ID A0A0D2JRZ2_9EURO Unreviewed; 2148 AA.
AC A0A0D2JRZ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z520_08005 {ECO:0000313|EMBL:KIX96227.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX96227.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX96227.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX96227.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN848078; KIX96227.1; -; Genomic_DNA.
DR RefSeq; XP_016630350.1; XM_016778502.1.
DR STRING; 1442371.A0A0D2JRZ2; -.
DR GeneID; 27713751; -.
DR VEuPathDB; FungiDB:Z520_08005; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000053411; 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 GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 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; IPR049551; PKS_DH_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; PF14765; PS-DH; 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; 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; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..807
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1633..1707
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1755..1832
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1596..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1715..1749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1843..1859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2148 AA; 233212 MW; C5890E9AA90BC984 CRC64;
MGRDIKVLLF GDQSEERFDD LRDLVTVTDN PLLSSFIEKA YFILRDEVTH LPHVTRGLPG
FTSIETLLWR YREAGVRHPA IESALVCIHQ IGTLLRYYGD GSEIYPKPED TRLVASCTGL
LSAAAVSCAR TYRELVSVGL EALKLAFRVG AQVTEVCEEI EQTSLPSSWA AIFPGVGKES
AYLALDDYYK KTKIPPTSRP YVSATSTNSV TISAPPGDLE RLIEDGIFKS CRPIRLPIFG
PYHAPHFYSD ETVVSLATSI EGESTGQWKA RIPIINNGKE YAYDASNFRQ LVEDVLEDIL
LKPLHWDRLC TNCVASVSSA EPEQCRVVPV GAKNASASLV NALNHKASFK IVVDNRKTEV
TDEPKEPKPI GGLGKPKIAI VGMSGRFPDA MSPSLFWDLL KKGLDVHREV PPDRFDAQAH
YDPSGKRRNT SHTPYGCFID HPGLFDARFF NMSPKEAAQT DPMHRLALLT AYEALEMSGF
VPNRTPSTMV DRVGTFYGQT SDDWREIQDG QNIQTYFIPG GVRAFAPGRI NYHFGFSGPS
FSVDTACSSS LAAINIACNS LWLGDCDTAL AGGLNVLTNP DIFSGLSRGQ FLSKTGNCKT
FDDAADGYCR GDGAGTVILK RLEDAEADND PILAVILGTG TNHSADAVSI THPHAGAQEY
LFKKVLTECN LDPHDISYVE MHGTGTQAGD AIEMESVLGA FAPANRQRPP ERPLYLGSVK
ANVGHGEAAS GITALVKILL MLENELIPPH CGIKGSINHN FPDLGARNVH ISLGRETPWK
RPQGGKRRMF LNNFSAAGGN TSLLMEDGAL PTFDGEDPRS TAVVAVTGKT KKALVDNTKN
LIGYISDKPV DLPCLSYTTT ARRVHYSYRT IVTGSDLAAI KSGLQKSLES EPTSVPSGVQ
MVFAFTGQGS HYTAMGKQLY ETNNQFKADI RRFDLLARNQ GLPAILPLVD GSTEIEKLSP
VVVQTGAVCV QMALVRLWRS WGIKPAAVIG HSLGEYAALQ AAGVLSINDA VFLTGTRAKC
LEQHCTMNTH AMLSVAASVQ ELEEVVDGKT LEIACINGAK ATVISGESSD IDKLKEQLSS
KGMKCTKLAV PFAFHSAQVE PALDDFEAAA AGVTYNAPKI PLIAPLLSTV IRDGGTVNAE
YLRRHCREPV NFLGAIQAAK DKGIIKDKSQ FLEIGSHPIC SGMVKSILGP TTVALPSLKR
DEDVYKTLTA TLCGLHYAGL TINWDSYHES FPRCQQTLKL PAYAWDATNF WINYENNWTL
TKPNLAPISE GEQPKKLSTS TVQRVVEEKF QDQTGTLTTE TDISKPELEE TIKGHLVNGS
ALTSSAVYAD MALTIGDYVH RKLQPEIDKF ALNCANMVVE KPLIFKGSEQ LLRVDCKADL
TQGTCYLTFY SVGPKGQKLM EHAHCEVQYG DAERWSTDLA RQKYLVQSQV DRLLQMGQNG
VLSRLQRKMA YKLFSALVDY QNAYKGMAEV ILDSPLREGT AKIELQTSSA GTFYIAPYHI
DCLCHLAGFI MNANDELDSS QTVYVNHGWD SLRFFEKPSP SKQYRSYVRM QPTGPNSKDY
SGDVFVFDGE GNIVGQIGGL TFQFLPKQVL DRVLPPPGGS KAAAPAATKT AAAEPKKAAP
KSPPKPKAAP AGPSVMSRAL DIMAEEIGVP VADLTDDTDL SALGVDSLMS LTISGKFREG
LDIEIPSTLL ADSETFKQVK DFLSQFESKD AGAAPPSPSS ASSVGSTELS GTSTPAQADT
ESMTSASQAD EKPAGKDDGK LDAIRAAIAE ETGMDPSEVT SDMDLEAVGI DSLMSLQILG
SLREDKGIDL PPSFFSDHST FGEIEKALGG GKAEKPKLPS KSEDMSTEQV VAEMQTNKDQ
KSAEPPKEQQ SAPAAGTSKA FKASSVLLQG NPKTATKTVF MFPDGSGSAI SYATIPPISP
KDVALVALNC PYMKEPEAFE GGIPGVTALY LEEIRRRQPK GPYILGGWSA GGICAYEACL
QLSAVGETVE KLIFLDVPCP LPPQALPPRL HHFFDTIGLL GQEGEAPSWL IPHFTATIKA
LSSYRPRLMD PAKEKIPNVY TIYAQDGVCK NDDDPRPELT PDDPPHMNWL LFNRKDFGPI
GWEKLFGGSD NIIGLDPVPN VNHFTMMREP MVKELPSRIQ KALDVTGE
//
