ID R7SR55_DICSQ Unreviewed; 464 AA.
AC R7SR55;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE SubName: Full=Thiolase-like protein {ECO:0000313|EMBL:EJF58428.1};
GN ORFNames=DICSQDRAFT_182527 {ECO:0000313|EMBL:EJF58428.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF58428.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF58428.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF58428.1,
RC ECO:0000313|Proteomes:UP000053319};
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; JH719435; EJF58428.1; -; Genomic_DNA.
DR RefSeq; XP_007368789.1; XM_007368727.1.
DR AlphaFoldDB; R7SR55; -.
DR GeneID; 18841189; -.
DR KEGG; dsq:DICSQDRAFT_182527; -.
DR HOGENOM; CLU_035425_0_1_1; -.
DR OMA; PSLYAMM; -.
DR OrthoDB; 1799125at2759; -.
DR Proteomes; UP000053319; 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:UP000053319}.
FT DOMAIN 12..200
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
SQ SEQUENCE 464 AA; 50211 MW; 8AB1125E864051DD CRC64;
MPSNVKGQRT FIIGVGCTAF IKPRGLRTTE EMGLEAATKA LLDAGITYDA VQAAYVGYCY
GDSTAGQRAL YQLGMTGIPI TNVNNNCSTG STALYNANTL VKSGLYDCAL ALGFERMARG
SLGSNFPDRE PPTAVFNTAS IELEETLSSG KNHGPGAPRM FSNGGQEYFD KFGGNINHLA
QIASKNHKHS VNNPYSQFRD GWSVEQVLAA PKITEQLTKF MCSPTSDGGA CCIVASEDFV
HQHGLENQAI EIVSQALTTD DPSTFETRSA MNVVGYTMSK NCADEVFAQA GFKDGEGRDQ
VGVVELHDCF AANELLTYDA LGLCEHGQAH KMVERGDNTY GGKYVINPSG GLEAKGHPLG
ATGLGMHFYI TMQLRQWAGP MQAPGLFDVS DKRGKFGLIH NIGLGGAVVC SLLRRPEFYK
EGGEDGRKRL GYNHGHEYRP ITREDVDKVK AQMNSPYILQ RAKL
//