ID H1V8Q5_COLHI Unreviewed; 1139 AA.
AC H1V8Q5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CCF36608.1};
GN ORFNames=CH063_01529 {ECO:0000313|EMBL:CCF36608.1};
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:CCF36608.1, 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; CACQ02002057; CCF36608.1; -; Genomic_DNA.
DR AlphaFoldDB; H1V8Q5; -.
DR STRING; 759273.H1V8Q5; -.
DR EnsemblFungi; CCF36608; CCF36608; CH063_01529.
DR VEuPathDB; FungiDB:CH63R_07082; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_3_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 3.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 663..739
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1139 AA; 125013 MW; B89746DEC6D863C5 CRC64;
MAARRRLLNH PALQYGLGNI RRVSRDAQVA AGFQTQLNII PQARPLAADS AVLRMEEAFE
VDAQFALSLN CLLHANNRVV FEADFDPVTL PASQMRRIFR QFVFTLSWLL RVPRETTTIR
QFSPLNPGDL SEILDWNRNV PDSSDECLHN LFKARARQQS SAPAVVAPDG TLTYAELDDM
SDRLAHHLRL RGVGPEKKVP LLFGKTMWSI VSFLGVMKAG GVCVPMDPSH PRRRIQDIIT
RCHACLVLTS KHTEAIVVDY IPTPAVEHFT VSAESLGALP SHTSLLLPQE EEPSPANAAY
ILFTSGSTGN PKGVVLEHRN LASTLTHYGR RVGWEASGGC RVLQFSSFVW DTHTLEVFGT
LLWGGCVCMP SEAQRADLES FIHDKAVEWV ILTPTVLRTL DAHAPEVATV RTVVSCGEPV
DLSASVGKPV DCAVWIVSLQ DPTQLAPIGT IGEIIVQGPG VARGYLDDEA LTTASFVSRP
SWLPPDQPRC DRARRFYCTG DTARYNADGS MTFTGRRDGQ VKIRGQRFEL GEVERALVRS
AGVREAIACV QPWRDSGSTL TAVLSLDDTE TELEGGTGEH PLRQVSMPTG YDLPRRLRDI
RDDVAALLPS YMVPEACLVV QGMPLTTSGK LDRTSVITWV QSQDMEAARA AFQPASAADV
LTAPASDREK LLRSVWASVL DIPEQEIGRE SNFLALGGDS IAAMRAANLL RKRGLVVPLQ
ALVQSSNLAA TTDHCEAVTE LPRPAAGPLQ PDDTPAVQDV RVEGFASTDI EAVAEATDAQ
ASMVALGELD PHALVLKTGL VFERGVDRTR IEHACRQVLQ HHGILRTVFV QRGPKLYQVV
LKRPADSQIQ PDCEDGSNRQ HDDILTRFYV ASDSQHCCCY RLRLEIHHAL YDAVSLDLVW
KDVAAAYAGR KLSDGTSFLE WAGRLARLDH SRAKRFWREA LQGSRLTYLV PPRQAPGTIR
QVTLQVPLRS LEVPGVTTAN LFAAAWALVM GREAGTQDVV FAEILANRYS PSVDMDQETV
LGPCMNTNPV RARFDSSMTF VSVATRLQEQ SLAAAPFAYL GYRTIQKDCT DWPLNSLFGS
VVNFQSPRAG VVGKQTDRHQ SMDVQGTYRF PKPSSGETGA GGLFHHVALR EPGPFRRGS
//
