ID A0A1V6UV50_9EURO Unreviewed; 2078 AA.
AC A0A1V6UV50;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=PENCOP_c004G08019 {ECO:0000313|EMBL:OQE42297.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE42297.1, 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: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
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:OQE42297.1}.
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DR EMBL; MDDG01000004; OQE42297.1; -; Genomic_DNA.
DR STRING; 36646.A0A1V6UV50; -.
DR OrthoDB; 3305653at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19542; CT_NRPS-like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF3; SIDEROPHORE SYNTHETASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500}.
FT DOMAIN 760..836
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1556..1632
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT COILED 755..782
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2078 AA; 227528 MW; 9DA331B40AA690EF CRC64;
MGFIPLEDAY LHNAPNGIQK VPTGANGDFS SFHMAHLASE HITTPTGMKE EIVLLSWLMV
LLRSREDSQI SYDWSHKCSA NDAEPESVNK LLMNEVMKGL QSNVGEVATA ISKNINTRAS
SPASLLLSTS SLSQTSEEAK DEGILHLEVR FNNAHLEIRP LWHTENMLPY TVNHHVEALA
DTIRVCLTNP EATIEQCLRP TTSDLNDIWG WNHALPPTYS FCMQEMVAER ACEYPDKVAI
DSWDGSLTYS QIDQWSTSVA CSLKEMGVEL HDVVPVCFEK SRWTIVAVLG VMKAGATLAL
MDPTLPLARL QNMAVQVGAK SMVSSRKQHE LSLTIMPTGT HFVVEEDAFT NPSNSPPIFD
LPVVPSSALM YIIFTSGSTG TPKGVKISHE TYTSSAIPRA KAVGYTPESR VLDFASYAFD
VSIDSMLLTL GNGGCLCIPS DEDRLNDINE VIRKMRINYA GLTPSVGRIL DADVIASLSG
LGLGGEAVSA RDANNWGKET RIIIGYGPCE CTIGCTVNAS AATGRDYLSI GPGNGAAMWI
ANPNDHNELV PVGAVGELLV EGPIVGQGYL NDPEKTAAAF INDPPWLVAG HKGYAGRRGR
LYKTGDLGRY DPDGLGGIVF VGRKDTQVKL RGQRVELGEI ESQLKAVLPS EANVIAEVIH
PKDYGGQAML VAFVAFQPKG HGNAELALDN ISSELNSILT KANADVAKTL PRYMVPTTYI
PVNLMPVLIS GKTDRKQLRA FGATVDLRQL DQGAASTASR ELNELEKRLR QAWAETLKLE
AEAIRPDDNF FALGGDSLAA MRLVSVCRAQ DLDLSVISTF GNPTLSAMAT VIQPCTSQVQ
NEIPAFSLIS QSAESARLEA AQACGVDQEK VEDIYLCTPT QESLFTFSLK STKAYIAQRV
ACIPSHISLD AWKKAWEDVV AASPILRSRL APLQDPGLQQ IVVKEGVSWR YSTDLDQYLE
NDRNERMNLG QSLARYGLVS DPNDDKRYMV WTVHHVLYDG WSEPIVLKQV SDALQNQNQS
IEIQTQMRNF VKYVRDTDET AMHDFWRREL KGAVGPQFPR LPSRDFMPTP NGLIEHQISL
ETGAGSPFTM ATLIRGAWAL VASQYTGSDD VVFGETLTGR DISLPGVESI VGPLIATIPI
RIQVRRSSSV ESYLQMVQQT ILARTPYQHM GMQNIRKVSQ DAQYACEAGT GLVIQPDPEY
VGSDLGFELG DVVREALHFN PYPLMVAFGI RRGGLRVCAS FDSSLIEGSQ MQRILAQLET
ACVQLSKGLD KRIDEISCLP ETEVDQIWQW NQAPPLSVDE TSGNLRAHAS TKQGSVYPRV
VVPWVCNARN PDLLSPIGSV GELWLEGACL SGEAIESPSW LVAGSSGCAG RSGKVQPTGD
MVLLQDDGSL VFVGRKENVV PLQGHAVDIA DLESHFEKHL PSATRAAASV FQPLREGTQK
VTEQELAIFI ESQASQEDSV RVMPAKYEMV GEQTTICDTI SVTLAVSLKK LDKFIRDSLP
SYMSPSAYIV VDKLPAGLEQ LDHTSLNKLA SKIPQSVLDQ LRGGFKEAWT KGLAQTNLSP
TEKILQSAWA NILRLSPEQI DVDDNFFRLG GDSVLAMKLV SSLRTQGHSL SVADIFQHMR
LGDAAKVLKV DQAKENVTPY KPFSALSNLD VKMFLSSDVR PKLANPGWPI EDVSPVTDSQ
ALDIRGTIGA PRTSIQYTML YFDQNINQEQ LLRACNDLVK THDILRTVFI EHESSFLQVV
LQDAHAPIVM HQTDKDIEQY ATELCKVDIE SNFELGSPFL KIFHVQGADG KHCLVLGLSH
AQYDGVSLPR LLQDLETLYA GGKVVDFEPF ASYMARVSDG RLQTQAVNYW GDLLKDSTLS
VLYGASTQPT DKAVFHEKAV EDFQSIPEIT TANVLTAAWA LVLARRLGKP DVTFGSVTSG
RTIDLANVEN VMGPCYQLTP VRVKFESQWT AMDLLRFVQK QSAESAAHDF LGFEKISKQC
AQWSPEARSF DSIVHHQDWD DFDDMPFAGS SCKVDISNPH GDAAYPLKAV SFVRGGKMHV
GFVGSEKDAT FVDATLDELA AAVQELSGCR SEPLVIDA
//