GenomeNet

Database: UniProt
Entry: H1VX96_COLHI
LinkDB: H1VX96_COLHI
Original site: H1VX96_COLHI 
ID   H1VX96_COLHI            Unreviewed;      2495 AA.
AC   H1VX96;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CCF44858.1};
GN   ORFNames=CH063_00531 {ECO:0000313|EMBL:CCF44858.1};
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:CCF44858.1, 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).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CACQ02007235; CCF44858.1; -; Genomic_DNA.
DR   STRING; 759273.H1VX96; -.
DR   EnsemblFungi; CCF44858; CCF44858; CH063_00531.
DR   VEuPathDB; FungiDB:CH63R_13251; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..426
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2406..2485
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          36..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2495 AA;  272530 MW;  EE713770050DC603 CRC64;
     MSVPEPIAIC GIGLRLPGGI DTPTSLYNFL VNRKDARSKP DKPRYSSQTH HFTESGTTRP
     LPTEEGYWLT HDDVTKFDPS MFSMNPKELS KLDPQQRLLL QVVWEALESA AETDWQGQRI
     GCYVGSFGDD WREMHAVDTQ DDGMYRLTGY MDFVQANRIS HAFDLRGPSM TVRTACSAAG
     LAVHLACQAI RAGECDSAVV AGSNLMLSPG FTKLMAEQSV LSPDASCKTF DAGANGYARA
     EAVNCLFVKR LHCAIRDGNP IRAVIRGSAT NSDGKTLGLT TPSAQAQQQL IRDAYRQAGI
     PESDMWQTAM VECHGTGTAV GDTIEACTVG TVFGEKGMLI GSVKPNLGHS EAASAITSIV
     KAVLSLETRT IIPNIKFENP SISILFDTSG LKVPTEPLPW PEDRAERIGV NSFGIGGTNV
     HIIIDSSASV AYPTAVRGPG NVDTPPPSPP LRRESATLLL FSASNEESLK KAVRGYQNII
     QANPLKLEAL AHTLTHRRSH LAYRTFAVVA GESGNMAPEF PPAPTFRPKS ESKDITFVFT
     GQGAQWARMG SHLMKASKEF LQDIREMDAA LKCLPREHQP AWEISRELMR ADAGSRLGEA
     EFAQPVCTAL QVALVRHLAR YGVSPKAVVG HSSGEIAAAY AAGTLTIKEA IIVAYYRGYM
     AKKLEKRGAM AAVGLGRDQV TRFLTTGVVI ACENSNSSVT LSGDLDVLRA VCEDIHAAKP
     DALVRILKVD KAYHSHHMKS IGAEYQALLK SHLNPKSPKI SFYSSVSPHT PLRGADFGPE
     YWQRNLESPV LFRQAVTRLL QTSSTSLLLE VGPHSALAGP LKQICSENSI SPPYVAAQKR
     GLNSAASFLA AVGELHCRGA AVDFPVMDGV RPLTDLPRYP WNLSKTYWPD SRITNLWQFP
     EYPPHELLGH RALETGNAEP SWRCCLSLDK VPWIKDHQVG SDIVFPAAGY VAMAGEAVRQ
     LTEHTGFTIR EMRIMNALVI SPGKAVELLT SFRRQRLTHN DVSEWWELTV QSCSSADTWT
     THCTCLIKGG NDLEVRNLPG LHKASFLRVT EPSRWYKQMS RVGYNYGPLF QCMQMVRSSV
     TSPAVEVEIS DCRVGGSAAQ SYAIHPTTID HVFQSLVVAN SSGEPRQLDK LYLPTYVEEI
     TINAKTETRG CLIQTLKTGR DGYCQGESIG FVPGNPTGQP LVHMKGLQFS PIDIVDSTKH
     SPDTSKVTHL VWKPDVDLAA STDLIQPTSP DDFSKFHGLL EDLFILCGLA TLREVGVAGV
     LSEQTQPHLR KHYQWLESHI VRSSRAWPAL TTVEIHNKIR DISLQLEKTP ASAVATLISR
     CYTHAQSLFS SDIGPLELFL QDNALHELYD WMNTLFTYKP LLQLLSHKRG RHLRILEIGA
     GTGGLTARIL KCLTECFDDG KALGKYVFTD VSSGFFPAAK ARFETIPEGF LDYRVLDISH
     DPADQGFGGE QYDLIVASNV LHATPDLTKT LQHVRTLLKP EGRLLMHELC CDTKWINFIM
     GYLSGWWLGE SDSRIDEPYI SPDRWEERLA LAGFEKPDVF YDAEQQHRLN ATIVARPAHS
     TSKMPSLSGE ITILCEEESH PVVVDLRNHL QKQGHSVTCT TLSAGNIQPC APVVSAVDLC
     RGDGYFHDMT QGKLDDFKRL LQKLQSNNLG LLWLTRPCQV DPQNPTFAPV LGVARTCRIE
     MGFPFSTLEV DGDGTDALTA VSRVLQKTLL RHGSSKLTHD EDAEFSYSSG RIFVPRCKWL
     PISRALQDTT SPSPSKMLHI SRTGALQSLC WIPRRLSDQI PSDQVQIKVH AAGLNFKDVV
     TAMGLIDPSS PKGLGCEASG VVTATGSLVT NLRIGDRVMV FAPQAACFST DIQAPAQLCV
     RIPDELGFAD AATMPCVFVT VLRALLDKAG LQAGQTLLVH SAAGGVGIAA MQVARWIGAT
     VYATVGSEEK VDFISKTWNI PREHIFSSRD SRFVEGIKTA TGGRGVDVVL NSLAGELLHA
     SWECVAPHGT FIELGKRDTL AGGRLAMEAF DGNRSFIGVE MANLAAQDPG IIARLLQRCI
     QLYKQGHITP VRPSRMFSCR EAEDAFRHIY KGTHVGKVVI DMQKAAVETL DVVPRQLPAP
     AFCNEATYLL VGGMGGLGAS IARWMACHGA RSFIFLSRSA GNSAVDQDLL AELRGRGCEV
     EAVSCDITNE TELHAAASRL PLWKRIRGVM NLAMVLSDAA LPNLTLSQWE TATSPKIRGT
     WNLHRVLPSD LDFFVLFGST SGIHGYPGQA NYAAANTFLD AFVQYRRRHG LPCSVLDLGG
     VEDVGYVSRT REVEDAMKKA GSKLLSESNM LRGLQLAMAQ SLSGDAGLES AIAGLGFGGQ
     VLIGLECSIP LDDVNNRVVW KQDPRMVLYP EDSDTPTRDG KQSGASGLSE FLARLQSKPE
     EVDTPSSIAY LAQEIALRVC GFLMKEVDET GVDTSVSPSA LGVDSLMTIE IRNWWKHSLG
     GDISVLQLTS AQSFDQLGHL AAKQLKKKMD LAANI
//
DBGET integrated database retrieval system