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Entry version 119 (11 Dec 2019)
Sequence version 1 (26 Apr 2005)
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Protein

Fatty acid synthase subunit alpha

Gene

atnF

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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 subunit alpha; part of the gene cluster that mediates the biosynthesis of aspercryptins, linear lipopeptides built from six amino acids including 2 highly unusual and nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584). The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin biosynthesis is the generation of the fatty acid precursors, octanoic and dodecanoic acids, by the FAS subunits atnF and atnM (PubMed:27310134, PubMed:26563584). The fatty acid precursors are likely transformed into the corresponding alpha-amino fatty acids in three steps (PubMed:27310134, PubMed:26563584). First, they are hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized to the corresponding alpha-keto acids by the NAD(P)-dependent oxidoreductase atnD, and finally converted to the alpha-amino fatty acids by the PLP-dependent aminotransferases atnH or atnJ (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated, and covalently tethered to the NRPS atnA by its fourth and sixth adenylation domains (PubMed:27310134). The second module of atnA is the Thr module and contains an epimerase (E) domain responsible for the epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally, despite atnA having only one epimerase domain, the first amino acid of aspercryptin A1 is D-Ser, suggesting that serine is either loaded directly as D-Ser on the first module or that the epimerase domain in the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134). After condensation of the hexapeptide of aspercryptin, the C-terminal reductase (TE) domain might be involved in the reductive release and production of the aldehyde hexapeptide (PubMed:26563584). Further reduction would generate aspercryptins (PubMed:27310134, PubMed:26563584). The variety of aspercryptins produced reflects the flexibiliy of the atnA NRPS, allowing incorporation of alanine instead of serine, valine for isoleucine, and a C10 fatty amino alcohol instead of the C12 version (PubMed:27310134). AtnB seems to be involved in the selectivity for Ile versus Val by the third module (PubMed:26563584). Moreover, type B, C and D aspercryptins have an additional N-terminal cichorine, acetyl and propionyl group respectively (PubMed:27310134).3 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: 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_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 sitei1217PROSITE-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 functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNADP

<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 subunit alpha1 Publication (EC:2.3.1.861 Publication)
Alternative name(s):
Aspercryptin biosynthesis cluster protein F1 Publication
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)
<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:atnF1 Publication
ORF Names:ANIA_07880
<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>OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
<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 identifieri227321 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
<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
  • UP000000560 <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: Chromosome II
  • UP000005890 Componenti: Unassembled WGS sequence

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Eliminates more than 99.5% of aspercryptin production (PubMed:26563584).1 Publication

<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_00004441291 – 1659Fatty acid synthase subunit alphaAdd BLAST1659

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 residuei195O-(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.

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 aspercryptin cluser-specific transcription factor atnN (PubMed:27310134).1 Publication

<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
162425.CADANIAP00003896

<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>Domaini160 – 235CarrierPROSITE-ProRule annotationAdd BLAST76

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>Regioni588 – 826Ketoreductase (KR) domainBy similarityAdd BLAST239
Regioni934 – 1564Ketosynthase (KS) domainBy similarityAdd BLAST631

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000177974

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5AV00

KEGG Orthology (KO)

More...
KOi
K00667

Identification of Orthologs from Complete Genome Data

More...
OMAi
TFSQDEM

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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016035 Acyl_Trfase/lysoPLipase
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
IPR009081 PP-bd_ACP
IPR016039 Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF52151 SSF52151, 1 hit
SSF53901 SSF53901, 2 hits

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.

Q5AV00-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVAAQDDGAQ RKLAHTLLLE LMSYQFASPV RWIETQDVVL GQYRAERIIE
60 70 80 90 100
IGPAATLTNM IKQTVQSKFL HSDRASLLQR QLLASEKQGK DIYYEDDGVG
110 120 130 140 150
IGTGAEAPAP SAKTQAQASG GAGTIAGAGS STAPVTAPPA PAAAKAVPAG
160 170 180 190 200
GMQAIEDRQA QAFEIVRTLL SRILKIALTD VVGTQSIKSL SGGRSTLENE
210 220 230 240 250
IIGDLASEFG SLPDRAEDLT VNDLSAALQK TFTGQMRKVI LKMLHAMFAS
260 270 280 290 300
KMPGQFTVAT ARTYLHSRWG LGSGRQDSVL LLAIAQQPGS RLKEEAEARS
310 320 330 340 350
FFDGLVQFYA DEHGLTLGAN SGAADETSGL GGGLVMDQKT LAALTGGQQE
360 370 380 390 400
LSKALLKIYA KHLDIDLDGD RRALHDLQAT VEKDLRLALD QIHQELGEDF
410 420 430 440 450
TDGVQPVFSA RKARRFDSAW SWALQDLLQL YYEVSRTGGE TEVDLAAKRC
460 470 480 490 500
KHIEDAADPR LLDVLQRIVG RFEQQPVLSS MFTQLAQRCR DSLLHGPRYL
510 520 530 540 550
ARPDQQGPRT TISAEGDITY TEQERAEPVP LADLVYLPKS TEAAPLEPFL
560 570 580 590 600
HLKQRTGGSS AWTYSHDLTE QYRAVLEQAT TVGESFAGRS VLITGAGVGS
610 620 630 640 650
IGAEVLKGLL AGGARVIVTT SRFSSSVVRK YQDLYTQVGS RGSELVVVPF
660 670 680 690 700
NQASVQDVTA LVNYIYDAQG GLHWDLDHIL PFAAMPENGR TIEKIDPHSE
710 720 730 740 750
LAHRTMMVNT LRLLGAVKAR KEAQGSRTRP TQVILPLSPN HGVFGGDGLY
760 770 780 790 800
SESKLGLEAL FNRWHSEDWS DYLSVCGAVI GWTRGTGLMS GNNLVAEGIE
810 820 830 840 850
ELGCRTFSQQ EMAQCLLCLM FNTMCSLCEE APLYADLSGR MGAVQNLRQK
860 870 880 890 900
VQELRTEINE TANTRRALLE ELAMEARCSE GPTPTIDSEP AKATATPTLT
910 920 930 940 950
AHVRLDFPPT VDYNQEIKPL TADLQGMVDL DRVVVVTGFG EIGPWGNART
960 970 980 990 1000
RWEMEAYGEF SLEGCVEMAW LMGLIRYENS SSPGWVDAKT NERVHDHEVK
1010 1020 1030 1040 1050
HKYEEHILSH TGIRLIEPDR FGANYHPEHK QLLHEVLIQE DFPELEVPEA
1060 1070 1080 1090 1100
TAQQMKLEHG NKVDIIPDPE GGDQCRVVLK KGAKLMVPKA LRLDRMVIGQ
1110 1120 1130 1140 1150
IPTGWDARKY GIPEDVISQV DPVTLYMLAC SIEALLSSGI TDPYEIYRYI
1160 1170 1180 1190 1200
HVSEAGNCVG SSLGGFNSLQ QMYRGRYMEK EVQKDILQET FVNTIGAWMN
1210 1220 1230 1240 1250
MLLMSSAGPI RTPVGACATA IESVELGYDT LISGKAKFCF VGGGDDFGEE
1260 1270 1280 1290 1300
VLYEFANMKA TANTVDEFEQ GREASEMSRP AASTRNGFME SHGCGVQILT
1310 1320 1330 1340 1350
TARLAIEMGL PVRGVIAFVE TSSDKASRSV PAPGRGILSK AREVRSSSPS
1360 1370 1380 1390 1400
SSLISSPLLN ISNRRKRLDF RKKQIEFARE TALEELQLEI AHVEESEVED
1410 1420 1430 1440 1450
YIRERTAQIN AEAQKDLRNA QYHLGNAFWQ NDPSIAPLRG ALAVWGLTID
1460 1470 1480 1490 1500
DLDVASFHGT STKLNEKNEC SLIQAQLSHL GRAKGNVILG VFQKYLTGHP
1510 1520 1530 1540 1550
KGAAGAWMLN GALQILDTGI VPGNRNLDNV EAELQKNEQI AFLNRSLDTG
1560 1570 1580 1590 1600
RGSMRAVSVT SFGFGQKGAQ TIVVHPKYLF ATLEEQEYEE YLDKRAKRQK
1610 1620 1630 1640 1650
KADSFFYRGL ASNRLFELKT APPWAPQKEL ETLLDPTPPQ TNVDDRVARS

IVQQESAEP
Length:1,659
Mass (Da):181,995
Last modified:April 26, 2005 - 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:i572041ADC2308725
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BN001302 Genomic DNA Translation: CBF73444.1
AACD01000135 Genomic DNA Translation: EAA59534.1

NCBI Reference Sequences

More...
RefSeqi
XP_681149.1, XM_676057.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CBF73444; CBF73444; ANIA_07880
EAA59534; EAA59534; AN7880.2

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2869007

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ani:AN7880.2

<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
BN001302 Genomic DNA Translation: CBF73444.1
AACD01000135 Genomic DNA Translation: EAA59534.1
RefSeqiXP_681149.1, XM_676057.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

STRINGi162425.CADANIAP00003896

Genome annotation databases

EnsemblFungiiCBF73444; CBF73444; ANIA_07880
EAA59534; EAA59534; AN7880.2
GeneIDi2869007
KEGGiani:AN7880.2

Phylogenomic databases

HOGENOMiHOG000177974
InParanoidiQ5AV00
KOiK00667
OMAiTFSQDEM
OrthoDBi39339at2759

Family and domain databases

Gene3Di3.40.47.10, 3 hits
InterProiView protein in InterPro
IPR016035 Acyl_Trfase/lysoPLipase
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
IPR009081 PP-bd_ACP
IPR016039 Thiolase-like
PfamiView protein in Pfam
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
SUPFAMiSSF51735 SSF51735, 1 hit
SSF52151 SSF52151, 1 hit
SSF53901 SSF53901, 2 hits
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 nameiATNF_EMENI
<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: Q5AV00
Secondary accession number(s): A0A1U8QSZ5, C8V3Y5
<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: May 23, 2018
Last sequence update: April 26, 2005
Last modified: December 11, 2019
This is version 119 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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