ID   NRPS7_ASPFU             Reviewed;        2353 AA.
AC   Q4WZ44;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Nonribosomal peptide synthetase 7;
DE            EC=6.3.2.-;
GN   Name=NRPS7; Synonyms=pesH; ORFNames=AFUA_3G15270;
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. NRPS7 has the following
CC       architecture: A-T-C-A-T-C. {ECO:0000269|PubMed:17464044}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; AAHF01000002; EAL92059.1; -; Genomic_DNA.
DR   RefSeq; XP_754097.1; XM_749004.1.
DR   AlphaFoldDB; Q4WZ44; -.
DR   SMR; Q4WZ44; -.
DR   STRING; 746128.CADAFUBP00003319; -.
DR   PRIDE; Q4WZ44; -.
DR   EnsemblFungi; EAL92059; EAL92059; AFUA_3G15270.
DR   GeneID; 3512484; -.
DR   KEGG; afm:AFUA_3G15270; -.
DR   VEuPathDB; FungiDB:Afu3g15270; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_0_12_1; -.
DR   InParanoid; Q4WZ44; -.
DR   OMA; FQIAPEM; -.
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; -; 2.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.30.559.10; -; 2.
DR   Gene3D; 3.40.50.12780; -; 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.
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; 2.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   SUPFAM; SSF47336; SSF47336; 2.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Virulence.
FT   CHAIN           1..2353
FT                   /note="Nonribosomal peptide synthetase 7"
FT                   /id="PRO_0000416548"
FT   DOMAIN          776..853
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1826..1902
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          305..684
FT                   /note="Adenylation 1"
FT   REGION          885..1147
FT                   /note="Condensation 1"
FT   REGION          1338..1725
FT                   /note="Adenylation 2"
FT   REGION          1939..2214
FT                   /note="Condensation 2"
FT   MOD_RES         813
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1863
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2353 AA;  258475 MW;  97E5645348093CD5 CRC64;
     MAPYIGTQEG SPSSLGTFSH VQLSKDTNVA SQYWEELFHS VGSQPRLACV PLDHQWPRAE
     TTVLASDGLL EAATTFSRTH NISLADLIYA VWAIVSARQT VSGQSTALFT VTGRSYPSAK
     QDTPENGRAE QDYPLLLSVP EDVDVLSWVR SVSTAAATAS ALSYIGYDRI MERTSGIRPQ
     VKVSVTFEVD SHDTMAPDDD FPLVFNIIAS ARLQLSMRHN ATVPRGDVRA LLDRFAATLQ
     RVTANHDAKV SSVDIMPPAE RQLLLDYGKA PLKPKSGMAH SLIEEQAKAR PDAAAVQYET
     EPPLTFSALN TRANQLARQI RPYGTKYIAV HLRMSTDFIV ALLAILKSGA AYVILDPDAP
     AARKSFILDD LQPGLVLVDI STAGELANEV QLGSLLSQAS SHDTGDLLHV QDPSSVAYVI
     YTSGSTGKPK PTLLEHQAVF NGLLAFPPIE GLRQLLFFNP AFSAAQRSIW ATLAVGGCLC
     LASKENLTVH TAKMINTMDI NSVDMTSSAA ALISPDDVPS LRRMVLGGEM VNPAVIQRWE
     HRVELLSSYG LSECTQLNWR HRLQSNVSSR LIGQPYDTTT SYILLPGTTE LAPLLVPGEL
     CLGGAQLARG YLHRPDETAK RFIPNPFGKG KLYRTGDMAV RHADGSVELI GRIDFQVKIN
     GHRVDPGEPN SIIQAIEEVE DSAVVPASVN NRTVLVAAVV SRPDTEWEAL VRKLRPFLAA
     RLPLYMVPQF WVSMPALSVN ANGKIDLVAI RRTVEALGES GQLLPERSSI GSREKRDLTD
     SEKVVRSLWA KVLSLSESEI SLEDSFISLG GTSLEAIQVV SQLQVLHQLS LRVEDILLGE
     TLFQVAAAVQ PQPVEGKPDN DTISAALFEV APSIESVGIS ISSIEDAFPV TPFQEAAIAN
     TMMGGTSYIY SRSYSFEGYS PDDVRAAFET LMKSDGWLRT TYVPHGTSFL QVVKKTADLP
     WETSDMDVTE YLQKQTSKGM YPGELWWTAA ALPNNVLVIT AHHALFDFWS NEFLIQDLTS
     VLQGTPRIQR RGFRPYVEYL QQHDPVAMQE FWQGYLEGAV PSHLGSQIAP ENTVAAEVHC
     DLKRTASQRR VTPGVLLYAA WAIVLGLANS TEDVVMGVTF SGRDVPLAGV LQMSGPTLMV
     APLRVKVNKV TPLDKHLEDV QSNLWAVARN APYGLRKILK ASGQAKDLFD TMVNFLIKIP
     TSTPAGGLRQ LPESNLGTVE YTRIELRNES LNRVTLTSTL EPRCAQALAD TLAAILGAAS
     DQPLTKLGEF RLVQPVPRLM ERLDDPVGSV PVSAVHTIQA EDRVESPGGE LAHSALQRMA
     ASHPSRTAVE DISGARITYA GLAIKMNQLA GLLRERGLEL EQIVPIMLEK SINTIVAMFG
     ILVAGGAFLP LGPENPRERN LGILEDCGAK LVIADQLNAD FFKGTSYEVI VIDAIAWDTI
     PLQRQVVPGL NPNSLAYVIY TSGSTGKPKG TLIPHSAIVA ALDGILYATT QDNSRRIMWS
     LNYTFDGSFY PLFPTLATGR TLCVAPQNTI VGNLADVITK LRVDQINLTP TMASLLHPDD
     VPTLEILATG GEPVTHHMLN VWAPRIKVYT SYGPTEATIC VTTRQVTPDM NIRNVGRPFP
     NTTALILDPD TMEELPSGSV GELCIAGPQL ARGYLNRPEA TNKAFQGTAD QRFYRTGDLA
     RLLPNGEIEL FGRKDDQVKI NGHRMELGEI ESVIKQTNVF RQCAVIAATV LKKKQLVAFC
     SSSVQTPGEA TGEDLLLAPT ELPEVDQIKA QLTTLPQYMV PTIWLPVSKL PSLTSGKIDR
     KRLTALVEGM ADNVLKSYLP HSETSEICSE AERELQSLWS ALFDTPAEDI HANSTFHALG
     GDSISALNLG SMLRRRGYKI QINDILSRST LREQAALMVQ GQPNGDSTAA EAVPQPVFQP
     PEAVYERLVE LGVSRNDVED IYPCSPGQIE FFTQGEKPDR FWQLMAVRTL PDDLDFDRWI
     YLTTQLTKTN QILRALYLQT DAENPQTLVQ VVLKHPVLNL AYRSYRTEEE KQSILEAEWQ
     RPFDPAKPFV RYTLLEDSQG TRSLVINLHH SSYDGTLLHI FDDQFQALHQ NQPIQQPTPF
     KDFITHFLRT PKQPQLDYWT RLLQNHSFDF PSAVIEPKLS STEVAKIDAS LGINGLASST
     GVTAPIVFQT AYSLLLAHLS GARDVIYDNL VTGRNVALDN PQLINGNCAN FLPYHSYVAD
     DIPIETLLRS TQADFWTSTE NGLVSLGEIY EALGRDRSTA AAKCLFCFQP FEPVTAQQDP
     MRWVVMKMSK NRMTFNYAIQ MEVVKAAAKG EYLVRFGYDE RAFSAEEARA ALAWYTRCLD
     GMVKSKVVGE LGV