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UniProtKB - Q4WYG2 (NRPS5_ASPFU)
Protein
Nonribosomal peptide synthetase 5
Gene
NRPS5
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Functioni
Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence.
GO - Molecular functioni
- ligase activity Source: UniProtKB-KW
- phosphopantetheine binding Source: GO_Central
GO - Biological processi
- amino acid activation for nonribosomal peptide biosynthetic process Source: GO_Central
- nonribosomal peptide biosynthetic process Source: AspGD
- secondary metabolic process Source: AspGD
- secondary metabolite biosynthetic process Source: AspGD
Keywordsi
Molecular function | Ligase |
Biological process | Virulence |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:NRPS5 Synonyms:pesF ORF Names:AFUA_3G12920 |
Organismi | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic identifieri | 330879 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:Afu3g12920 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000416546 | 1 – 2202 | Nonribosomal peptide synthetase 5Add BLAST | 2202 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 554 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 | |
Modified residuei | 1602 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 | |
Modified residuei | 2164 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Phosphopantetheine, PhosphoproteinFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 517 – 593 | Carrier 1PROSITE-ProRule annotationAdd BLAST | 77 | |
Domaini | 1563 – 1643 | Carrier 2PROSITE-ProRule annotationAdd BLAST | 81 | |
Domaini | 2130 – 2202 | Carrier 3PROSITE-ProRule annotationAdd BLAST | 73 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 58 – 443 | Adenylation 1Add BLAST | 386 | |
Regioni | 625 – 918 | Condensation 1Add BLAST | 294 | |
Regioni | 1105 – 1482 | Adenylation 2Add BLAST | 378 | |
Regioni | 1664 – 1952 | Condensation 2Add BLAST | 289 | |
Regioni | 2103 – 2129 | DisorderedSequence analysisAdd BLAST | 27 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 2111 – 2129 | Polar residuesSequence analysisAdd BLAST | 19 |
Domaini
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. NRPS5 has the following architecture: A-T-C-A-T-C-T.1 Publication
Sequence similaritiesi
Belongs to the NRP synthetase family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG1178, Eukaryota |
HOGENOMi | CLU_000022_0_5_1 |
InParanoidi | Q4WYG2 |
OMAi | SLGFDCC |
OrthoDBi | 4243at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 3 hits 3.30.300.30, 2 hits 3.30.559.10, 2 hits 3.40.50.12780, 2 hits |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site |
Pfami | View protein in Pfam PF00501, AMP-binding, 2 hits PF00668, Condensation, 2 hits PF00550, PP-binding, 3 hits |
SUPFAMi | SSF47336, SSF47336, 3 hits |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 2 hits PS50075, CARRIER, 3 hits PS00012, PHOSPHOPANTETHEINE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q4WYG2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNLTLTTTSI TIQPSATMAN RAPTLLDHFH DQLQKHSSSV AIEDGTQSAD
60 70 80 90 100
QGAWERVTYA QLDALSDSWS KRLRQAGVGA GCIVPLLSKR SVAMVAATLA
110 120 130 140 150
ILKLRAAYVS IDIDSWGKDR IDTVLKTVNP QIIVSTSPCP KDHYPYPVVA
160 170 180 190 200
LERNDFDETV TSNGTQWTRN DEDSIDRGND LAYIIFTSGT TGIPKGVKIG
210 220 230 240 250
QRSISRYVKE GGDLPFNFNT THGTRVLLIC SIAFDVCAGV MFNTLCNGGT
260 270 280 290 300
LVLADPSTFE TAAKTCHVLP LTPSILVTLD PKAGFDTVEK IFLGGESPSP
310 320 330 340 350
SLIEAWSSPR RRLYNAYGPT ETTCTAFMGE LLPGSPITIG YPISYSTVTL
360 370 380 390 400
LDEDGMESVE GEICIAGLGL ALGYFHDPER TNSAFVEWNG VRIYKTGDYG
410 420 430 440 450
RRTKHGLQFC GRRDSVVKNR GFLINLEADV EPALLSYDKV DSASAFMSQG
460 470 480 490 500
QLIAFVTPTS AKEGLREYLA NTVSSFLVPD TIYSLDEFPR TSNGKVDRRS
510 520 530 540 550
LMRMHELEQG SDTASLERGL GAVESVRRGL SHVLRLPESQ ILPASSFRHL
560 570 580 590 600
GGHSLAAVML VSVLRRMGFG ISVAEVLLLD TVENIAAAVV ELSDIPHALS
610 620 630 640 650
AQEDLIERLR HDISTTRPLD EGVTIAPMTD MQTRLLGASV ATPGLSFIKT
660 670 680 690 700
SFTLDHPEKE DLTSTLRAAW VRLHQTHEIL RTAFVLTASN GTQIISQEPD
710 720 730 740 750
FSWKEKFVTE SEWESVCRRE EHLDVADFPD FDAENRASLS RVVLIIAPRR
760 770 780 790 800
RTRFVWTVHH SLIDGWSMAT LMRDFASCLD GKPIPAPPQF AQVAQAIGQL
810 820 830 840 850
KAESSDRAVS FWKEYLDGYT PAQRLRVSPP SDVSDYTQAA LSRKLTVSVS
860 870 880 890 900
ALEDAARDRF AVTPATLLYA AWGLLLSRYS GTDRAALGAV LSGRSLPIPG
910 920 930 940 950
VENIIGPLIN TLPLAINTQE AQSTYSFVQS VFRRLCDILE FQWSPVALIQ
960 970 980 990 1000
EGCGCNPSEL FETLFALQYD FPQTPWKSSE VPEPRDIRYE EATQVPLTVL
1010 1020 1030 1040 1050
LDNANGQFEV RFIYRRSHFG DATVQRMIGQ FGNLLENLIA AQPDTDLSNV
1060 1070 1080 1090 1100
TGQMFNNRVY EMSIAKPGQP VSACKVPESL TEAIENSIQA HPDIYAVEGL
1110 1120 1130 1140 1150
TGRLTYREFG RMTEHISQRL LQHIQPGSVA CMISDGSLLW LLAMVAIIRA
1160 1170 1180 1190 1200
GAIYCPVDEK LPRDRKDYMV RNSRAALILY ANSSQEPLCN GVPSLNMESI
1210 1220 1230 1240 1250
MQEISSSSGS PIATSRNRPS GDTVACLVYT SGSTGLPKAV QLQHKGILNV
1260 1270 1280 1290 1300
ISQPEGRLYS RPGQRNAQML SLGFDCCIKE VFSTICFGAT LVLKDPENPI
1310 1320 1330 1340 1350
SHLARVDATM ATPSLLATLE PTDYPNLKVI TVAGEAVSQV LNDKWAAGRT
1360 1370 1380 1390 1400
LINGYGPAEC TLISTTAILH PGNRVSIGKP LPGLSCYLLD SNKRPVPMGV
1410 1420 1430 1440 1450
SGEIYISGVQ VTPGYLHNEQ ETSKRFLSDS FNPGQVMYRT GDIGRMLEDG
1460 1470 1480 1490 1500
NIEYIGREDN QIKLRGFRID LGEVQSTISK LASTASNVAL IVSNGNLVAF
1510 1520 1530 1540 1550
MTPETIDVRS LAKSLETQLP QYAVPNRIIA LATLPTSANN KVDSSALQRY
1560 1570 1580 1590 1600
LRDHGKDGAV VEDLETDTQR VLAVIWADML GRDLNQTPIS PSDRFFELGG
1610 1620 1630 1640 1650
HSLLQIKVAQ AISKRWNIRP LPLKQVIRHH SLQDLSLAID ELVSDPRTVS
1660 1670 1680 1690 1700
TMPFLEMTPV ARNGQLPLSY LEKEMLLNHL ISGGSPAGNM NFVCKIRGDI
1710 1720 1730 1740 1750
NAETLADAFQ RVTADVEVFR TRYSVIEGTL FRQQAPGSVK VPRVVQTGNL
1760 1770 1780 1790 1800
SSFVHGRITK SFDLSTEPPV DVSIIIGTPM QAMLVVVMSH VVGDAATMAT
1810 1820 1830 1840 1850
YLNRVSRTYD LLRSNSQTTN TSTVPDNLTY IDWAHWASTL QPNPRALTFW
1860 1870 1880 1890 1900
SSYLSNPPSP LTFGNPSPAP ATYIGLTRSW TLPPSMYRKL SDLAAKASVT
1910 1920 1930 1940 1950
MHQLILAAVF FSLQCVDRRD DILVAAPFTH RTEPGTESLP GLFLDRLLLR
1960 1970 1980 1990 2000
IQRSPHQSSI FDFLSSVRET SQQALAHVIP FHTLRHSLAH KPSLIDPLFK
2010 2020 2030 2040 2050
VMVTYHTAAD QRPLLDLSGA EVQPIPWRHT GGSKFPLKFE FTEMATQDLE
2060 2070 2080 2090 2100
VDMEYDLGCI REDIALRLEF ALSFALQLMV LERETDDIIQ LVQMSFCPGE
2110 2120 2130 2140 2150
GSPVGLTPSH EGSAELTNGT NKTDSTTGQQ ELENNLTDVV CECLGLEIQD
2160 2170 2180 2190 2200
VDADKSFWDL GAQSMDALKL QHLCEKRGVR VRLRDIFVSR SLLELATCAV
II
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000002 Genomic DNA Translation: EAL92291.2 |
RefSeqi | XP_754329.2, XM_749236.2 |
Genome annotation databases
EnsemblFungii | EAL92291; EAL92291; AFUA_3G12920 |
GeneIDi | 3512626 |
KEGGi | afm:AFUA_3G12920 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AAHF01000002 Genomic DNA Translation: EAL92291.2 |
RefSeqi | XP_754329.2, XM_749236.2 |
3D structure databases
AlphaFoldDBi | Q4WYG2 |
SMRi | Q4WYG2 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 746128.CADAFUBP00003549 |
Genome annotation databases
EnsemblFungii | EAL92291; EAL92291; AFUA_3G12920 |
GeneIDi | 3512626 |
KEGGi | afm:AFUA_3G12920 |
Organism-specific databases
VEuPathDBi | FungiDB:Afu3g12920 |
Phylogenomic databases
eggNOGi | KOG1178, Eukaryota |
HOGENOMi | CLU_000022_0_5_1 |
InParanoidi | Q4WYG2 |
OMAi | SLGFDCC |
OrthoDBi | 4243at2759 |
Family and domain databases
Gene3Di | 1.10.1200.10, 3 hits 3.30.300.30, 2 hits 3.30.559.10, 2 hits 3.40.50.12780, 2 hits |
InterProi | View protein in InterPro IPR010071, AA_adenyl_domain IPR036736, ACP-like_sf IPR045851, AMP-bd_C_sf IPR020845, AMP-binding_CS IPR000873, AMP-dep_Synth/Lig IPR042099, ANL_N_sf IPR023213, CAT-like_dom_sf IPR001242, Condensatn IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site |
Pfami | View protein in Pfam PF00501, AMP-binding, 2 hits PF00668, Condensation, 2 hits PF00550, PP-binding, 3 hits |
SUPFAMi | SSF47336, SSF47336, 3 hits |
TIGRFAMsi | TIGR01733, AA-adenyl-dom, 1 hit |
PROSITEi | View protein in PROSITE PS00455, AMP_BINDING, 2 hits PS50075, CARRIER, 3 hits PS00012, PHOSPHOPANTETHEINE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NRPS5_ASPFU | |
Accessioni | Q4WYG2Primary (citable) accession number: Q4WYG2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 18, 2012 |
Last sequence update: | April 17, 2007 | |
Last modified: | May 25, 2022 | |
This is version 109 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families