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Entry version 86 (02 Jun 2021)
Sequence version 1 (23 Jan 2007)
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Protein

Non-reducing polyketide synthase nscA

Gene

nscA

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997).

The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997).

The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997).

The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997).

The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997).

There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997).

1 Publication1 Publication

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.Sequence analysis

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Secondary metabolite biosynthesis

This protein is involved in Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei562PROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Multifunctional enzyme, Transferase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Non-reducing polyketide synthase nscA1 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Conidial yellow pigment biosynthesis polyketide synthase nscA1 Publication
Neosartoricin biosynthesis protein A1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:nscA1 Publication
ORF Names:NFIA_112240
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri331117 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillusAspergillus subgen. Fumigati
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006702 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:NFIA_112240

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004378881 – 1794Non-reducing polyketide synthase nscAAdd BLAST1794

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1754O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A1D8I9

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
36630.CADNFIAP00010391

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A1D8I9

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1717 – 1794CarrierPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni19 – 256N-terminal acylcarrier protein transacylase domain (SAT)Sequence analysisAdd BLAST238
Regioni392 – 825Ketosynthase (KS) domainSequence analysisAdd BLAST434
Regioni427 – 448DisorderedSequence analysisAdd BLAST22
Regioni928 – 1249Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST322
Regioni1314 – 1633Product template (PT) domainSequence analysisAdd BLAST320
Regioni1637 – 1665DisorderedSequence analysisAdd BLAST29
Regioni1682 – 1718DisorderedSequence analysisAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1642 – 1656Polar residuesSequence analysisAdd BLAST15
Compositional biasi1686 – 1707Polar residuesSequence analysisAdd BLAST22

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity).By similarity

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1202, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000022_6_1_1

Identification of Orthologs from Complete Genome Data

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OMAi
FLECPTI

Database of Orthologous Groups

More...
OrthoDBi
68112at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR042104, PKS_dehydratase_sf
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR030918, PT_fungal_PKS
IPR032088, SAT
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF00550, PP-binding, 1 hit
PF16073, SAT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 1 hit
SSF52151, SSF52151, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04532, PT_fungal_PKS, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A1D8I9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATPRGQTVW FGNEFPNDDL KDLFRRLHQH SKDRRFRLLS VFLDESTAIL
60 70 80 90 100
KEEVANLPQQ LQELVPHFDT ACTLPEVDFR QGPLGAAMES ALLTILELGM
110 120 130 140 150
LIGNYEAEDI EWDLDPSQTI LAGLSIGIIA GAAVALSSSL ADVAKVGAES
160 170 180 190 200
VRVSFRLGVY VADISTKLEA PQSDGTLQSW AHVVTGMSHE AVQEELSQFN
210 220 230 240 250
AVTQNPEITK VFVSAADKTS VSVTGPPSRI KAAFQHSPSL RYSKSLPLPV
260 270 280 290 300
YDGLCHAPHL YSQDDIEIVI NSAKSVIPTS RPVRLPLISS QTGKPFEAKT
310 320 330 340 350
AGELFLEIGT ELLTGTIYLD NVTAGILEHV KLKEPTGNYQ IISFRMSQVL
360 370 380 390 400
NGIQAAIETD FPALGRARRD LVSWVHGDYG ARRPSSYAAS KLAIVGMACR
410 420 430 440 450
LPGGANDPEL FWELLEQGRD TLTTVPPDRF DLNTHYDPTG KTENATQTPF
460 470 480 490 500
GNFIDRPGYF DAGFFNMSPR EAEQTDPMHR LALVTAYEAM EMAGLVPGRT
510 520 530 540 550
PSTRPNRIGT FYGQASDDWR ELNASQNIST YAVPGGERAF ANGRINYFFK
560 570 580 590 600
FSGPSYNIDT ACSSGLAAVQ AACSALWAGE ADTVIAGGLN IITDPDNYAG
610 620 630 640 650
LGNGHFLSKT GQCKVWDKDA DGYCRADGIG SVVIKRLEDA EADNDNILAV
660 670 680 690 700
VLGARTNHSA EAVSITHPHA GAQKANYRQV LHQAGVNPLD VSYVELHGTG
710 720 730 740 750
TQAGDAVESE SVSDVFAPSM PRRRPDQRLY LGAVKSNIGH GEAAAGIASL
760 770 780 790 800
LKALLVYQKN MIPKHIGIKT EINPIIPKDL DRRHVGLAMS NTPWPRPAGK
810 820 830 840 850
KRLAVVNSFG AHGGNTTVLL EDAPERVKVS TQDDRTTHPV VISAKSKKSL
860 870 880 890 900
QANIEKLLSW LDQNPDADLA DLSYTLCARR MHHSMRFGAA ASDIAALQKT
910 920 930 940 950
LRSWLDSPKA STELRAIPND APSVVLTFTG QGAYYSGMGR ELFAEFSYFR
960 970 980 990 1000
TQVLQLDQIA QRLGFPSVVP VIDGSIDDGP ASPILTQLSV VVLEIALARF
1010 1020 1030 1040 1050
WSHLGIRISA VVGHSLGEYA AFAVAGVISA ADALYLVGRR AQLTEERCTQ
1060 1070 1080 1090 1100
GSHSMLSVRA SEDDIEELIA GSPDTAEIAY EVCCRNTPQD TVIGGTKESI
1110 1120 1130 1140 1150
DRIRQALEAN SIKCTQLDVP FAFHTAQMDP ILDSLETLAT PIAFKAPSIP
1160 1170 1180 1190 1200
VLSPLLGSVV FDRKSIHAQY LRRATREAVD FVAAIEAAQD FGLVDAKTIW
1210 1220 1230 1240 1250
IDVGPHPICA GLVRGIDSSA SVISSCRRNE DNLATMSKSL VTLHLAGLTP
1260 1270 1280 1290 1300
CWAEYFRPRE REYSLLKLPT YSWNETDYWI PYIGTWTLDK ALLKYGEKKA
1310 1320 1330 1340 1350
PLSLAMSRPS ALRTSLVHQI TAETVEATTA TLHVLSDMQH PDFLEALHGH
1360 1370 1380 1390 1400
RMNNCGVATS SIWSDMAFTV GEYLYRRLVP QVKDVHMNLS DFEVLHAQVA
1410 1420 1430 1440 1450
LEKKGSVQPL VLKAHLDLST SSMSLTWFNA SAETGECAAE SFATGVVRFE
1460 1470 1480 1490 1500
DPAAWTREWD RLSHLVLGRI EALEQRAAEG KASKLSKPLA YALFKNVVDY
1510 1520 1530 1540 1550
ADRYRGMDQV VLHEHEAVAE VTLVAERHGT WHTPPHWIDS VSHLAGLVMN
1560 1570 1580 1590 1600
GSDASNTRDY FYVTPGCSSF RLLNPLKAGG KYRSYVRMFP LLEEANMYAG
1610 1620 1630 1640 1650
DVYILQGEQI VGMVGQIRFR RVPRLLMDRF FSPAAASHAE KQLQETAPSA
1660 1670 1680 1690 1700
TSVKKSTPPA AEAPASVPAL LSNPVAIPFP AASKSEVSTP PLTPPSQQES
1710 1720 1730 1740 1750
PGESAVITPA TSDRGDPVDA GVVGQCLQVM ARETGLEVDA LTPDASFVQL
1760 1770 1780 1790
GIDSLMSLVL SEKFRAELGI EIKSSLFLEC PTIGEMTAWL EEYC
Length:1,794
Mass (Da):195,269
Last modified:January 23, 2007 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB7A561B466D86FB3
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DS027692 Genomic DNA Translation: EAW20700.1

NCBI Reference Sequences

More...
RefSeqi
XP_001262597.1, XM_001262596.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EAW20700; EAW20700; NFIA_112240

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4589233

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
nfi:NFIA_112240

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027692 Genomic DNA Translation: EAW20700.1
RefSeqiXP_001262597.1, XM_001262596.1

3D structure databases

SMRiA1D8I9
ModBaseiSearch...

Protein-protein interaction databases

STRINGi36630.CADNFIAP00010391

Proteomic databases

PRIDEiA1D8I9

Genome annotation databases

EnsemblFungiiEAW20700; EAW20700; NFIA_112240
GeneIDi4589233
KEGGinfi:NFIA_112240

Organism-specific databases

VEuPathDBiFungiDB:NFIA_112240

Phylogenomic databases

eggNOGiKOG1202, Eukaryota
HOGENOMiCLU_000022_6_1_1
OMAiFLECPTI
OrthoDBi68112at2759

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR042104, PKS_dehydratase_sf
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR030918, PT_fungal_PKS
IPR032088, SAT
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF00550, PP-binding, 1 hit
PF16073, SAT, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF52151, SSF52151, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
TIGRFAMsiTIGR04532, PT_fungal_PKS, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNSCA_NEOFI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A1D8I9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2016
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 86 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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