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Database: UniProt
Entry: S7QNU1_GLOTA
LinkDB: S7QNU1_GLOTA
Original site: S7QNU1_GLOTA 
ID   S7QNU1_GLOTA            Unreviewed;       459 AA.
AC   S7QNU1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Thiolase-like protein {ECO:0000313|EMBL:EPQ61188.1};
GN   ORFNames=GLOTRDRAFT_69476 {ECO:0000313|EMBL:EPQ61188.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ61188.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ61188.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ61188.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982}.
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DR   EMBL; KB469296; EPQ61188.1; -; Genomic_DNA.
DR   RefSeq; XP_007861414.1; XM_007863223.1.
DR   AlphaFoldDB; S7QNU1; -.
DR   STRING; 670483.S7QNU1; -.
DR   GeneID; 19307984; -.
DR   KEGG; gtr:GLOTRDRAFT_69476; -.
DR   eggNOG; KOG1406; Eukaryota.
DR   HOGENOM; CLU_035425_0_1_1; -.
DR   OMA; PSLYAMM; -.
DR   OrthoDB; 1799125at2759; -.
DR   Proteomes; UP000030669; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00829; SCP-x_thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020616; Thiolase_N.
DR   PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669}.
FT   DOMAIN          7..233
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
SQ   SEQUENCE   459 AA;  49484 MW;  2BF2C20C0EEFCD65 CRC64;
     MGRRSFIIGV GCTAFIKPRG LRTTNEMGLE AATKALLDAG ITYDAVEAAF VGYVYGDSTA
     GQSALYPLGM TGIPIANVNN NCSTGSTALF QANNLVKGGL VECALALGFE RMNPGSLGTV
     YKDRESPTVL FNQRSQELEE GMSAGANFGP GAPRMFANAG QEYFDKYGAN IDHLAQIAAK
     NHKHSTNNPY AQFRNGWTKE QVLQAPKITK QLTKLMCSPT SDGAACCIVA SEDFVHKHGL
     ENQAIEIVGQ ALTTDYPTAF DTRSAMDVIG FGMTRACADK AFQQAGFGVG EGRDQVGVIE
     VHDCFASNEL ITYDALRLCT TGEAHKLVER GDNTYGGKWV VNPSGGLEAK GHPLGATGLG
     MHFYITMQLR NWAGPMQAPG LFDVQDKRGK YGMVHNIGIG GAVVVSLLRR PEFYKEGGTD
     GRQRLGYNHA HECKSITRKD VDKVKARETS TYVLEHAKL
//
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