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Database: UniProt
Entry: H1VUJ4_COLHI
LinkDB: H1VUJ4_COLHI
Original site: H1VUJ4_COLHI 
ID   H1VUJ4_COLHI            Unreviewed;       603 AA.
AC   H1VUJ4;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CCF43903.1};
GN   ORFNames=CH063_13473 {ECO:0000313|EMBL:CCF43903.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF43903.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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DR   EMBL; CACQ02006464; CCF43903.1; -; Genomic_DNA.
DR   STRING; 759273.H1VUJ4; -.
DR   EnsemblFungi; CCF43903; CCF43903; CH063_13473.
DR   VEuPathDB; FungiDB:CH63R_14371; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_453142_0_0_1; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE   4: Predicted;
FT   DOMAIN          71..391
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   REGION          447..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CCF43903.1"
SQ   SEQUENCE   603 AA;  64956 MW;  19A57A4D9D29CFDD CRC64;
     MDVLKSFLLD RDEYGNPRRP LASVAYHIAR THNPAFDRRV AFVAHDAQDA AATLATASPA
     VVAAKRPVVL CFGGQTGRTV SVSKALYDDS DLFKSHLDKC EAICSNLGVS IYPAIFQNQP
     VDDTVTLHCM LLSLQISCAQ SWIDSGLQVD TLIGHSFGQL TALCIAGSLD LHDTFRLVAG
     RARLLRDSSA ILQDRGAMLA VECDTADLDD IVTGVRTAAA GHRVDVACYN GPRNFVLAGD
     IASIAAATDL CRRHGRVKTT KLQNDHAYHS YLTDVILPDL RELAASVTVR PPRIRVETCT
     ADATWPSSFG PDEVVEHTRQ PVYFDQAVAR IAARLPXAVW LEAGSATPII PMARRVLSST
     TTQNKPRSAD VFIPVNLGTT VDAAAQLAKA TCDLWTAGSA AQYWLFHSSS GYRYQEDFNV
     PPYQFEKSSH WLPFEAPAXA PVATGAKPEI VSAPSPDSDP EAEPETHFPP GFVTRVYPGE
     AAVPGEHLFV VDTQGPLFQL AARGHAVTGQ SICPASMFVE MVARATMLVP KKPSTRRGGG
     GQVPSLSDLT MSAPLGIGNS QTTVIRLPCQ RNLFLDARRR HLRREAPPAA RPPGVLAAQD
     GXX
//
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