ID A0A1V6NWL5_PENDC Unreviewed; 1906 AA.
AC A0A1V6NWL5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENDEC_c031G03128 {ECO:0000313|EMBL:OQD68736.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD68736.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
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 -!- 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:OQD68736.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYL01000031; OQD68736.1; -; Genomic_DNA.
DR STRING; 69771.A0A1V6NWL5; -.
DR OMA; THLACNA; -.
DR OrthoDB; 20296at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_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; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000191522};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 522..597
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 619..1051
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1816..1891
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1541..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1906 AA; 206351 MW; DFBF86DDAE8B649D CRC64;
MSTSMGSEND FNLTEDPSKL GHNIPALFDR VHGRYSQKAA IVCGEHTIAY STLAADSDRL
ACLLLSRGIS RGHTVAIAVD RTADMVMLML GVLKAGAAYI PVNPALPSAR VNQMLDDEAL
RMVIIDEKAG SGEYKCGDKA VCYTASELRN RIKDKANEKP EVDIQADDIA YIIYTSGSTG
KPKGVEIHHG ALCNYALSMQ QRPGCTDQDR VMYKSTISFD MAVYEIYVPL LCGATIVQAQ
THETVDARAM LDLMEQQGIT IFFATPTTWQ MLLDVGWRGT PGLFKLLTGG EALSPRMAER
LTACAEEVWN IYGPTEATVS VAAWRVKVGE DILIGTPNAN TRLYLLDKDL QSVPVGSTGD
LYISGAGVAR GYRNNPELTK AAFLKDPFCE NSMMYKTGDL ARFLDHKKLK VLGRADSQIK
IRGQRLEPGD IEESITAHEG IANAIVVSRD ERLVAYCVRQ QGSASAEIPL ANLLRPWLEA
RLPAYMVPSF FVPIDRLPST SNGKVDVKAL PDPLSSITPA QIPASVLEQQ LLAIWIDVLG
HDQIGVEDNF FHVGGDSARV IQVQAKLEKL LSRPVRAPKL YEHFTITALA AYLSGTGDEP
LAKEVPEEKE EESAGDTIRE DIAVISMACR LPGEIYTPED FWKVLIEARD VITEVPKDRW
DADAIYDADH EARGKSYSTG GGFVQSATSF DAPFFGISPR EARAVDPTQS MILETCWEGF
ERAGYGTKAL RGSQTGVFIG SGNSSLDDGQ LSAAGREKLE GYLGLGTAPS VISGRVSYAL
GLEGPTMTVD AGCAASLVAT HLACSALRQG ECDMAVAGGV TFLPSPGLHV EFSRIRVASP
DGRSRPFSAD AAGMGLAEGA SAVVLKRLSD AQRDGDEIHV VIRGSAVNHG GRGSTLSAPS
GPGQKRLVRA ALAAARLKPH DIDYVEAHGT GTKQGDPIEG TALAEVFGSS RDDISGPLWI
GSSKSNIGHT QAAAGVAGLI KVALAMRHNM LPQTLHATKL NPMIDWEGAN MRLSQSKKAW
LPRENDPTIP RRAGVNSFGI SGTNAHLIVE EPPKRDISRA KNFDDARSSS PLPFLISAYT
NAALREQAKN LLNHLSSDAA GNTQLPDVAY SLATTRTHFP QRIVLTAQDK ADLLGKLASI
VDNEVNASSD SGKTTRIAML FSGQGTQWVN MGKCLSEHHR VFRETVEQIA HLFKSALDKP
LLEVVWADPA SEAASLLQRT DYAQPALFAL QVALWRLWQS WGVQPEVVLG HSIGEIAAAY
VAGVMDLADA CRLVATRGKL MHVLPENGGM VALESGVSDV IAAIEQLSVG DRVSIAAINT
PRQVVASGDM DAIHKLVSHF TSRGRQSKVL KTSRAFHSHH LDESMLASLR TVAESIVFKE
QSLPIVSTVT GRLAEPGQLS NADYWVQQAC NPVLFAEGMK TLANQGMNCF VELGPGSTLC
GMGASCLDED SQANKKTGRR GVDLAWLPSL NSKSEGTVTV QNSLSELHIR RKEVDWTAYF
EDFGGRHVQL PTYAFQRQRY WLDGMQPLYS VQASIDSVGA SDESVGASDD SFGGSDNTDD
TSFDSVGVSA GPDEAKPNSQ IQIGWHAIDT GIYPPYSNWG LLCPAGDVPS MALVKQALLH
SSRQPIVVNQ LEKAVNMAGV LCFWESQSQD ELTAKASEQL QRAARICFSP LLVWVTRGVI
GAQSVGGGFG EGSLWSIMRR ARINYPQLRL RIIDLEDDVD IATATTLCSI LMMSNEPECV
IRGGRVLVPW MQMQSQALHE SISIIPKSQR HPQQYELRLK NQESDEAVTP NHNGTDMVLD
NFVNEMRKAG PDERVMMLER LVRDVTAEAL GMTTAEEVDM HRGLVDIGVD SLGSMRMVKQ
LAVRTGVTLP VTFKEAYADL TSLSEALRQQ IEDSWAAESS SRPISV
//
