ID   NRPS6_ASPFU             Reviewed;        1290 AA.
AC   Q4WYP0;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Nonribosomal peptide synthetase 6;
DE            EC=6.3.2.-;
GN   Name=NRPS6; Synonyms=pesG; ORFNames=AFUA_3G13730;
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. NRPS6 has the following
CC       architecture: A-T-C. {ECO:0000269|PubMed:17464044}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; AAHF01000002; EAL92213.1; -; Genomic_DNA.
DR   RefSeq; XP_754251.1; XM_749158.1.
DR   AlphaFoldDB; Q4WYP0; -.
DR   SMR; Q4WYP0; -.
DR   STRING; 746128.CADAFUBP00003471; -.
DR   EnsemblFungi; EAL92213; EAL92213; AFUA_3G13730.
DR   GeneID; 3512418; -.
DR   KEGG; afm:AFUA_3G13730; -.
DR   VEuPathDB; FungiDB:Afu3g13730; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_60_3_1; -.
DR   InParanoid; Q4WYP0; -.
DR   OMA; FTTTHRI; -.
DR   OrthoDB; 4243at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
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; 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   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Virulence.
FT   CHAIN           1..1290
FT                   /note="Nonribosomal peptide synthetase 6"
FT                   /id="PRO_0000416547"
FT   DOMAIN          775..851
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..657
FT                   /note="Adenylation"
FT   REGION          846..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..1162
FT                   /note="Condensation"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..870
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         812
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1290 AA;  141796 MW;  8E03CF4ABCAC8611 CRC64;
     MTAIDVPWLS TPRRDNSHGT RSNSSCQPSC TQRIAVPISP DAVKYPLAVF CFAWAVTLGA
     YLDSQELVIG FAFHGWDGDT SIPSAGTCRI RIRPEQEILP ALDEVVADGD KGLRSWVAQG
     AGSETDIAIQ RKEVGDSLHP AVHGDEKLSP EIIITPSGNQ GPYHVQGRFD PHIVAPALAH
     MMLHQFAFAV QGIVRGQSSI ASSQVKDLQA ISPDGMAQLM RWNRQSAAEE DGACVQDLIQ
     RTCQQQPHAM AVCAWDGSWS YQELDCQASH LASQLCDHGI EPEKFVGLLF EKSKWTTVAI
     LAVLKAGGAF VLLDPTQPAA YLSAICTMTR TALLLCSSHN QRLAAELRQT TIQVPRDPYH
     GAMPTSDFRR QSSPAVQPHH TLYACFTSGS TGRPKGFIID HVAFNSGLQT YAHATGLGCD
     SRVFQFASYS FAPSITDQLA SLIVGASICV PAEEELQNDV EGSISQLQAT WLKLTPSVAR
     TLDPGRLPCV KTLILVGEEA QVSDVAAWQD HGITVLGLYG QSENAKGTMV SRKSSEDADP
     GNIGSPFCAV GWVVDPDDYH RLMPIGATGE LLLESPCLCR GYIDNEDETK LAFVSKPSWL
     TQVRGQGTAQ PLLRTGDIVR YNCVDGTFCL VGRKGNRVKL RGQRLELAQV EHHLRSCLSS
     THPVLADVVQ PANENGRDPM LVAFVPWADS QSAADATDGF FAPPTKDFQT QARAVLGRLR
     HLLPSFMVPS TLLAVRTIPR TGTGKIHRRR LQEAASMLSR KQLMAYISPF IPYRAPETEL
     ERKLQRACGR LLNIEADQIS MQDNFFDLGG NSLTARQLVA VARAEGLQVS VAQIFQQPTL
     AGLAQTHRHP VRRAEVPRSS HDPDPFGRVR DDVRREGLPH IARGNIEDAL PVLYTQMTTA
     RDHCVDFFPL RVIGGQLDPE QLRLAWTRVI QAFPILRTVF PRFRGRFIQL VVRDIGDSNF
     YRVVEAPSGQ TAEEWARALC TEAIQFRCPV DRPVAQLTLI QAAGSSALVL RLCHAQYDGS
     CLEHLVRSLM MAYHGRPLVV ESDFQAYTRT CLRLRIPEVL DFWRRFLAGS SPTQLASSMT
     GDREAARKIN RSFFRREVNS LAAPAGFTLA TVVKAAWSWV LRNETRSEDV VFGQLVSCRG
     SVPLPHADTI IGPCMNIIPV RVGRDLLGAV QAQHAQTMEF DMIGMDEIVR HCTSWPAGTE
     PDSIIIHENF HVDWEVHDGG VTIQKIAAVF NQQPSSLTFL ITIPTETGLI AVLMAPANMS
     STHADRVLDL FCNTLTRLAW SPAAVLRRSE