ID   NRPS5_ASPFU             Reviewed;        2202 AA.
AC   Q4WYG2;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Nonribosomal peptide synthetase 5;
DE            EC=6.3.2.-;
GN   Name=NRPS5; Synonyms=pesF; ORFNames=AFUA_3G12920;
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. NRPS5 has the following
CC       architecture: A-T-C-A-T-C-T. {ECO:0000269|PubMed:17464044}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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; AAHF01000002; EAL92291.2; -; Genomic_DNA.
DR   RefSeq; XP_754329.2; XM_749236.2.
DR   AlphaFoldDB; Q4WYG2; -.
DR   SMR; Q4WYG2; -.
DR   STRING; 746128.CADAFUBP00003549; -.
DR   EnsemblFungi; EAL92291; EAL92291; AFUA_3G12920.
DR   GeneID; 3512626; -.
DR   KEGG; afm:AFUA_3G12920; -.
DR   VEuPathDB; FungiDB:Afu3g12920; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_0_5_1; -.
DR   InParanoid; Q4WYG2; -.
DR   OMA; SLGFDCC; -.
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; IMP:AspGD.
DR   Gene3D; 1.10.1200.10; -; 3.
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; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW   Virulence.
FT   CHAIN           1..2202
FT                   /note="Nonribosomal peptide synthetase 5"
FT                   /id="PRO_0000416546"
FT   DOMAIN          517..593
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1563..1643
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2130..2202
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          58..443
FT                   /note="Adenylation 1"
FT   REGION          625..918
FT                   /note="Condensation 1"
FT   REGION          1105..1482
FT                   /note="Adenylation 2"
FT   REGION          1664..1952
FT                   /note="Condensation 2"
FT   REGION          2103..2129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2111..2129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         554
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1602
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2164
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2202 AA;  242170 MW;  FE6D9110D8F568B0 CRC64;
     MNLTLTTTSI TIQPSATMAN RAPTLLDHFH DQLQKHSSSV AIEDGTQSAD QGAWERVTYA
     QLDALSDSWS KRLRQAGVGA GCIVPLLSKR SVAMVAATLA ILKLRAAYVS IDIDSWGKDR
     IDTVLKTVNP QIIVSTSPCP KDHYPYPVVA LERNDFDETV TSNGTQWTRN DEDSIDRGND
     LAYIIFTSGT TGIPKGVKIG QRSISRYVKE GGDLPFNFNT THGTRVLLIC SIAFDVCAGV
     MFNTLCNGGT LVLADPSTFE TAAKTCHVLP LTPSILVTLD PKAGFDTVEK IFLGGESPSP
     SLIEAWSSPR RRLYNAYGPT ETTCTAFMGE LLPGSPITIG YPISYSTVTL LDEDGMESVE
     GEICIAGLGL ALGYFHDPER TNSAFVEWNG VRIYKTGDYG RRTKHGLQFC GRRDSVVKNR
     GFLINLEADV EPALLSYDKV DSASAFMSQG QLIAFVTPTS AKEGLREYLA NTVSSFLVPD
     TIYSLDEFPR TSNGKVDRRS LMRMHELEQG SDTASLERGL GAVESVRRGL SHVLRLPESQ
     ILPASSFRHL GGHSLAAVML VSVLRRMGFG ISVAEVLLLD TVENIAAAVV ELSDIPHALS
     AQEDLIERLR HDISTTRPLD EGVTIAPMTD MQTRLLGASV ATPGLSFIKT SFTLDHPEKE
     DLTSTLRAAW VRLHQTHEIL RTAFVLTASN GTQIISQEPD FSWKEKFVTE SEWESVCRRE
     EHLDVADFPD FDAENRASLS RVVLIIAPRR RTRFVWTVHH SLIDGWSMAT LMRDFASCLD
     GKPIPAPPQF AQVAQAIGQL KAESSDRAVS FWKEYLDGYT PAQRLRVSPP SDVSDYTQAA
     LSRKLTVSVS ALEDAARDRF AVTPATLLYA AWGLLLSRYS GTDRAALGAV LSGRSLPIPG
     VENIIGPLIN TLPLAINTQE AQSTYSFVQS VFRRLCDILE FQWSPVALIQ EGCGCNPSEL
     FETLFALQYD FPQTPWKSSE VPEPRDIRYE EATQVPLTVL LDNANGQFEV RFIYRRSHFG
     DATVQRMIGQ FGNLLENLIA AQPDTDLSNV TGQMFNNRVY EMSIAKPGQP VSACKVPESL
     TEAIENSIQA HPDIYAVEGL TGRLTYREFG RMTEHISQRL LQHIQPGSVA CMISDGSLLW
     LLAMVAIIRA GAIYCPVDEK LPRDRKDYMV RNSRAALILY ANSSQEPLCN GVPSLNMESI
     MQEISSSSGS PIATSRNRPS GDTVACLVYT SGSTGLPKAV QLQHKGILNV ISQPEGRLYS
     RPGQRNAQML SLGFDCCIKE VFSTICFGAT LVLKDPENPI SHLARVDATM ATPSLLATLE
     PTDYPNLKVI TVAGEAVSQV LNDKWAAGRT LINGYGPAEC TLISTTAILH PGNRVSIGKP
     LPGLSCYLLD SNKRPVPMGV SGEIYISGVQ VTPGYLHNEQ ETSKRFLSDS FNPGQVMYRT
     GDIGRMLEDG NIEYIGREDN QIKLRGFRID LGEVQSTISK LASTASNVAL IVSNGNLVAF
     MTPETIDVRS LAKSLETQLP QYAVPNRIIA LATLPTSANN KVDSSALQRY LRDHGKDGAV
     VEDLETDTQR VLAVIWADML GRDLNQTPIS PSDRFFELGG HSLLQIKVAQ AISKRWNIRP
     LPLKQVIRHH SLQDLSLAID ELVSDPRTVS TMPFLEMTPV ARNGQLPLSY LEKEMLLNHL
     ISGGSPAGNM NFVCKIRGDI NAETLADAFQ RVTADVEVFR TRYSVIEGTL FRQQAPGSVK
     VPRVVQTGNL SSFVHGRITK SFDLSTEPPV DVSIIIGTPM QAMLVVVMSH VVGDAATMAT
     YLNRVSRTYD LLRSNSQTTN TSTVPDNLTY IDWAHWASTL QPNPRALTFW SSYLSNPPSP
     LTFGNPSPAP ATYIGLTRSW TLPPSMYRKL SDLAAKASVT MHQLILAAVF FSLQCVDRRD
     DILVAAPFTH RTEPGTESLP GLFLDRLLLR IQRSPHQSSI FDFLSSVRET SQQALAHVIP
     FHTLRHSLAH KPSLIDPLFK VMVTYHTAAD QRPLLDLSGA EVQPIPWRHT GGSKFPLKFE
     FTEMATQDLE VDMEYDLGCI REDIALRLEF ALSFALQLMV LERETDDIIQ LVQMSFCPGE
     GSPVGLTPSH EGSAELTNGT NKTDSTTGQQ ELENNLTDVV CECLGLEIQD VDADKSFWDL
     GAQSMDALKL QHLCEKRGVR VRLRDIFVSR SLLELATCAV II