ID A0A1V6U1P8_9EURO Unreviewed; 3958 AA.
AC A0A1V6U1P8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSTE_c001G00730 {ECO:0000313|EMBL:OQE31773.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE31773.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
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:OQE31773.1}.
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DR EMBL; MLKD01000001; OQE31773.1; -; Genomic_DNA.
DR STRING; 303698.A0A1V6U1P8; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000191285; 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:0043604; P:amide biosynthetic process; IEA:UniProt.
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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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; cd02440; AdoMet_MTases; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 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; IPR010071; AA_adenyl_domain.
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; 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; 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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
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; PS00455; AMP_BINDING; 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:UP000191285};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..445
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2406..2481
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3528..3603
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 526..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2483..2511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2524..2569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2524..2556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3958 AA; 438051 MW; 6528B6087BEAEAF9 CRC64;
MSQLPEPIAI VGSGCRFAGG ASSPSKLWDI VYHAQDVLQE IPPDRFNLKA FHHQDPQHPG
KTNVRNAYLL TENVRHFDAQ FFNLKAVEAN AIDPQHRILL ETVFEGIDSA GLKLEELKGS
DTGVYVGLMY GDYENLQFRD LKNLPTYNAT GTARSIVSNR ISYFFDWNGP SMTIDTACSS
SLVALHLAVQ ALRSGECKVA VAAGSNLLLG PEHFVSESKL SMLSPDGRSR MWDQGANGYA
RGEGVASVIL KPLSAAIAAG DYIHCLVRET GVNQDGRSRG ITMPSATAQA DLIRSTYAKL
DLNPLLPDER CQYFEAHGTG TKAGDPIEAE AIHRAFFGPP TGNKESKDSP RTPLYVGSVK
TDIGHTESTA GLAGIIKATL ALQHKIIPPN RLFEELNPDI DPFYGPLKIP QEPIPWPAVA
TGNPRRASVN SFGFGGTNGH VILESYETPV APAAEKIHQT SSFSPFVFSA YSQQSLTANL
KSYARYLEEN PDINPADLAW TLQSRKSRLP MRVSFPASSI KDLQSTLSGI QDDSQNGTRP
SRGSKEPRIL GVFTGQGAQW ARMGAGLIEK SPYASKILSD LEERLAELPK EDRPSWSLRE
QLLAKESRLG EAALAQPLCT AVQIVLVELL RLAGIQLSVV VGHSSGEIGA AFAAGLLSAS
DAICIAYYRG LHSHLAQGPE GIKGKMMAVG TTFEDAQELC ALDEFQGRIV VAAVNSPTSV
TLSGDADAVV EMAGICADEG KFHRQLKVDK AYHSHHMRPC SQAYMNSLRR VGVKVQTPTS
DCVWVSSVNP EQSSDDGIDD LDATYWDRNL VSPVKFMQAV QKAIQLGPFD LAIEVGPHPA
LKGPVEEMLR DQNITLPYTG VLQRNTEATQ SFSNALGLCW MHLDSLNLKI EHFESTMSGT
NNKPRFIPNL PLYNWDHERE YWHESRHSRT YRTQGDHHHA LLGDMTPERF PHQISWRNLL
RPRELPWIHG HKIQEQTVFP AAGYVVTALE AAKFVAPAEK SIQLVEIEQF IIHQAVVFDN
DDIDSSVEVL FNVSNIRQFE NTRLRARFTY SACAKHQSTF QLIADGDLVI TLGEPSQDVL
LARSAESFDM VNVDKEAFYN SLSELGYGYT RHFQGLSGLQ RKLHKAQGFV GLPDLELDEV
PLVVHPATLD LAIQSIILAY SFPRDGEVWS VHVPVKIERI RVNPALCGQN WVEAKHLPFM
SSVPDREEGT GFSGNVQIAS ADGNHAAIEV EGLRVVPFSS TTAADDKRLF NTIEWHNTEP
IPEDIYSPPS SEETDLALLL ERGSSFYLRQ FEAEFPLTHP ARKDDNHRAY LNYAAHVNNL
VLQGKLPHAR PEWLEDTLQD VIASTEKFSH LAEVKTMHTV GAQMPRVMRG ETSLLEHLIE
NSLLDEYYST AVGMSQVSDW IGEVVGQIGQ RYPRMKILEI GAGTGGATKQ VLPRLGDRFL
SYTFTDISSG FFPTAQVEFE KYQDRMTYAV LDMEKGIKEQ KFEPNSYDLV LASLVLHATK
DLDATLRRAR SLLRPGGFLV LLELTSSHVI RGPFIFGCFP GWWAGQQDGR VLSPCVPASR
WDELLRNAGF SGVDTIVPEE DSAIFPNSVL VSQAVDDRVD FLREPLLSSP TIFKDRTVIE
NLFIIGGKSL NISRLTRDLQ SLLKAQCSNI TVLESFDAVT HTQLPSNTTV LILADLAGNT
FQDITEERFT GLKRLFDSEK NILWVTQNRR VDDPFPNMAV GFARAAAWEN LGLRFQFLDL
ENVRKPDPRA LAEHLLRFVA LGRWDASGQS SRAPLWSPET EVIINSEGKE LVPRLRTLQN
LNDRYNSARR DIEKEVKGAE SVVTISSKND QFFVRERANT LDISLSNAVK VTHSILHAVK
SPIGYTFVAL GENTKTGTQC LVLADSVSSV MDPREGIRMA LQVPQGREES FIHLVAVNLL
VLQVLKTTSP GDTILVYNIP ATIALAFNQL AKEAGISIAY ASSNQAEAKS RSWIFAHPSM
YRSEIEALLP RDIARYIDFS NPVDIAHGPL RHYPPFGCAI DNTSNLFSTV GTGRYVQNGD
SALLQQVVYM ALAGLDIWEE NLAQGVPATR SINDLNQDSE SWNKLTTLTW SSPSIHVKVL
PVEAMFKRDR TYWLVGFTGN MGRALCDWMI LNGAKYIVLT ARTPKVDPNW LAKAEQRGAT
IRIFSKQVVP ALARDITDLQ AVQECRQKII TELPPIAGIA HGAMVLTDGL TATASYSDLT
AVLRPKVEGS LNLDQVFHDD KELDFFIFFS SVASVFGNPG QSAYAAANQF MSAITEQRRK
RGCAASILYL GTVIGAGVVT REMNATEQLA MYDRGFMPMS EADVHVAFAE AVRASKPESK
EQAQIITGLR SLPKASTSMS PSYSWPQFSD LTIPETEGNQ STSTSTGDIS LKDRLIAATS
DEEVLSIVSE TFIAELRKVL QLPTESELTE SHRSDELGLD SLISVRIRSW ILTNYQVNIP
ALRILGGATI GELVEQTRSS IPSELIPNVG NGEKISKVPA PIPTPPPVSK APVTNQIVAT
QDTQVAEKFS SSESQDPGSQ TPSDLEDGIS TPWSEISRPN KDEEKSLSEL PLVRSGPLSY
IQSMFWFVQE LLPEKGTLNN TGIYKIRGEI RSADLARALE AVSQRHEALR TCFRVEDGRV
IQGILPRSPL TLEEKKIHSE AELIREYEAL RHHVYNLPNG QTIRIILVSG KSQSYLLMGY
HHLVFDGASH LPFIEDLERA YSGKQLDNNV LQYLDFSNQQ QSEYHSGQWK DDISFWRARF
PTIPDPLPLH RSRLSERRPL SQYAAHTISI RIPKNISEQI REVARSYRAT SFHVHVAAFK
AILHRFLDVE DICIGVAEGS RREENMQKSI GPYLNIVPMR MKAESTQSFG RAIEQARLDT
LQTLAHSHVP LEVILNELHV TRSPTHTPLF QVFLNYMEGV DERQRLGDCE MELSTHQSAK
LAYDFSATIF NNAAGDASVD FTVQQGLYSE TDAALIARGY EDVLYEIIQS PKRPSFNSEW
PETLVHCFEK FLPAYSDNTA VTDSTGTSLS YGQLAQLIDT ISLGLLEKDV TPGSRVAILQ
QASVNWIASL MAILKVGAVY VPLDPDTPTA RLSLIVNDCK PAVILTDNQR DCQKDEFDPP
IQGAVVNVSR LSLSPLKKPL EILARPQETA IILYTSGSTG TPKGVELRHE SLKHEFDLCK
AVYGLGQSDV VLQQSAYSFD LSVTQIFIAL TVGAELRVVS HEFRSDARSI VNCIKNAGVT
ATYATPTEYK AWLRHSNQDI LRSSPWRLSL TAGEAVTEPL LQLFRDLNCP QLRLFNVYGP
TETTCGSTKM ELEYHQPNFY DGRIPVGRAA ANEAFYIMDT QRNIQPIGLP GEIFIAGVGV
ALGYLNNIEL TKKAFHPDPF QPGSIMYQTG DRGRLLPDGS LLLEGRIQGG LEVKVNGVRI
DLEDIEQTIL KSANGKLANA AVSVRKFNDI QVMVAHVVSA DNDDSGEEEV FLSKLLASLP
LSRAMKPSAI IGISSLPTSV SGKLDRKLVE QLPISQDLSE TRKPKVHSAG EARMEALWRE
VIPNELLGRI HSESDFFGCG GNSLLLIELQ AQIREQLSID IPLIELFQSS TLRSMVQLVE
ASSVDHDTFI DWEIETTPEI GLSAKSLSTM VNTPPRIVVL TGATGFLGQY ILRDLVQQKN
VERVICLAVR NANQRQNELL LSEISNGKVT VYEGDLQSAR FGLDEETISD VFHMADVVIH
NGADVSHLKT YASLRASNLH STQELVRRCL PRAIPIHYIS TTGVSMYAKW TNDTFPETSV
LNSPPPRDGL HGYVSSKWAS EVYLEKIHEN YQLPIYIHRP SSIIRPEVEI NGANPAPDVL
QNLLSYSRRL HAVPITIGMH GVLDLVAPET VASNIVKDLI EKNSHGKVIF RHQATDLEIP
FSGLKDHIQK ETRHSIETIS MEEWLSRAEG LGLSSAMVAV FRGVQELGIP FPKLKKGQ
//
