG RGAGTGAGQG
GGGPGAGGAE EQLQAGITAV VAAVTSQASR EAEGTAGDET MVGFGAGSER EEEGVTSPLS
PGGGGGSPVG SPPNGSGTGR SAEYEARLYK RRLYPAGRIL HLFPAAAVAG LQSLQRHGSD
GAAGGGSVTP RSGDDGGDDG GDGGGVNATA ASASTTPADA AAARSSAAQA PYVLYEVRDP
TAYSRVRLCR TMVSDHLIPA YLTALDSVMA TLGDEQQRAA REAWEREQER EREQSMEM
//