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Entry version 40 (11 Dec 2019)
Sequence version 1 (01 May 2013)
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Protein

Fatty acid synthase alpha subunit hexA

Gene

hexA

Organism
Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini)
Status
Reviewed-Annotation score:

Annotation score:5 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 transcript 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

Fatty acid synthase alpha subunit; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690).1 PublicationBy similarity3 Publications2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">'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.1 Publication1 Publication
View all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei1135PROSITE-ProRule annotation1
Active sitei1135For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1569MagnesiumBy similarity1
Metal bindingi1669MagnesiumBy similarity1

<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 functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandMagnesium, Metal-binding, NADP

<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_and_taxonomy_section">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:
Fatty acid synthase alpha subunit hexABy similarity (EC:2.3.1.86By similarity)
Including the following 2 domains:
3-oxoacyl-[acyl-carrier-protein] reductaseBy similarity (EC:1.1.1.100By similarity)
Alternative name(s):
Beta-ketoacyl reductaseBy similarity
3-oxoacyl-[acyl-carrier-protein] synthaseBy similarity (EC:2.3.1.41By similarity)
Alternative name(s):
Dothistromin biosynthesis protein hexA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:hexA1 Publication
ORF Names:DOTSEDRAFT_66976
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiDothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri675120 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesMycosphaerellaceaeDothistroma
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000016933 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004434581 – 1692Fatty acid synthase alpha subunit hexAAdd BLAST1692

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 residuei125O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of the acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.Curated

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 positively regulated by the dothistromin-specific transcription factors aflR and aflJ (PubMed:23207690, PubMed:25986547).2 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
64363.EME39096

<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_and_domains_section">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>Domaini90 – 174CarrierPROSITE-ProRule annotationAdd BLAST85

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>Regioni508 – 746Ketoreductase (KR) domainSequence analysisBy similarityAdd BLAST239
Regioni954 – 1419Ketosynthase (KS) domainSequence analysisBy similarityAdd BLAST466
Regioni1569 – 1571Acetyl-CoA bindingBy similarity3
Regioni1615 – 1631Acetyl-CoA bindingBy similarityAdd BLAST17
Regioni1639 – 1642Acetyl-CoA bindingBy similarity4
Regioni1668 – 1670Acetyl-CoA bindingBy similarity3

<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

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
PLWAICQ

Database of Orthologous Groups

More...
OrthoDBi
39339at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.47.10, 3 hits
3.90.470.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008278 4-PPantetheinyl_Trfase_dom
IPR037143 4-PPantetheinyl_Trfase_dom_sf
IPR040899 Fas_alpha_ACP
IPR026025 FAS_alpha_yeast
IPR041550 FASI_helical
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR036291 NAD(P)-bd_dom_sf
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR009081 PP-bd_ACP
IPR004568 Ppantetheine-prot_Trfase_dom
IPR002347 SDR_fam
IPR016039 Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01648 ACPS, 1 hit
PF00106 adh_short, 1 hit
PF18325 Fas_alpha_ACP, 1 hit
PF18314 FAS_I_H, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000454 FAS_yeast_alpha, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00825 PKS_KS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF53901 SSF53901, 2 hits
SSF56214 SSF56214, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00556 pantethn_trn, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

M2YJJ3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQKTIKRKI QSAERPAEAD VAFLASTQHS KDLCYEYDAP EEVAVEEPVD
60 70 80 90 100
ETPAPETAPE RPPLSRAKTA AVKPQETAAP TTATIADVPL SAEEIVRALV
110 120 130 140 150
ARKLKKPILS IPTSKSVKEL CNGKSTLQNE IVGDFHSEFT NLPDRPEDIP
160 170 180 190 200
LKELVPASQS LMLGRVSSAL LSKLVSSKMP ARFNADAIGK YLASKWGLGP
210 220 230 240 250
LRSVAVMLFA IAAEPEARLG SVAAAEKYLD DTAAKYAEWA GITLQERSTQ
260 270 280 290 300
SSAGGGGSSG TVDPTVLAEL TKTNTRLAKR QFQALAEYLQ VDLMKPSSEQ
310 320 330 340 350
ESEALAVELQ QKLDAWTAEF SEEFLAGVAP TFSEKKSRRY NAWWNAARQD
360 370 380 390 400
VLALFSGNLQ EDLSRDAAAL EAFLDRLSNR AGESLLAMTR SLSRRNQANA
410 420 430 440 450
IPGLTDIARR AEKAISSCID RPATAKVHLP ATRPRTTVSD EGDIKFNEVP
460 470 480 490 500
RPDVSGHAAY ADVLQAKDLN GHPAAARFVS LKSAHSHTDL TNGMLDRIRT
510 520 530 540 550
ALDSGMSFAG KNILITGAGQ GSIGAEVVRI LLTGGARVIV TTSREPSSTA
560 570 580 590 600
KYFQQMYEES GAKGSELILT RFNQASAKDC ENLVDHIYDS SGLDRDLDAV
610 620 630 640 650
LPFAAAPEGG TEIQDVGAKN ELVHRLMLAS VFRMLGRVIK NKRDRSIDCH
660 670 680 690 700
PTQVLLPLSP NHGTFGGDGM YAESKLGLES LVNRVQSESW SDELAICGVK
710 720 730 740 750
IGWTRGTGLM NANDIVAEAI EDHGVLTFSV QEMAFNIAML MTPELVDLCE
760 770 780 790 800
NAPLMADFGG GLSALEDCAK ILSAARTEIN TAADVARAVK AEDDLERAAS
810 820 830 840 850
RTLPAPSSTS PVAKKSMLRI GFPRLPDFEL ELSPLEHLRD IKDPSETVVV
860 870 880 890 900
VGFSELGPWG SARLRWEIES KGDFSQVGYM EMAWMMDLIK HVDGPTKNGY
910 920 930 940 950
YVGWVDSKTG ESVHDAEIEA RYGEVIRKHS GIRFVDPEGS AGYDPSKKEY
960 970 980 990 1000
LHEVAVEEDL PEFEASSATA EAFRLRHGTN VSISPIEGTE NCRVQVKRGA
1010 1020 1030 1040 1050
SIKIPKSVPF TWGSVAGQLP KGWSPKKYGI PEDLIPQLDP VSLYTICCVA
1060 1070 1080 1090 1100
EAFYSAGITD PLEIFKYIHL SEIGNFLGSS MGGALKTRQM YRDIYLDKDI
1110 1120 1130 1140 1150
QSDVLQETYL NTTGAWVNML LLGSTGPIKT PMGACATGVE SIDSAFESIM
1160 1170 1180 1190 1200
SDKTRMCIVG GFDDFHEDES YGFSTMKATV NVEEELAKGR LPSEMSRPTA
1210 1220 1230 1240 1250
ESRSGFVEAH GCGVQILCRG DVALEMGLPV YGIIAGSTMA ADKVGRSVPA
1260 1270 1280 1290 1300
PGQGILTFAR ETGQAQLDKS SPSTNTTSRT SSVSLARRGA TVSPLRASLD
1310 1320 1330 1340 1350
AWGLTIDDLD VASLHGTSTK ANDLNEPEVI CKQMDHLGRT PGRPLWAICQ
1360 1370 1380 1390 1400
KSVTGHPKAP AAAWMLNGCL QVMDSRTIPA NRNADNVDPA LQTATHLCFP
1410 1420 1430 1440 1450
TRPVRVQDVR AFILTSFGFG QKGGQVVGVA PKYFFATLDE EVYKDYSVRV
1460 1470 1480 1490 1500
TKRSKTADRA YAKALMSNAI VKVQDHSPYE QEDQSRIFMD PLSRITEDAE
1510 1520 1530 1540 1550
TGSYHFDTKD IRNVADVKAR LTRLVRGERL NARPDAASGL AQAARSAQAW
1560 1570 1580 1590 1600
IEKQTGGRSS VDTSTVGIDL VDLSAFSAHE NETFIERNFT EQEKAFAKQS
1610 1620 1630 1640 1650
LDQKMAFASR WAAKEAVFKC LHTQTKGAGA AMKDIEIVKS DNAPKVKLHN
1660 1670 1680 1690
DCIKAGRKAG LEDIQLSISH GEDCLIAVAI GIAGNGPAKY TL
Length:1,692
Mass (Da):183,262
Last modified:May 1, 2013 - 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:iB556CA38EFA88391
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
KB446546 Genomic DNA Translation: EME39096.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
EME39096; EME39096; DOTSEDRAFT_66976

<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
KB446546 Genomic DNA Translation: EME39096.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi64363.EME39096

Genome annotation databases

EnsemblFungiiEME39096; EME39096; DOTSEDRAFT_66976

Phylogenomic databases

OMAiPLWAICQ
OrthoDBi39339at2759

Family and domain databases

Gene3Di3.40.47.10, 3 hits
3.90.470.20, 1 hit
InterProiView protein in InterPro
IPR008278 4-PPantetheinyl_Trfase_dom
IPR037143 4-PPantetheinyl_Trfase_dom_sf
IPR040899 Fas_alpha_ACP
IPR026025 FAS_alpha_yeast
IPR041550 FASI_helical
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR036291 NAD(P)-bd_dom_sf
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR009081 PP-bd_ACP
IPR004568 Ppantetheine-prot_Trfase_dom
IPR002347 SDR_fam
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF01648 ACPS, 1 hit
PF00106 adh_short, 1 hit
PF18325 Fas_alpha_ACP, 1 hit
PF18314 FAS_I_H, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PIRSFiPIRSF000454 FAS_yeast_alpha, 1 hit
SMARTiView protein in SMART
SM00825 PKS_KS, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF53901 SSF53901, 2 hits
SSF56214 SSF56214, 1 hit
TIGRFAMsiTIGR00556 pantethn_trn, 1 hit
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 1 hit
PS50075 CARRIER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiHEXA_DOTSN
<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: M2YJJ3
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 28, 2018
Last sequence update: May 1, 2013
Last modified: December 11, 2019
This is version 40 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
  2. SIMILARITY comments
    Index of protein domains and families
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