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Database: UniProt
Entry: A0A1V6QCK3_9EURO
LinkDB: A0A1V6QCK3_9EURO
Original site: A0A1V6QCK3_9EURO 
ID   A0A1V6QCK3_9EURO        Unreviewed;      3928 AA.
AC   A0A1V6QCK3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSOL_c081G11659 {ECO:0000313|EMBL:OQD86944.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD86944.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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:OQD86944.1}.
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DR   EMBL; MDYO01000081; OQD86944.1; -; Genomic_DNA.
DR   STRING; 60172.A0A1V6QCK3; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19532; C_PKS-NRPS; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; IPR045851; AMP-bd_C_sf.
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; IPR013120; Far_NAD-bd.
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; 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; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-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; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..437
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2351..2426
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3490..3570
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2436..2497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2467..2482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3928 AA;  429907 MW;  86323C2B1F556D28 CRC64;
     MSPSHNEPIA IVGNACRFPG DATSPSKLWE LLKEPREVAR PIDRFAASSF YHQNGHYHGA
     SNVRDAYLLS EDPRYFDAQF FNIPPGEADS IDPQQRTVLE TVYEAVESAG LVLEDLRGSD
     TAVYVGVMCD DYGNICYVDQ EAVPTYAATG TARSILSNRV SFTFDWRGPS MTIDTACSSS
     LVAIHQAVQV LRSGNSNVAV AAGANLIFSP NMFIAESNLN MLSPTGKSQM WDANANGYAR
     GEGIAAVIMK RLSDAIRDGD HIECVIRETG CNQDGHTPGI TMPSHEAQTK LIHDTYRRAG
     LDLSKPEDRP QYFEAHGTGT KAGDGVESKA IYHAFFPEGQ TTDESLWVGS IKTIIGHTEG
     TAGIAGVMKA SLAIQNKTIP PNLHFKTLNP EIIPYYGKLQ IAKIAQDWPA LPAGAVRRAS
     INSFGFGGTN AHAIIEAYEP EVCPVQAEAV VKAAIALPLT FSATSENSVT NLMTKYLEYL
     TENPDADLTS LAFTLHDRRS TFAYRSHIAG QSVEEILPKL QNAAEEQQSG NSASIIRGTS
     AKKHLLGVFT GQGAQWATMG RELIRASKLA QDIIGKLEQS LAELPASDRP SWSLMEQLMA
     DPAQSRIAEG ELSQPLCTAV QVVLVEVLKL AGITFDVVVG HSSGEIGAAY AAGFFNATDA
     IRIAFYRGRY AFMAKGPEGQ KGGMLAVGTT LEDARELVEL PSFEGRVSVA AYNSDASVTL
     SGDLDAIEEV KEVLDDERVF NRQLKVDTAY HSHHMIPCSA KYYEALDNCK VQILKPSGET
     KWYSSVYDGK LMEPCEELKH TYWVDNMVNI VLFATSLESA LNNTVPQPTQ VIEVGPHAAL
     KGPASNVIEE VVKAALPYTG TLARGQNDVN AVASTLGYLW AQFGRSSADW KGYSQVFSSS
     IPTILQELPS YPWNHDRLFW YEARKSRVNR LRQDPAHVLL GTRTDSINER EYRWRNYISS
     KEIPWLSGHS IQGQTLFPAA GFLVMAVEAA RVVGRDQAIH AIELQNSQIH RALAVNEDKG
     IETLFTLSNV TSVQTGAGTS TVTANFACDA CLQKGSDVFT SIASGKLIMS LGTPSSSALV
     EYPKEAGLGM LDVDCEEFYA YLASIGYNYA DLFRGITSMS RCCDLAQGEI ITSTASQSGP
     MDEFLLHPST LDVAFQAIFA AISYPGDGAL WALHIPTTIR RVVINPVICP MKGGLDEKVR
     FSATSNRADD GTFSGSVDIF PVHSDHSLCQ VEGMEVSPVS PPTAKNDRHM FGHTSRWLST
     PDAEAVAKPV SITTEQEQEH QLLDRLALQE LRKMVASGNS EHAHLRTWAQ GVLKVAGTDA
     STGQNDNSSV TVDEASAADL AVLKALGSDE SGLLNKFYAS AFGAAEARSS LISLVHQISR
     RYPHMHIMEL SAGNGAATKP LLETLGALCS AYTVTDSTDE HFAALNKEHG DDLFTQTLDL
     DQDLEEQGFS AASFDLIIAP AGLHNVQDRA QTIQKLRWLI RPGGFLFVQQ ITNASAAHVG
     LTVASLASQT EVPELSEYDA LLQDAGFSGI DSVTPDSVSP FSVFVSQAID AQINAIRAPL
     TAGNKTTIDQ ILLIGGRRFQ TSRLIDNIKN ALAQYCDNIT SIQSMREFKP SLLASRPLVL
     SLTELDEPFF QDLTDQKYKA LQTLFFRSRY IVWATRGANG DNPYANVMKG VVRCLLIEIP
     HLHCQMFNIE GKVKIKQHAT ILAEQLLRLH IADGWKDKIP AYSALWTSER ELMLVDDKLH
     ITRYDSEAEL NDHYNGLRRR VVADVSTADR VVAITADRML QQFRLNPQAP IGVEEAKVSV
     NVEKSLSTAF KVGDLGYFYL SIGTNKETGE TVLALTDQHQ SLLTVPESRL LAVNVAASER
     RTLLVSVGAT LLASALLEKS TASDRLVFHE APTILAELLR EKARKTGAQV VFTTTDKETT
     DYWQHVHAYT PGRELSRLVQ ANTSLFVNFS PASEGSEVVN RLKAQLPFRA RCRTLSDYLP
     SQSVLYSDTT EAQLAKALKD AHDNAVSEAS SVAFGQVANT FVQQLAADQT LSEPLTTMDW
     TDPTPFLANL TLAMDEVRFR SDRTYFLVGM TGSLGLSTCE FMMERGARHF ALSSRRPNID
     QRWLDKVETK FGASVKAYPL NITSRESLQG AYKEICATQP PIAGVANAAL IMRDGLFMES
     NATTMNEALG PKIDGTIYLD ELFANVDLEF FILFSSLVYI TGNIGQTSYA AGNGFMVSLA
     HQRRQRGQCA SVMNLGGING IGYITRTDHN ILNRLDIMGY GIMSELDYKY FFAEAVMAGP
     PDSGRDPEVS AGLKFVNPKT DKNPPKWWED PKFSPYVIDK SAREGGGKGA EGVLSTKAQL
     QEAATDKDAF NIILTALQAM LHKKLDLPPS QSVLSDVAIV EMGVDSLVAV DMRSWFSSEF
     DHDIPIIKIL GGATLADLVE DTVANLSPSI APNLGGAAAA EEEPNVEAET PAEACTAAPS
     DDEPISSDDY TPATTDIDEG SVTGKSSADE KVETDAAPGA PAVVRPDFFR VEKMTPGCSR
     FWFLRQYLED ASCFNIIVRT RLTGQVDVAR VQEAVRKVGA RHEALRTAYY VDEEGEPMMG
     VMPDSKLRLE VSKITHESEA EKAHKEVSKY NFNIENGEVI RMQLLTVGPR EHHLIFAVHH
     IAIDGFSFNL MIRDMDMFYQ GKPVPQIASQ FTDLAIQQRK DIESGRLQDD IVFWKDKYTT
     LPDPLPLFPF PGVGGRLPQT KYEHEEVEMV LDSAIAQKIR ILCRQNHCTT FHFFLATFRL
     FLTRWLEIDD LCIGIADANR KDIKTLATVG FLLNLIPLRF GGLTGKETFS TLLNAAKQTS
     YSALNHSALP FDLLLQELEV PRSSSHSPMF QAFLDYRQLA LKTPPMLESQ TEGESNFGAT
     AYDVVLDITD DAASDITIKW QTQKSLYNGR HTQAMMDSYM RLLHHCAKGP AGSIASAPLY
     RDEHVAAAIK AGRGPQFDSQ WPETLSFKVD QVSAQFPNDI ALRDGLGDSM TYKTMDRILD
     QISEQLVQAG IQPGDKVGVF QQPSAMWICS LLAIWRSGAV YVPLDPRNGL PRLAATCGIV
     DPSSVLCDSS TAADVAQLAL PAGASTINVD QVRQANKSPA RRPNLSKGDS SAIIVSSSGS
     TGVPKGIEVR HLSLLNLFEG DSQIWNLGRP NTVQQSAYSF DISLDQIFTS LVNGGNLYVA
     SQAQRSDPQA MAELIANNQI TYTMATPSEY SNWINYAAPT LSKATGWRRA NVGGEGWNAT
     LRDSFATLNL PNLKIQNCYG PAENSVWCTR QPIAYPAEST LIPAGPALPN YSFYIVDKQL
     NVVPTGVQGE ILIGGAGTAV GYYKRTDLTN EKFIEDKNAS SVHVAKGWNR AYRTGDKGYL
     MIDGTLVVLG RITGDTQIKL RGFRIELEDI EATIVRASNG VLSRVVADVR GEGQESYLVG
     FVEFADGYLT DQQKTYLAQL LNQVPLPQYM KPNMLIALDR IPLNSHGKVN RLAIATIPVQ
     SQVDDAEIST EVTDTEKAIW ELWQEILPQS VLDGVVINLN HDFFQLGGNS LLTVRLQSRI
     REAFGIVVPL PKVMESSKLF ALGALLDNLL ANSGINWDLE TALTDDMLQI PPADASSTTR
     KNAQPLTVIL TGASGFIGRH MLERLIQDPK IGRVHCIAHR LLSDELPHRQ KFNAVVASSS
     KISVHEGDLN APRLGLSETE FAALAQQADM IIHSGANRSF FTTYDQVQAI NVQSTKELAL
     MSAASLRDHR RVVPFHFLSG TEAATIKPAS DGSQGYVASK WASERFLEKY AAQLRLPVHV
     HRQLPVPEGR EAQGEELDQI LQEFVDVAAK MTELPNSTTW GGHYDLIPAD RLSRDIVGHA
     FTALASTDNQ ISSDNVKQYS HLSSVRMDIA KVVERLGSLP EYAQSDRPKI PAHVWVGKAK
     IAGFRYQFST MDMVLQDAEG KGLATLSR
//
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