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UniProtKB - Q0C8L6 (LOVF_ASPTN)

Entry version 105 (02 Dec 2020)
Sequence version 1 (17 Oct 2006)
Previous versions | rss
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Protein

Lovastatin diketide synthase lovF

Gene

lovF

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Status
Reviewed-Annotation score:

Annotation score:4 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

Lovastatin diketide synthase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) (PubMed:10334994, PubMed:12929390, PubMed:21495633). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:22733743). Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178). Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633). The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965). Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900). LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080). LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates (PubMed:21069965).13 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphate2 PublicationsNote: Binds 1 phosphopantetheine covalently.2 Publications

<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: lovastatin biosynthesis

This protein is involved in the pathway lovastatin biosynthesis, which is part of Polyketide biosynthesis.3 Publications
View all proteins of this organism that are known to be involved in the pathway lovastatin biosynthesis and in Polyketide biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei173For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei555For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei893For beta-hydroxyacyl dehydratase activityPROSITE-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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionAcyltransferase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00875

<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:
Lovastatin diketide synthase lovF1 Publication (EC:2.3.1.2442 Publications)
Short name:
LDKS1 Publication
Alternative name(s):
Lovastatin biosynthesis cluster protein F1 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:lovF1 Publication
ORF Names:ATEG_09968
<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>OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
<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 identifieri341663 [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. Circumdati ›
<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
  • UP000007963 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		FungiDB:ATEG_09968

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Lovastatin acts as a hypolipidemic agent that works as inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) which reduces HMG-CoA to mevalonate and is the key step in cholesterol biosynthesis (PubMed:6933445). Lovastatin, simvastatin and related compounds are widely used to treat hypercholesteremia and reduce the risk of cardiovascular disease (PubMed:6933445). Furthermore, statins such as lovastatin were found to be anticancer agents (PubMed:29236027, PubMed:29932104).3 Publications

<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

Loss of lovastatin biosynthesis.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_00004496621 – 2452Lovastatin diketide synthase lovFAdd BLAST2452

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 residuei2410O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

Interacts with LovD.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		33178.CADATEAP00001139

<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		Q0C8L6

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>Domaini2373 – 2450CarrierPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni13 – 384Ketosynthase (KS) domainSequence analysisBy similarityAdd BLAST372
Regioni496 – 790Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisBy similarityAdd BLAST295
Regioni861 – 1166Dehydrogenase (DH) domainSequence analysisBy similarityAdd BLAST306
Regioni1343 – 1528Methyltransferase (CMet) domainSequence analysisBy similarityAdd BLAST186
Regioni1745 – 2064Enoylreductase (ER) domainSequence analysisBy similarityAdd BLAST320
Regioni2088 – 2260Ketoreductase (KR) domainSequence analysisBy similarityAdd BLAST173

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

Multidomain protein; including a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a methyltransferase (CMeT) domain responsible for the incorporation of methyl groups; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.2 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1202, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000022_31_0_1

Database of Orthologous Groups

More...OrthoDBi		19161at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 2 hits
3.40.47.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH_C
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 2 hits
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 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
PS00012, PHOSPHOPANTETHEINE, 1 hit

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

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

Q0C8L6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPLDAPGAP APIAVVGMGC RFGGGATDPQ KLWKLLEEGG SAWSKIPPSR 
        60         70         80         90        100
FNVGGVYHPN GQRVGSCMDP QYRLILEVVY EALEAGMYYI PWFHTWVLTL 
       110        120        130        140        150
HGSAAGIPLE QVSGSKTGVF AGTMYHDYQG SFQRQPEALP RYFITGNAGT 
       160        170        180        190        200
MLANRVSHFY DLRGPSVSID TACSTTLTAL HLAIQSLRAG ESDMAIVAGA 
       210        220        230        240        250
NLLLNPDVFT TMSNLGFLSP DGISYSFDSR ADGYGRGEGV AAIVLKTLPH 
       260        270        280        290        300
AVRDGDPIRL IVRETAINQD GRTLAISTPS GEAQERLIRD CYQKARLDPK 
       310        320        330        340        350
QTSYVEAHGT GTGAGDPLEL GVISAAFPRQ QIQVGSVKAN IGHTEAIPLS 
       360        370        380        390        400
SQSWIPTDGV CRASINNFGF GGANAHAIVE RYAPFAETSM CSPNGYPGNY 
       410        420        430        440        450
DGHVETDQAH IYVLSAKDEN SCMRMVSRLC DYATHAREAD DWQLLANMAY 
       460        470        480        490        500
TLGSRRSNFR WKAVCTAHNL TSLAQNLAGD GMRPSKSAEQ VRLGWVFTGQ 
       510        520        530        540        550
GAQWFAMGQE LSRPETESRV DQAEFSLPLS TALQIALVRL LWSWNIQPVA 
       560        570        580        590        600
VTSHSSGEAA AAYAIGALTA RSAIGISYIR GALTARDRLA SVHKGAMLAV 
       610        620        630        640        650
GLSRSEVGIY IRQVPLQSEE CLVVGCINSP SSVTVSGDLS AIAKLEELLH 
       660        670        680        690        700
ADRIFARRLK VTQAFHSSHM NSMTDAFRAG LTELFGADPS DAANANKDVI 
       710        720        730        740        750
YASPRTGDRM HDFNSLRDPM HWVECMLYPV EFESAFRQMC LDENDHMPKV 
       760        770        780        790        800
DRIIEIGPHG ALGGPIKQIM QLPELAPCDI PYLSCLSRGK SSLSTLRLLA 
       810        820        830        840        850
SELIRAGFPV DLNAINFPRG CEAARVQVLS DLPPYPWNHE TRYWKEPRIS 
       860        870        880        890        900
QSARQRKGPV HDLIGLQEPL NLPLARSWHN VLRVSDLPWL RDHVVGSHIV 
       910        920        930        940        950
FPGAGFVCMA VIGISTLCSS DHESADFSYI LRDVNFAQAL ILPADGEEGI 
       960        970        980        990       1000
DLRLTICAPD QSLGSQDWQR FLVHSITADK NDWTEHCTGL VRVDMDQPAS 
      1010       1020       1030       1040       1050
SLSNPQRADP RPWSRKTAPQ DLWDSLHRVG IRHGPLFQNI TRIESDGRES 
      1060       1070       1080       1090       1100
WCTFAIADTA SAMPHAYESQ HIVHPTTLDS AIQAAYTTLP FAGSRIKSAM 
      1110       1120       1130       1140       1150
VPARVGCMKI SSRLADLEAR DMLRAQAKMH SQSHCALVTD VAVFDEADPF 
      1160       1170       1180       1190       1200
GGPVMELEGL VFQSLGASLG TSGRDSTDTG NTCSSWHWAP DISLVNPVWL 
      1210       1220       1230       1240       1250
ERTLDTGIQK HEIGVILELR RCSVHFIQEA MESLSVGDVA RLSGHLAKFY 
      1260       1270       1280       1290       1300
AWMQAQLACA QNGELGPESS SWTRDNEHAR CSLRSRVVAG STNGEMICRL 
      1310       1320       1330       1340       1350
GSVLPAILRR EVDPLEVMMD GHLLSRYYVD ALKWSRSNAQ ASELVRLCCH 
      1360       1370       1380       1390       1400
KNPRARILEI GGGTGGCTQL VVDSLGPNPP VGRYDFTDVS AGFFEAARKR 
      1410       1420       1430       1440       1450
FAGWQDVMDF RKLDIEDDPE AQGFVCGSYD VVLACQVLHA TSNMQRTLTN 
      1460       1470       1480       1490       1500
VRKLLKPGGK LILVETTRDE LDLFFTFGLL PGWWLSEEPE RQSTPSLSPT 
      1510       1520       1530       1540       1550
MWRSMLHATG FNGVEVEARD CDSDEFYMIS TMMSTAVQAT PTSCSDKLPE 
      1560       1570       1580       1590       1600
VLLVYVDSST PMSWISDLQG AIRCRNCSVT SLQALRQVPP TEGQMCVFLG 
      1610       1620       1630       1640       1650
EMEHSMLGSV TNDDFTLLTS MLQLAGGALW VTRGATMKSD DPLKALHLGL 
      1660       1670       1680       1690       1700
LRTMRNESHG KRFVSLDLDP SRNPWTGDSR DAIVSVLDLV SMSDEKEFDY 
      1710       1720       1730       1740       1750
AERGGVIHVP RAFSDSINGG EEDGYALEPF QDSQHLLRLD IRTPGLLDSL 
      1760       1770       1780       1790       1800
YFRKRSVDPY EPDKLPDDWV EIEPRAFGLN FRDIMVAMGQ LESNVMGFEC 
      1810       1820       1830       1840       1850
AGVVTSLSET ARTIAPGLAV GDRVCALMNG HWASRVTTSR TNVVRIPETL 
      1860       1870       1880       1890       1900
SFPHAASIPL AFTTAYISLY TVARILPGET VLIHAGAGGV GQAAIILAQL 
      1910       1920       1930       1940       1950
TGAEVFTTAG SEAKRNHLID KFHLDPDHVF SSRDSSFVDG IKTRTSGKGV 
      1960       1970       1980       1990       2000
DVVLNSLAGP LLQKSFDCLA RFGRFVEIGK KDLEQNSRLD MSTFVRNVSF 
      2010       2020       2030       2040       2050
SSVDILYWQQ AKSAEIFQAL SEVILLWGRT AIGLIHPISE YPMSALEKAF 
      2060       2070       2080       2090       2100
RTMQSGQHVG KIVVTVAPDD AVLVRQERMP LFLKPNVSYL VAGGLGGIGR 
      2110       2120       2130       2140       2150
RICEWLVDRG ARYLIILSRT ARVDPVVTSL QERGCTVSVQ ACDVADKSQL 
      2160       2170       2180       2190       2200
EAALQQCRAE NLPPIRGVIQ GAMVLKDALV SQMTADGFHA ALRPKVQGSW 
      2210       2220       2230       2240       2250
NLHRIASDVD FFVMLSSLVG VMGGAGQANY AAAGAFQDAL AEHRMAHNQP 
      2260       2270       2280       2290       2300
AVTIDLGMVQ SIGYVAETDS AVAERLQRIG YQPLHEEEVL AVLEQAMSPV 
      2310       2320       2330       2340       2350
CSPTAPTRPA VIVTGINTRP GPHWAHADWM QEARFAGIKY RDPLRDNNGA 
      2360       2370       2380       2390       2400
LPLTLAEDDN LHARLNRATS QQASIAVIME AMGRKLISMF GLTDSEMSAT 
      2410       2420       2430       2440       2450
QTLAGIGVDS LVAIELRNWI TARFNVDISV FELMEGRTIA KVAEVVLQRY 

KP
Length:2,452
Mass (Da):268,120
Last modified:October 17, 2006 - 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:i4CB919463978E0D7
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
CH476609 Genomic DNA Translation: EAU29417.1

NCBI Reference Sequences

More...RefSeqi		XP_001209270.1, XM_001209270.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		EAU29417; EAU29417; ATEG_09968

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4319643

<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
CH476609 Genomic DNA Translation: EAU29417.1
RefSeqiXP_001209270.1, XM_001209270.1

3D structure databases

SMRiQ0C8L6
ModBaseiSearch...

Protein-protein interaction databases

STRINGi33178.CADATEAP00001139

Genome annotation databases

EnsemblFungiiEAU29417; EAU29417; ATEG_09968
GeneIDi4319643

Organism-specific databases

EuPathDBiFungiDB:ATEG_09968

Phylogenomic databases

eggNOGiKOG1202, Eukaryota
HOGENOMiCLU_000022_31_0_1
OrthoDBi19161at2759

Enzyme and pathway databases

UniPathwayiUPA00875

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 2 hits
3.40.47.10, 2 hits
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH_C
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 2 hits
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 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 nameiLOVF_ASPTN
<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: Q0C8L6
<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: April 22, 2020
Last sequence update: October 17, 2006
Last modified: December 2, 2020
This is version 105 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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