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UniProtKB - B9WZX0 (FTMA_ASPFM)

Entry version 60 (25 May 2022)
Sequence version 1 (14 Apr 2009)
Previous versions | rss
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Protein

Nonribosomal peptide synthetase 13

Gene

NRPS13

Organism
Neosartorya fumigata (Aspergillus fumigatus)
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>-Experimental evidence at protein leveli <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

Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities (PubMed:16755625, PubMed:23649274).

The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA (PubMed:16755625, PubMed:17464044).

Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B (PubMed:16000710, PubMed:21105662, PubMed:23090579).

The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively (PubMed:19226505).

The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B (PubMed:18683158).

Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties (PubMed:19763315).

In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).

Curated9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • verruculogen biosynthetic process Source: GO_Central
Complete GO annotation on QuickGO ...

<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 functionIsomerase, Ligase
Biological processAlkaloid metabolism, Virulence

<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:
Nonribosomal peptide synthetase 131 Publication (EC:6.3.3.-1 Publication)
Alternative name(s):
Brevianamide F synthase1 Publication
Fumitremorgin 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:NRPS131 Publication
Synonyms:ftmA1 Publication
<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 fumigata (Aspergillus fumigatus)
<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 identifieri746128 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Fumigati

<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_00004241091 – 2211Nonribosomal peptide synthetase 13Add BLAST2211

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 residuei631O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei1714O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is under the control of StuA, which is responsible for transcriptional activation during acquisition of developmental competence.1 Publication

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		B9WZX0

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

More...SMRi		B9WZX0

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>Domaini594 – 671Carrier 1PROSITE-ProRule annotationAdd BLAST78
Domaini1677 – 1756Carrier 2PROSITE-ProRule annotationAdd BLAST80

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>Regioni76 – 475Adenylation 1Sequence analysis1 PublicationAdd BLAST400
Regioni710 – 975Condensation 1Sequence analysis1 PublicationAdd BLAST266
Regioni1169 – 1563Adenylation 2Sequence analysis1 PublicationAdd BLAST395
Regioni1814 – 2069Condensation 2Sequence analysis1 PublicationAdd BLAST256

<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

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. NRPS13 has the following architecture: A-T-C-A-T-C.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NRP synthetase family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 2 hits
3.30.300.30, 2 hits
3.30.559.10, 2 hits
3.40.50.12780, 2 hits

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00501, AMP-binding, 2 hits
PF00668, Condensation, 2 hits
PF00550, PP-binding, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336, SSF47336, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01733, AA-adenyl-dom, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00455, AMP_BINDING, 2 hits
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 2 hits

<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.

B9WZX0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMALAVGAP SEQRGNLPYN TLKDGPTVDS MKATTDGKNG QGESAFWDTC 
        60         70         80         90        100
VHTVFREHCQ RAPNSPAVNA WDGSFTYAEL DSLSDAIASV LILSGVGPES 
       110        120        130        140        150
IIPIYMQKSR WTTVAILGVL KSGGAFTLLD PSHPRSRVEE ISKEIQARFI 
       160        170        180        190        200
LTSEKLSKQC LEMFSVLVVE HLSRACLPSP GQAGHTRSRP ENAAYIAFTS 
       210        220        230        240        250
GSTGKPKGIV IEHRSYCSGA RSHLKVFGID STSRVLQFAS YAFDVSIMET 
       260        270        280        290        300
LSTLMAGGCL CVMSESERSD PNLFVVSYKN LRISHCFMTP SFARTVPWTE 
       310        320        330        340        350
CCNPPPTLIV GGELMRPSDA RAYKEMGIRC MNAYGPAECS VNVSVQSRVE 
       360        370        380        390        400
AAVDPRNIGY TTGATAWIIS PENPEELMPT GTVGELLVEG PIVGRGYLND 
       410        420        430        440        450
PKATRQAFID TPAWLRRHRK GTSYQHRVYR TGDLASLDSI TGALLLHGRK 
       460        470        480        490        500
DAQVKIRGQR VELPDIEHHL QLTLPNDNAE VIVEKVTFSD DGSEKLIAFV 
       510        520        530        540        550
LVRPSNTDSV IGNTGDRLFL APQSQIMEQF AISKKHLQTH LPSYMVPDIF 
       560        570        580        590        600
IPISTLPQTA SGKTDRKALR TRAAALSRRD VQCFLLSPAG GKRPPSTPKE 
       610        620        630        640        650
ATIRSLYSNV LNLPIDLIGM DDTFLRLGGD SLQAIRLVAA ARAAGLILHA 
       660        670        680        690        700
KDILSSQSTL AEQSKRAGLI QTIDRTWESS PPFALLHGPT RHAIVDLAQK 
       710        720        730        740        750
QCRVPSNLIE DIYPCTALQE GMFITSLKHP GMYTGQIIFD IPDRMELPRL 
       760        770        780        790        800
KAAWLSVVSE NAALRTRIIE THEGLMQAVI VDDFVWEEET DEMLLSSDGE 
       810        820        830        840        850
ALEITKIGVP LVRFRYRPRH RQLMMTIHHS IWDGWSLRLV HEQLQRAYIG 
       860        870        880        890        900
RDLLPSTSYR SFIQYTQELP GADEFWASEL AGVNAPIFPT LPSGNYRPRV 
       910        920        930        940        950
NASHRHVVRN LASTGKEEHT AATYIHLAWS LLVAHYTDAD ETVYGVTVNG 
       960        970        980        990       1000
RSADVPGIEN IVGPTIATVP TRIRVNEEDT VEMALDHVQD ALARMIPYEQ 
      1010       1020       1030       1040       1050
AGLQRISRCS RDASEACRFQ NLLIIEAPTD SDVDCEKNEA GNFSIIGGTT 
      1060       1070       1080       1090       1100
QTGMDYTAFS SYAMMLVFRT SANKSAISFD ITYDAQVIGH DEVERMAHQF 
      1110       1120       1130       1140       1150
EHVLRHIYTL ATGRIGDISF IGPRDIEQVQ QWNSSMPPAD NRFLQELIFA 
      1160       1170       1180       1190       1200
QCSRRPQASA IISWDGSWTY RELWAHSSFF ARQLQRYGVT RGTPVAVCLD 
      1210       1220       1230       1240       1250
RSRWSIAVIL GVLLARGTCV LIDLLAPRQR VRDILQIAGT GILVHSHATA 
      1260       1270       1280       1290       1300
TLTSGLCPTV INVSFLAAQS DSSQPEFPFT LETWGGTPED LAFIIFTSGS 
      1310       1320       1330       1340       1350
TGHPKGIEMP HRTLSTSISH HSAGMRVTSS SRVLHFSSYA FDVSIYEIFT 
      1360       1370       1380       1390       1400
TLAAGGTICV PSEFDRMNNL AGFIQDTQVN WAFLTPSTAR SLNPADVPLL 
      1410       1420       1430       1440       1450
TTLVLGGEAV THESVEVWAK GRSLINGYGP AEATICGVGN IPEAGWKSGV 
      1460       1470       1480       1490       1500
VGRIIGGLGW VTVPSDPNRL AAVGAVGELL LEGPFLARGY LNLPEVTKAA 
      1510       1520       1530       1540       1550
FIDPPSWRTR IPAPSPYSFL YRTGDLVRYQ PDGSIQYVGR KDSRVKLRGQ 
      1560       1570       1580       1590       1600
LVDLGAVEAS VMRVYPAAGQ VVADVLVSEN TARLIAMVKL GPSVTENHDG 
      1610       1620       1630       1640       1650
PMFAAPDLVF NEAAASIQAR LRAIVPAYMV PSMFIPLRHI PRTLTGKTDR 
      1660       1670       1680       1690       1700
RRLRDKILSL SHSDLQRYMM SSSTKTPMSD DNERRLQEIW AEVLQLPCEA 
      1710       1720       1730       1740       1750
IGREDSFLSL GGESLATMKM VALARRVGFM FAVTDVMNNT SLSTLARSRH 
      1760       1770       1780       1790       1800
LITEQAILTS SPSLSLPTIE GESLQEILRP LLNAGHIQGG NDIAAIHPVT 
      1810       1820       1830       1840       1850
AAQAFLVQRY PWSHFQFDLS GAVSPSKLQT ACTALMARFT ILRTVFVEHA 
      1860       1870       1880       1890       1900
GCLLQLVLRE VPNRVHEITT NEPLDDFCNS VCQQQQDVCV VNSTTLPTLF 
      1910       1920       1930       1940       1950
TLVSNRQLNR HRLLLRLAHA QYDLTTIPLI VQSLADEYNR TLRSGFSADF 
      1960       1970       1980       1990       2000
GYYLSHHKRQ NNDDRSHNFW KRYLSGSSMM STNQTADPTT VQERVFHVTG 
      2010       2020       2030       2040       2050
SCIIIPTSHP PDITIATAVK AAVCLVLAAR TGCTDIVIGQ TVDARCSSAD 
      2060       2070       2080       2090       2100
STLDQIVGPC TNYIPYRLSV CCSKTALEYL RSAQAQHTTC LRYSSLDLDQ 
      2110       2120       2130       2140       2150
IVAKCTSWPS STQFGYIVQH QDTGAELALT LGGDTTSLPM TSYGRVFPQG 
      2160       2170       2180       2190       2200
EVWIGSTPCS TGLRIDVIAL SAVLSQKDAQ TMAEEVGAAL EKLLGCGYRR 
      2210 
LSHLIGNTFA T
Length:2,211
Mass (Da):242,786
Last modified:April 14, 2009 - 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:i1E275CDC515B5618
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
AB436628 Genomic DNA Translation: BAH23995.1

<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
AB436628 Genomic DNA Translation: BAH23995.1

3D structure databases

AlphaFoldDBiB9WZX0
SMRiB9WZX0
ModBaseiSearch...

Family and domain databases

Gene3Di1.10.1200.10, 2 hits
3.30.300.30, 2 hits
3.30.559.10, 2 hits
3.40.50.12780, 2 hits
InterProiView 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
PfamiView protein in Pfam
PF00501, AMP-binding, 2 hits
PF00668, Condensation, 2 hits
PF00550, PP-binding, 2 hits
SUPFAMiSSF47336, SSF47336, 2 hits
TIGRFAMsiTIGR01733, AA-adenyl-dom, 1 hit
PROSITEiView protein in PROSITE
PS00455, AMP_BINDING, 2 hits
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 2 hits

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 nameiFTMA_ASPFM
<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: B9WZX0
<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: October 16, 2013
Last sequence update: April 14, 2009
Last modified: May 25, 2022
This is version 60 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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