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Entry version 107 (10 Feb 2021)
Sequence version 1 (26 Apr 2005)
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Protein

Fatty acid synthase beta subunit aflB

Gene

atnM

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 beta subunit; 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%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: 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.

<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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNAD, 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%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:
Fatty acid synthase beta subunit aflB1 Publication (EC:2.3.1.861 Publication)
Alternative name(s):
Aspercryptin biosynthesis cluster protein M1 Publication
Including the following 5 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydrataseBy similarity (EC:4.2.1.59By similarity)
Enoyl-[acyl-carrier-protein] reductase [NADH]By similarity (EC:1.3.1.9By similarity)
[Acyl-carrier-protein] acetyltransferaseBy similarity (EC:2.3.1.38By similarity)
[Acyl-carrier-protein] malonyltransferaseBy similarity (EC:2.3.1.39By similarity)
S-acyl fatty acid synthase thioesteraseBy similarity (EC:3.1.2.14By similarity)
<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:atnM1 Publication
ORF Names:ANIA_07873
<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>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%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 identifieri227321 [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. Nidulantes
<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
  • UP000000560 <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: 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

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004441301 – 2111Fatty acid synthase beta subunit aflBAdd BLAST2111

<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%5Fsection">'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%5Fsection">'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.CADANIAP00003889

<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
Q5AV07

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>Domaini1606 – 1708MaoC-likeSequence analysisAdd BLAST103

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>Regioni200 – 565Acetyltransferase (AT) domainBy similarityAdd BLAST366
Regioni618 – 863Enoyl reductase (ER) domainBy similarityAdd BLAST246
Regioni1195 – 1688Dehydratase (DH) domainBy similarityAdd BLAST494
Regioni1727 – 2091Malonyl/palmitoyl transferase (MT/PT) domainSequence analysisBy similarityAdd BLAST365

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QQJX, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000114_5_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5AV07

Identification of Orthologs from Complete Genome Data

More...
OMAi
YHAELAC

Database of Orthologous Groups

More...
OrthoDBi
8490at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 2 hits
3.40.366.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013785, Aldolase_TIM
IPR016452, Fas1/AflB-like
IPR013565, Fas1/AflB-like_central
IPR040883, FAS_meander
IPR003965, Fatty_acid_synthase
IPR029069, HotDog_dom_sf
IPR039569, MaoC-like_dehydrat_N
IPR002539, MaoC-like_dom
IPR032088, SAT

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08354, DUF1729, 1 hit
PF17951, FAS_meander, 1 hit
PF13452, MaoC_dehydrat_N, 1 hit
PF01575, MaoC_dehydratas, 1 hit
PF16073, SAT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005562, FAS_yeast_beta, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01483, FASYNTHASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52151, SSF52151, 2 hits
SSF54637, SSF54637, 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.

Q5AV07-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFNFPHPAID LASRMKSSPL MAGGSSSASS EDLFSPPMME DLDTPMTEYP
60 70 80 90 100
MGSPPRMPYR GEDIEIAFLR SEASIKKSSL FNDKFAATLD DLSARPIDSA
110 120 130 140 150
SLIGKLQSMT RSVREILDSG DQLVHEDGPQ EILKQFVRVV NKHLCQDEDI
160 170 180 190 200
HTVLAPLALE PEEKFHIIQT YYQAISMTQF VSPKWTSSLL SDALCRRANI
210 220 230 240 250
VTVFNGQGVE GYFSELQHLY DTYGGLLAEP LYALSKQLKG LASDVRAQDM
260 270 280 290 300
YPHGLDVIGW LENPEARPST DYLLSAPVSQ PLIGLVQLLN YAITCKILNK
310 320 330 340 350
SPGEFARHLS GSAGHSQGIV VAAMLATVVS WPTFFDAAST ALQVLFWIGC
360 370 380 390 400
RSQQCYPSHS IPPSLVDQSE RLSPMLSVKG ASRESLLKYL DEHNRHLPPA
410 420 430 440 450
QQGSLALING RQQFVVAGNP LSLYAFANKL RAASNNSSTT NTARVPFSQR
460 470 480 490 500
PLLITARFLP ISVPFHTSLL EDAEAQILED LRSVHVPGNS LLFPVLRTDN
510 520 530 540 550
GADLREFDNL VPELVHMVVC GVVDWDRATR FPTATHLLDF GPGRETGIGA
560 570 580 590 600
LLASTKAGTA ARVILSTTLT GPSKKTLGYM PELLSRRRPV VYNTSWEQDF
610 620 630 640 650
APRLVRVGDD ILLDTKFSRA LGLPPVMVAG MTPTTVSPDF VAEVINANYH
660 670 680 690 700
IEIAGGGYHD AAGMRSALTR LVNLIPAGRG ITVNLIYANP RAMGWQIPLL
710 720 730 740 750
VQLRQEGLPI TGLTIGAGVP SPDIASEYIR DLGLSHISFK PGSKEAIDNV
760 770 780 790 800
LRIAESNPGF PIILQWTGGR AGGHHSYEDF HEPILDRYAQ IRAYPNLILV
810 820 830 840 850
AGSGFGGSDD TIPYITGSWS KKLGYAAMPF DGVLVGSRVM TAKEARTSPA
860 870 880 890 900
VKQAIVDTPG VPDSQWEGTY KKATGGIITV KSEMGEPIHK LATRGVLLWA
910 920 930 940 950
ELDKEVFSLP AAQQVQELQR RKGSLMKRLN ADFQKVWFGI DQQGNPVEIS
960 970 980 990 1000
EMTYAEVLTR AVDLLYLKDQ QAWIDPSYRS FVADFIRCVE NRLSARQPRP
1010 1020 1030 1040 1050
RAVFQSALQL DRPQVFLSEF LQAYPAALED VIVREDEDQL VKLYKQPGRK
1060 1070 1080 1090 1100
PLPFIVALDE SFEYWFKKDS LWQSERLEAV TNQDVGRICI LHGPVAAQYT
1110 1120 1130 1140 1150
KVANEPVKQI LDNIHKPHVQ AILKQQYAGD TSRVPTLDYL YSAGAVSPML
1160 1170 1180 1190 1200
SPQDELLLPH VKHSRSYDPP TLAYDLEGPE ENLPTEKQWL ALIGGTKPSW
1210 1220 1230 1240 1250
RKALLTLNEI VQGKMLVENP IKGLFAPRAG LSVRIIQAGR PQKTVILMRQ
1260 1270 1280 1290 1300
KSSQGQEKDE ATVEIRALST SEIMLTLRAP MTGGSAGNPP VDLVLYFTYK
1310 1320 1330 1340 1350
PTYGNNPIHE VMGTRNQRIS RFYEQLWVGN AGDEGTSLQK SADDVQVLTR
1360 1370 1380 1390 1400
EAILNFTKAI DNRNSAYNGK KNSKLLAPLD MAIVVAWKPL MRCLFTDAVN
1410 1420 1430 1440 1450
GDILKLLHLK NDFRVIDNAS PMREGDVLSS TAAIESIRIR PDSGKVVRAV
1460 1470 1480 1490 1500
ATIFKKGTPI ITVASEFILQ GRYEDYHNTF ETKEEQVYKL PLKSKRDVVL
1510 1520 1530 1540 1550
LASKPWFRIA AADLSLDDHL DDELTFRLKS SYHFRDANTY SQIETCGTVS
1560 1570 1580 1590 1600
CAVGNKDMTI GTVMFKSNSH FLKNPVIDFL TRRGFAYDEV KQLPNAVPLA
1610 1620 1630 1640 1650
ADVRIEMPTS SDQYAAASGD SNPIHLSRAF ARYAGHNEGR VIHGMQTSGL
1660 1670 1680 1690 1700
VRGVVELHAA GNDPRRMKAW SASFKGKVSP GETLLVDISH TGMNNGRLIV
1710 1720 1730 1740 1750
VATARSESSS VEVFRATAEV AQKPGAYLFT GQGSQKPAMG MDLYETSQAA
1760 1770 1780 1790 1800
RDVWHTAEQF FVNTYGISIL EIVRNNPKEY TVHFGGSRGK AIRENYISLD
1810 1820 1830 1840 1850
FEVVNEQGEI ESVRAFQEIT PSSRSFTYTS SGGLLHETIF TQPALVVMEL
1860 1870 1880 1890 1900
ARFHDMRARG LINEDSCYAG HSLGEYAALA AMGEVFTVEG VTAAVFYRGL
1910 1920 1930 1940 1950
TMQKSIELDR SGRDYSMVAA NPSRVSKNLS ESDLCAIVDS IEAATGGLCE
1960 1970 1980 1990 2000
IVNFNVESTQ YVCAGDLRSL DCLAGVLDSL VAHPEHLTSL ETLNASVPAI
2010 2020 2030 2040 2050
VASCLAQTDK KPTPLVLQRG KATIPLKVNV PFHSSLLRPG ADTFRRALRK
2060 2070 2080 2090 2100
AIPEHMVRPE KLIGRYIPNL TAMPFELSKG YFENVLAISE SPFVREILER
2110
WDDNNVAVAV C
Length:2,111
Mass (Da):232,678
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:iC8292622D4E784B1
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: CBF73431.1
AACD01000135 Genomic DNA Translation: EAA59527.1

NCBI Reference Sequences

More...
RefSeqi
XP_681142.1, XM_676050.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CBF73431; CBF73431; ANIA_07873
EAA59527; EAA59527; AN7873.2

Database of genes from NCBI RefSeq genomes

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GeneIDi
2868965

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ani:AN7873.2

<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: CBF73431.1
AACD01000135 Genomic DNA Translation: EAA59527.1
RefSeqiXP_681142.1, XM_676050.1

3D structure databases

SMRiQ5AV07
ModBaseiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00003889

Genome annotation databases

EnsemblFungiiCBF73431; CBF73431; ANIA_07873
EAA59527; EAA59527; AN7873.2
GeneIDi2868965
KEGGiani:AN7873.2

Phylogenomic databases

eggNOGiENOG502QQJX, Eukaryota
HOGENOMiCLU_000114_5_0_1
InParanoidiQ5AV07
OMAiYHAELAC
OrthoDBi8490at2759

Family and domain databases

Gene3Di3.20.20.70, 2 hits
3.40.366.10, 1 hit
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013785, Aldolase_TIM
IPR016452, Fas1/AflB-like
IPR013565, Fas1/AflB-like_central
IPR040883, FAS_meander
IPR003965, Fatty_acid_synthase
IPR029069, HotDog_dom_sf
IPR039569, MaoC-like_dehydrat_N
IPR002539, MaoC-like_dom
IPR032088, SAT
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08354, DUF1729, 1 hit
PF17951, FAS_meander, 1 hit
PF13452, MaoC_dehydrat_N, 1 hit
PF01575, MaoC_dehydratas, 1 hit
PF16073, SAT, 1 hit
PIRSFiPIRSF005562, FAS_yeast_beta, 1 hit
PRINTSiPR01483, FASYNTHASE
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SUPFAMiSSF52151, SSF52151, 2 hits
SSF54637, SSF54637, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<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 nameiATNM_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: Q5AV07
Secondary accession number(s): A0A1U8QFM2, C8V3X8
<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: May 23, 2018
Last sequence update: April 26, 2005
Last modified: February 10, 2021
This is version 107 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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