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Database: UniProt
Entry: F8PT64_SERL3
LinkDB: F8PT64_SERL3
Original site: F8PT64_SERL3 
ID   F8PT64_SERL3            Unreviewed;       469 AA.
AC   F8PT64;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF00561};
GN   ORFNames=SERLA73DRAFT_105362 {ECO:0000313|EMBL:EGO00894.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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DR   EMBL; GL945478; EGO00894.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8PT64; -.
DR   STRING; 936435.F8PT64; -.
DR   eggNOG; KOG2624; Eukaryota.
DR   HOGENOM; CLU_010974_5_0_1; -.
DR   InParanoid; F8PT64; -.
DR   OMA; DGEHVDC; -.
DR   OrthoDB; 5474043at2759; -.
DR   Proteomes; UP000008063; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   PANTHER; PTHR11005:SF103; STEROL ESTERASE TGL1; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..425
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   469 AA;  53168 MW;  BEE5DAD721FDA823 CRC64;
     MGFVPLLGRL SVHEYIALIV GFSFLALETL LRFIIIVLPK PIIRWFYDRS RFLFHQYGQE
     TKPKPKSREN TISDKILKAK DFGELCELFS YTHEEHVVLT KDGYLLGLHR LPSKKGQRKS
     SPGTSTGKPV VYLHHGLLMN SEVWVCLTEA ERSLPFVLVE QGKRFDVWLG NNRGNKYSKK
     SLYHNPNSTK FWDFSIDDFA WHDIPDSISY ILDTTKAESL SYVGFSQGTA QAFAALSIHP
     QLNEKVNVFI ALAPAMSPAG LAAPIVDGLM KASPTLMFLF FGRKSILSSA AMWQSIIYPP
     IFAKVIDTSL GFLFDWHNHN ITSTQKIAAY AHLYSFASVK SVVHWFQIMR NSAFQMYDDD
     IIPVVRTSVS SYRPARFPTR NIVTPIVLLY GDQDSLVDIK TMLRELPEHT VAKRLEGYEH
     LDILWGKDVD TDVIPEVINA LKIHCIDPGK LKDGVKVYLQ TDSAPSYSE
//
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