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Database: UniProt
Entry: A0A139H7J4_9PEZI
LinkDB: A0A139H7J4_9PEZI
Original site: A0A139H7J4_9PEZI 
ID   A0A139H7J4_9PEZI        Unreviewed;      2442 AA.
AC   A0A139H7J4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC578_4652 {ECO:0000313|EMBL:KXS98349.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS98349.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXS98349.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS98349.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXS98349.1}.
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DR   EMBL; LFZN01000115; KXS98349.1; -; Genomic_DNA.
DR   STRING; 321146.A0A139H7J4; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000070133; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 1.10.287.370; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF02996; Prefoldin; 1.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          369..801
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1673..1750
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1809..1886
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1752..1803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2379..2406
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2442 AA;  265003 MW;  361AB1E02AE08295 CRC64;
     MSNILLFGDQ TAEQYPLLRK VALHKDNVLV HNFVQRCALA LREEARALPQ TQRVLLPDFL
     TINNLIEAYY QKGDKLPALE SALVTIAQLG HYIGYFSEHP SELPAASNTR VLGLCTGLLA
     AAAVVSSKTI DELVSLGVEF VRLAFRSGAA VDAVRSVLGQ TGEEKEPWST IVTGADAASA
     KKALDAFHKE KGIPQSNQAY ISAVSVMAIT ISGPPTTVER FLQHGPLSQN NRVPIPIYGP
     YHAEHLYNDA DIERLFSAKA ARELRSHTPA SLVHSAATGK PIVAENSYEL AKLALGEMLQ
     RPVRWDYLLE ETVSQMAASK QGAKIYAMGV SNTANSLVSA LKAGGQTNVS VVDQSAFVEQ
     QGYNGRTQND KIAIVGMAGR YPNSANHEAL WDLLMKGLDV HRKIPADRFD ADAHCDPSGK
     GKNKSHTPFG CFIDEPGLFD PRFFNMSPRE AAQTDPMGRL ALVTAYEALE MSGYVPNRTP
     STKLHRIGTF YGQTSDDWRE INAAENVDTY FITGGVRAFA PGRINYYFKF SGPSYSVDTA
     CSSSLAAIQL ACTSLWAGDC DTACAGGLNV LTNPDIFSGL SKGQFLSKTG SCKTYDNAAD
     GYCRGDACGT VILKRYQDAI ADKDNILGCI LGAATNHSAE AVSITHPHAG AQEFLYKQVL
     ANAGVDAHEI SYVEMHGTGT QAGDGIEMTS VTNVFAPRHR QRRPEQTVHL GAIKANVGHA
     EAASGINSLH KVLLMMKHDK IPANVGIKGE MNKTFPADLK DRNVHISRDA VSWPRKGAEP
     RKVFLNNFSA AGGNTALLLE DGPIREAPAA VDPRSTLPVT VTARSIASLK RNLINLQQYM
     IENPGTTATS FSYTTTARRI QHNYRVAFPL ADMSKAIDSL QAQVKESYNP VPMAATKTAF
     CFTGQGSQYT GLGQKLYQDL KSFRDDINQL DQLARIQGLP SFLELLDGTD VQTLSPVKVQ
     LGMACIQVAL ARMWASWGIT PTAVIGHSLG EYAALHVAGV ISAADMVLLV GRRAELLVRD
     CTPHTHGMLA VKGSAEAIRA TLGSKMTEIA CINGPEETVL CGSGDVVASA NETLTQRGFK
     ATKLNVPFAF HSAQVDPILD QFKRIASSVT FNKPTVPVLS PLAGEIIREA GIIGPDYLAR
     HARETVNFWT ALTSGQKAKV FDEKTAWLEV GAHPVCSGMV KASIGATVTA PSLRRGEDAW
     KTIAASICHL FNAGVYINFD EYHREFNDAQ ELLQLPTYSF DNKKYWLDYH NNWTLRKGEP
     AEVREVVVEK AVAQPVPAVE IPAKRLSTSC QKVISEEFTE NQAKVVVRSS LADSKLYPVV
     CGHMVNNAAL CPSSLYADMA LTVGDYIWKE MRPGTEAPGI NVCNMEVPKP FIAQIPQPAQ
     GQHIELEANA DLEQGIVKLQ FRSVQPDGKK ILDHAHCNVR FEEKAAWADE WARYSFMVKA
     QIDLLTAKTM NGGAHKVQRG MAYKLFKALV NYEGKYRAMS EVVLDGQNTE ASATLDFPTK
     PEDGDFYCPP YHIDGSCHIS GFIVNASDLL DSEQNVYVSH GWGAMKFSKP LTAGMKLRNY
     VRMLPQPNNI SKGDVYVLEG DEIVAVCEGI KFQQIPRRVL NTFLPPNKGS AAQPAAVAAP
     VKSTPVRAAA PAPIKVAPSP AAVRAPAPAP IKLAAPVSAP KAAKPKKAPA AKKTSGGLVD
     KVMKILAKET EVDMSELVDD AQFENLGVDS LLSLTISAIF REELDMEISS SLFTDNATVG
     DMKKYFAQLD NGSVSSASEP DEDSEDESIP ATDMPTPLDM LSTPASSAPS VAASDAGKPE
     LDSPVRDSLA EVGDVSLARH VVAQEMGVDL SEITDDAELA ELGMDSLMSL TILGELREKT
     GVDLPSTFLS SNPTIKDIEN ALGMRPKAKA AAPAPRPAAT PKTTVVDMNK VSARLAEINK
     TDISRYPPAT SVLLQGNAKV ATKKLFFLPD GSGSATSYVS IPNLGPDVAA YGLNCPFMKD
     PEQWQCGIEV SSLIYLAEIK RRQPTGPYII GGWSAGGVIA YAVAQALLAA NETVEKLLLL
     DSPCPVNLDP LPARLHIFFN EIGLLGTGDP SKTPKWLLPH FSAAIRSLSA YDPKPSIAHL
     PTFAIWCTDG VAGNPGDPRP PPAEDEDPAP MKWLLNHRTD FADNGWAQLC QGPFKNGIMG
     GHHFSMMKDP HAADLGALIR EALDWDGMQS SAQTVRPLPL VNKESFGTDR TKNAEILSHD
     NSCQTHTIHL TCLSKLALPH PLTQMATSIQ NPSSQQEPPT NPRGIPYAPF IDRVEDYVST
     RADVETTLKS FQEMISKYQF MQSNNLRRIA SLKDKLPDLR RTWEMICFLE QKRNCEDPIE
     ATFEVNDTLY AKAHIRDVEE VFLWLGANVM LSYPLPAASE LLQKKISAAQ KSLEDCEEDV
     GFLREQITTM EVATARVYNW DVGMRRKEAA AAAATGKEEL DE
//
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