ID A0A2C6ACU1_9HYPO Unreviewed; 2073 AA.
AC A0A2C6ACU1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDD83_5136 {ECO:0000313|EMBL:PHH89840.1};
OS Cordyceps sp. RAO-2017.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH89840.1, ECO:0000313|Proteomes:UP000221130};
RN [1] {ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHH89840.1, ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|EMBL:PHH89840.1,
RC ECO:0000313|Proteomes:UP000221130};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH89840.1}.
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DR EMBL; NJEV01000258; PHH89840.1; -; Genomic_DNA.
DR STRING; 2004951.A0A2C6ACU1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000221130; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic 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 Gene3D; 3.30.70.3290; -; 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; 2.
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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000221130};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 145..450
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT DOMAIN 514..678
FT /note="Polyketide synthase dehydratase"
FT /evidence="ECO:0000259|SMART:SM00826"
FT DOMAIN 1363..1656
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT DOMAIN 1988..2060
FT /note="Polyketide synthase phosphopantetheine-binding"
FT /evidence="ECO:0000259|SMART:SM00823"
SQ SEQUENCE 2073 AA; 227376 MW; 0A9C57A2B9782AE1 CRC64;
MHFGLSQKVI VDSAASFGVA GTAAASTAVT GHPEEEHGSG AEVDKQLETL VNGDGAKAGK
TTKEQVSRLL PVSANNDTSL QSRVRALQAY IHSRSAPLAG IAYTLGSRRQ HLSHRTFVVA
RDGAGLPEFG QLQKASPSAP CVAFVFTGQG EQWFGMGKEL IHNSPSFEAD IRSMDMALQS
LHDPPSWSIQ GFLRCEQPEH LVHRAEYSQP LCTALQVALV NLLAKCGISP GAVVGHSSGE
IAGAYAAGTI TMAEAISVAY YRGLAAKSQA RQGCMAAVGL GREAVSPLLA DGAVVACENS
PGSITISGDV EAVERTLELI KYKNPEALAR KLSVDKAYHS HHMREVGQAY EASLLQKPIL
PEQPRVRFYS SLTGQRAEED VLFGPAYWRQ NLESPVLFRD AVEALLDDLG QSPLFLEVGP
HGALREPVRQ TVAGRSTENM AYITTLTRGS DCFVDTLAAL GRLYAHGCDV NFAFLNPPAP
VLTDLPAYPW DHSQKFWTED RLTRAWRYKQ ERHHEMLGSR CLESSDIEVS WRNVLEASDV
PWLGDHKIVN DIIFPCAGYV AMMGEAIRQT TGSESYTLRN MVVKAALMFE ASETVELMTR
MKPVRLTDSA NSSWSDLSIM ALRKGTWAEH CVAQGKAGQQ KTLPRREPVH YPRRVGKASW
YERLAQLGLK YGPRFRGMQR ISSHTTETRA VAEIETETHA REARYAVHPT ALDACLQLFT
VSIARGLSRH MVTLCVPSAM GSISIKPADS RLKAEAVASA TPRGGIKGDV AVVAGADDVV
VQIQDAIFRP LDSPDSVEDS APPSNARLEW RPDVDFVDLG STIRRTTDKR KAKIWLQRVT
ALCILRALDA LQSLDVPAGY LAKYVDWLRI EKRCMLDDEW AFMVPEARSW AELAPGSIET
LMPAILGDFG SVWDPNTRRC TQLLLKMSTP DNIRAVFQDD MHPLNLMMED SLLESIYTFH
TDLRDTGELI SLCAHAQPMM KVLEVGAGTA TSTLNVLKAL VSDDGTCMYS QYIFTDISAG
FFAAAADKLR QYPNIDYKVF DIAKDPAKQG FEPASYDLIL ADNVVHVAPS LQEALRNLRL
LLRPGGRLVL GELVHRATFK VTRFATGLLP GWWAGEADGR HDGPLVSAER WDDELRLAGF
SGTGTVFLDD DSPYQVSFVM ASTAVEARKA DVGLSDVTFL YRGFKHEFAL ELAARLAQEG
IDIHWSQIGS NEAIDGRDVV STVDLEGPYL HDISKTDYDR LVAHLSKLTS STLWLTRAAQ
VESVDPRYGL TIGLARTIRT ELGLRFSTLE LQSLGPDAVD ASAAVFHKLR RPSPSAHLDA
ESEFVFHDGA VLIGRYRWVR STDETQVEVR ADFPSRLVVG RYGQVDSMRW VQYPRPALEA
HEVELDVRCV GLNFRDLLLA MGIVDDRKDS MGVEAAGVIA RVGSAVRHVK AGDRVMAIFN
SCFSTRTAIP AQLVALIPED LGFEDAATMS SSILVQSACG GVGLAALQIC KTVGAQVYAT
VGSEEKIQHL VDNYGITRDR IFSSRDSSFL QGIMQATNGR GVDMVLNSLS GELLQAAWQC
VAKHGKMMEI GKRDFIGRGQ LMLDPFEANR SFYGVDLYTI LTDRPELSCQ LLNQCIRYYK
EGHIKPIRPI QVFPAQRAAD AFRIMQRGQH LGKLVISMPG LEETKQMTTT AFARPGAALS
DNFTYFMVGG LGGLGKAVTR WMVERGARHF VFLSRSAGQT SEDQEFLQEL ESQGCHAVAV
AGSVVEQADV ERAIQAATTP IAGVVHLSMV LRDGPLFEID HANWAHVTGP KVIGAWNIHN
ALANSKLDFF ILFSSVAAAV GQPGQANYSA ANSFLESFAQ YRRGLDLPCS VISLGVMQDI
GYISGSSRLR NQVRSTSSHI IQEGDLIEAM DIIIHQSRPS CASTGGPHAA YMYCNMGQLM
VGLRSTKPLS DPGNRTIWKR DVRMSRYHRL EVADERGTGP QGNQLDMLLD SVALNPGVLC
NPETLEVITW GIGRMCCQMM MWPKENLDVN MSIVTMGVDS LVSIEIRNWW RRTFGVETST
LKILGAGTIE NLGAMALASL KEKHDVKEDL DQE
//