ID A0A1V6US59_9EURO Unreviewed; 3877 AA.
AC A0A1V6US59;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENCOP_c005G01989 {ECO:0000313|EMBL:OQE41240.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE41240.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
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:OQE41240.1}.
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DR EMBL; MDDG01000005; OQE41240.1; -; Genomic_DNA.
DR STRING; 36646.A0A1V6US59; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000191500; 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; 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 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:UP000191500};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..440
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2261..2341
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3455..3533
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2240..2263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2351..2404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2364..2404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3877 AA; 422212 MW; 0F640A1FF29F7316 CRC64;
MPSQQPEAIA IVGSGCRFPG SASSPSALWK LLESPRDVGM EIPPDRFDAS AFFHPDGSHH
GTSNVLRSYL LEEDVRAFDA AFFNISPNEA DSMDPQQRIL LETVYEALEA GGHTVESLRG
SDTAVYAGTM TADYNDTLTR DHNTMPNYFA TGTNRAIISN RVSYFFDWHG PSMTIDTACS
SSLVALHQGV RTLRASESRV AVACGTQVLL NPEMYIGESK LTMLSPNGRC RMWDADADGY
ARGEGVAAVV LKRLSDAIAD GDHIECIVRE TGANQDGFSN GLTVPNSNAQ SALIRQTYKR
AGLDPANNPH DRPQFFEAHG TGTQAGDPKE AAAIHECFGQ HITSSEDPLY VGSIKTIIGH
LEGCAGLAGV LKASSMIQAG SFAPNLLFET LNPKIEPFYK GLQVPTKLTP WPALQEGVPR
RVSVNSFGFG GTNSHAILES YEAPTIAGSS GQTLTPFVFS AASEASLLGQ LQFFAEHLKT
HHDSIDISDL AWTLHSRRSQ LSTKAAFSAV TVEQLASKIV IKLAEVTQNP TTTVGLRSTI
KTSPRLLGVF TGQGAQWPAM GAHLIRSSEF VQKRIQELED SLNTLPEGDR PTWSLKEEML
AGADTSRLAE AALSQPLCTA IQVALIDLLR AAGINFSAVV GHSSGEIAAA YAADFISGHD
AIRLAYYRGF FAHLAGNEAT GQKGAMLAVG TSWEDAQDFI NLSTFKGRLT IAAHNSPASV
TLSGDADAVV HAKKVFDEDR KFARALKVDT AYHSHHMLPC GEAYVKALRA CGIRINRERS
KACSWFSSVT ASAEPMEPID DLLDVYWRDN MTNAVLFADA VKNAAASDEL INLVIEVGPH
PALKGPAMQN ISEVRETPIP YTGVLSRGKN DIEAFAEGLG FMWTHIPQLV DFKSFEKAVA
AEGSRPPKLV AGLPSYQWNH GRSHWSESRI SRKMRTRKHG HHEILGFLST DSNAQELRWL
NVLKQSEIPW LAGHQLQGMT VFPAAGYIAM ALEASRHVAG NRQVKLFELH DLIIPRALTF
EDGDSAGVET LVTLTGVKYL PDQSATTQFA CYSVPVLTKG SDLDMELMAS GTVKIIFGIP
DVAALDRLPV TENNMAAIDP DRFYAGLAEL GYNYGGPFRT MSGMKRKLNQ SSVLVESFPY
KDSDVSDFLV HPSTLDVAFQ ASILAFSAPG DGRLGSLSVP VGMKALRVNP EVCASLPTSG
SKVPVISALD PEFEGFSASI DLLDQDAGNC MIHVEDIVLQ PFAPATAADD SVMFTNTKFG
FALPDGAAAV NLSSMVAQVT HRYPHARILE IGAGAGGATK SILESIGGKY SSYSYTDASE
DYFARASEFF IAHSDKMTFS TLDIEKPPTE QGYEPRSFDI IIASNVLSTT DPLHTALKNA
RELLKPGGYL LLSEPTSASA VGTSEGQVDQ IDGRTSSSPL TLGIWHSALR KAGFGGVDAA
TPDMDRADGS FSVMASQAVD DQVHFLRRPL SASTAPIHIE SLVILGNGTL ETVRLAEEVV
DHLGRFCGET TILSGLPTEE EALELNPSST FVNLVDLDSA IFKNMTTEKM DGLKRMVELA
KHIVWVTQGA HTDHAYHMAS VGFSRTVQQE AAHITWNLLD VSDLQHNTSK AISEYLLQQT
ALDTWEAPPS ALGDREHRDF AFLWSKEPEV FLDHGKLKIP RLMVNTEQNA RLNSSKRVIT
KTVPISHPNI TVISPAADVP SSLVELVGGK PKEFSDDFIK VESSTLMAVR VTPDMFLYVG
AGRGKDGKLQ VFVSTTNSSQ AAPVASVPAD VEAEADDLLV SVASELIVSS LLDQIPNRSH
MLVHCSGEDR FLAAALTKQA AARAVGVEFT CDGQDKQRDP AWITLDVRTP NHCVRERLRQ
IMPTHFLDLT ATPSLSESGL RVDKFLPARC SRINPTSLYR HQASALSQSY DHAALERLLK
DAVSRTVVFP GGVQDLVTQV DRVSALSYKH ATYAVHWPVY GFVEIEVRPL EAEALFSKDK
TYILVGLSGS MGQSLCEWMV SNGAGCVCLT SRRPKVDEDW LKSFRGTGAT IKVVPMDVLD
KENLQRAVDD IRATCPPIAG IANGAMILED QLFSNMSAES MQRVLGPKID GSKNLDDIFY
NEDLEFFVMF SSIACVFGNV GQSNYNAANA FMGGLARQRR RRGLAASALD IGQVTGIGLI
EAANQSVHDQ LRKLRLALVS ETVLRKALGE AIQAGYPGQN DYDYIPTVTT GVRIYGDDEK
DEVTGPWFSN SFFSHMIRQS DASSSGSDEQ DKKSLPVRQQ LPTATSKQEA LEILEGKFFL
VRDSIVEIHH DAPLLELGID SLVAVEVRTW FNKELKVDMP VLKVIGGASL AELCQGAFEK
LPAELAASIG TEGKDAEPAK PAATESKPQS QPQSRVEGSV SDSTSSSGDN STSTPGENST
PDKQAATTLT TMTTPSVVSD HESSEAAKQA TPERLARKFL KSERLSLPQS RFWFLRHLLE
DPTTPNVVFQ FHVTGNLHVG ALERAIRTVT TRHEALRTCF IENENEAGEA YQRVLRSSPM
RLERKKVASE EEVDVEYKKL KEHVFDLESG DVMRIVLLTL TSGNHYLLIN YHHIVMDGAS
FNIFTADLEK AYSGQSLGAP PGQYPAFSVA QRQALEKGEM SDELAYWQGV FPAGEQPPVL
PLLPMARTSS RVAMKGFAAH QVAIDLEPEL VARVKAVSKA QRSTPFHFHL AAFKAMLFCL
AGEETKDLTI GIADAARNDS SVEGSIGFFL NLLTLRFRRQ NDQTFADAVS EARDTTYAAL
GTSRLPFDVL LTELGIARSS LHSPFFQAFL DYRQGAQQKY PWGNCEFEFQ DVHPGRTAYD
ITLDVTEWNA TDTLVMIRVQ TSLYDLTAAN LLLKTYVNFL ETVTSDASLT LEATPIFGQQ
QLTEAVEVGR GESNPCPVKL VLKKEDHTNF KAGLNLTSDW PGTLPLRIDQ VAEENPRKVA
LMDGTGKVLT YSGMVNRIEA ISEALQNAGV HEGSRVLVYQ QPAADWTCSM LAIMRIGAVY
VPLDLRNPLA RLATVAKNCE PLAILADETT KGDAPQLQAE APGSSIINVS SLPEAAVAHI
QNSSNAESTA AILYTSGSTG LPKGIVVTHA GLRNEIEGYT KSWGLGAERA LQQSAFTFNH
SSDQMYTALC NGGMAYIVPA DKRGDPISIT KIIQEQGITY TKATPSEYSL WMQYGGDTLR
QANSWRFAFG GGEQLTTLVT QEFASLDLPQ LRFFNSYGPT EISISSHKME IPYRETEKLT
DMGRIPCGFS LPNYFTYVVD EQLRPVPVGM PGEICLGGAG VSRGYLKNQE LTDKHFVTNP
FATSEDIARG WTRMYRTGDI GHLQEDGAMV FHSRMAGDAQ VKIRGLRIEL SDIESNMICV
ADGALREVVV TLRDGDSPFL VAHVVFEPKH NITDKDAFLR DLLARLSLPQ YMIPVMAIPL
DKFPLSNHSK VDRKAVQAMP LPDRVLQTQD DAELTETMVQ LRNVWREVLG KNVDKLGLDL
GPSTDFFIVG GNSLLVIRLQ ACIRQAFNVA LPLAKLLGAS VLGDMARKIE ESPTVDPINW
EQETTPPAVP TFLRDLAPKT TATAKTVLVT GATGFLGQAM LPQLAARPDV AAIHCVAVRD
KPRVRPLFSA PNVAYHPGDL SLPFLGLGVD EFRELASQVD VILHMGAVRS FWDNYNVLRP
SNVHPTKELA KLAAAHQVPI HYISTVGVLP ELATTKDAGS AVAYVPTADG TEGYIGSKWA
SERILERSAE ELDVPSSIYR FLPATQQDPV EKQRLMDAFI HYVDTSSKVP DMSVWAGRVD
LIPTEQVSQW LGDSITAAPA TTATTKFSHY ESPLAVHTDE LSAYIQQQRG DREGLEPMPV
LKWFGLIKSL GFDYLLASQE ATVGGSGENG QVLQSRR
//
