ID   NRPS9_ASPFU             Reviewed;        1135 AA.
AC   Q4WMK2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Nonribosomal peptide synthetase 9;
DE            EC=6.3.2.-;
GN   Name=NRPS9; Synonyms=pesJ; ORFNames=AFUA_6G09610;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=16962256; DOI=10.1016/j.gene.2006.07.008;
RA   Cramer R.A. Jr., Stajich J.E., Yamanaka Y., Dietrich F.S., Steinbach W.J.,
RA   Perfect J.R.;
RT   "Phylogenomic analysis of non-ribosomal peptide synthetases in the genus
RT   Aspergillus.";
RL   Gene 383:24-32(2006).
RN   [3]
RP   REVIEW ON FUNCTION, AND DOMAIN.
RX   PubMed=17464044; DOI=10.1099/mic.0.2006/006908-0;
RA   Stack D., Neville C., Doyle S.;
RT   "Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi.";
RL   Microbiology 153:1297-1306(2007).
CC   -!- FUNCTION: Nonribosomal peptide synthesis (NRPS) is a key mechanism
CC       responsible for the biosynthesis of bioactive metabolites which are
CC       potentially contributing to organismal virulence.
CC   -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC       (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC       (C) domains) which when grouped together are referred to as a single
CC       module. Each module is responsible for the recognition (via the A
CC       domain) and incorporation of a single amino acid into the growing
CC       peptide product. Thus, an NRP synthetase is generally composed of one
CC       or more modules and can terminate in a thioesterase domain (TE) that
CC       releases the newly synthesized peptide from the enzyme. Occasionally,
CC       epimerase (E) domains (responsible for l- to d- amino acid conversion)
CC       are present within the NRP synthetase. NRPS9 has the following
CC       architecture: C-A-T-C. {ECO:0000269|PubMed:17464044}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; AAHF01000006; EAL88812.1; -; Genomic_DNA.
DR   RefSeq; XP_750850.1; XM_745757.1.
DR   AlphaFoldDB; Q4WMK2; -.
DR   SMR; Q4WMK2; -.
DR   STRING; 746128.CADAFUBP00007370; -.
DR   PRIDE; Q4WMK2; -.
DR   EnsemblFungi; EAL88812; EAL88812; AFUA_6G09610.
DR   GeneID; 3508148; -.
DR   KEGG; afm:AFUA_6G09610; -.
DR   VEuPathDB; FungiDB:Afu6g09610; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_60_3_1; -.
DR   InParanoid; Q4WMK2; -.
DR   OMA; DHAPDSK; -.
DR   OrthoDB; 4243at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR   GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019184; P:nonribosomal peptide biosynthetic process; ISM:AspGD.
DR   GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Virulence.
FT   CHAIN           1..1135
FT                   /note="Nonribosomal peptide synthetase 9"
FT                   /id="PRO_0000416550"
FT   DOMAIN          672..748
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          23..77
FT                   /note="Condensation 1"
FT   REGION          177..562
FT                   /note="Adenylation"
FT   REGION          485..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..999
FT                   /note="Condensation 2"
FT   MOD_RES         709
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1135 AA;  125762 MW;  A2603238F2383EFB CRC64;
     MPRSTPVASE QVDFVMKLLG NTTKQITTAT YIKLAWAVVI SCNTGSNDTV FGITVNGRGA
     PIDGAGEMTG ATIATIPQHG CILRVWSLPR MPAGMISRER VQRLLQHLEL VLQDLMADPS
     CKVGDLPRMS RQEWDQIQRW SGTLPPVSRQ CVHEIVNQRS LQFPNACAVS APDGDLSYAE
     LIRSANAVAA ELLVHGVERG NYIPVLFEKC KWSPVAMLGV LKAGAAFVLL DSSYPPQRLH
     TICGGLKTQI ILCSKDMYAR AASLGPTAIA IHENAAFLAD IPDVTFPVVS PENAAYVVFT
     SGSTGTPKGA VIDHQSYCSG ALAHNRAHVL GRNSRVLQYA SYAFDVSIME TLSTLMAGGC
     VCILSDLERH DHFANSVQRL AVTHAFLTPS TARLLMQREL PSLCVLVLGG EAMSLADRSY
     WMSRVRLMNE YGIAECSVAS TIREVSHVEQ KDIGFPMGVV AWVVDQNDHE KLVAIGATGE
     LLLEGPSPPV GRSSSNRAGS GRCAMGSQAG SYKTGDLVRY NEDGSLSFIS RKDSQIKIRG
     QRFELEEVEQ HLRRIDEIQE ATTVVAAPSD RPKQPYLVAF IVPRARESFC VCSARALIPH
     PTEEFRLQAA TIQTKLHSIL PAHMVPAIYL PVNRMPKTSS DKIDRCRLKE EVGKWSWSDL
     RAYSVSSMSH RAPSNRVEQD LQRVWEQILG ILLDSVGVED SFFHLGGDSI IAMQVVAEAR
     SRGLDHSVQD INQLKTIKAI ANKIGDVQRA AIKLVQNHAM LRARYVRQKD GAWKQFFTGY
     TEQCFRFSVH QVKSAQEMRQ IIGESQTSLN PEHGPVFTVD LFHHGGEQSL LMIGHHLVLD
     LVSWRIILAD MEAMILDPQH QPHLTMSFQT WAHLQAEYGT RHLEPPPGQQ PCSIDEPSMR
     QFWGAENNAN TGGDSKTRLI RMNDDLTRKL FGPSSQALDV EPVELLHAAI LFSFVNTFPQ
     RPALVIFGEA HGRETWDSSV DVTRTIGWFT TLWPVVAQVN PSDSLETVAR TVRQARRAMD
     MHGWTHFTSV YHNTRQTKRS AGAHLMEITF NYAGKFQQVE QDGSLFRMEP MAKQNLFDGA
     AELGRWAMLE INSVILNGLL EFHVPYNRGT DEARVLTPWM DNLVKCLEGL ASGFA