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Entry version 119 (02 Dec 2020)
Sequence version 1 (01 Nov 1999)
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Protein

Lovastatin diketide synthase lovF

Gene

lovF

Organism
Aspergillus terreus
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 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 sitei183For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei635For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei973For 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

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-18789

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
<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
<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 identifieri33178 [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. Circumdati

<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_00004302681 – 2532Lovastatin diketide synthase lovFAdd BLAST2532

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 residuei2490O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9Y7D5

<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

<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
Q9Y7D5

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>Domaini2453 – 2530CarrierPROSITE-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 – 433Ketosynthase (KS) domainSequence analysis2 PublicationsAdd BLAST421
Regioni545 – 870Malonyl-CoA:ACP transacylase (MAT) domainSequence analysis2 PublicationsAdd BLAST326
Regioni941 – 1246Dehydrogenase (DH) domainSequence analysis2 PublicationsAdd BLAST306
Regioni1423 – 1607Methyltransferase (CMet) domainSequence analysis2 PublicationsAdd BLAST185
Regioni1825 – 2144Enoylreductase (ER) domainSequence analysis2 PublicationsAdd BLAST320
Regioni2168 – 2340Ketoreductase (KR) domainSequence analysis2 PublicationsAdd 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

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, 1 hit
3.40.47.10, 1 hit

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, 1 hit
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.

Q9Y7D5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPLDAPGAP APIAMVGMGC RFGGGATDPQ KLWKLLEEGG SAWSKIPPSR
60 70 80 90 100
FNVGGVYHPN GQRVGSMHVR GGHFLDEDPA LFDASFFNMS TEVASCMDPQ
110 120 130 140 150
YRLILEVVYE ALEAAGIPLE QVSGSKTGVF AGTMYHDYQG SFQRQPEALP
160 170 180 190 200
RYFITGNAGT MLANRVSHFY DLRGPSVSID TACSTTLTAL HLAIQSLRAG
210 220 230 240 250
ESDMAIVAGA NLLLNPDVFT TMSNLGFLSS DGISYSFDSR ADGYGRGEGV
260 270 280 290 300
AAIVLKTLPD AVRDGDPIRL IVRETAINQD GRTPAISTPS GEAQECLIQD
310 320 330 340 350
CYQKAQLDPK QTSYVEAHGT GTRAGDPLEL AVISAAFPGQ QIQVGSVKAN
360 370 380 390 400
IGHTEAVSGL ASLIKVALAV EKGVIPPNAR FLQPSKKLLK DTHIQIPLCS
410 420 430 440 450
QSWIPTDGVR RASINNFGFG GANAHAIVEQ YGPFAETSIC PPNGYSGNYD
460 470 480 490 500
GNLGTDQAHI YVLSAKDENS CMRMVSRLCD YATHARPADD LQLLANIAYT
510 520 530 540 550
LGSRRSNFRW KAVCTAHSLT GLAQNLAGEG MRPSKSADQV RLGWVFTGQG
560 570 580 590 600
AQWFAMGREL IEMYPVFKEA LLECDGYIKE MGSTWSIIEE LSRPETESRV
610 620 630 640 650
DQAEFSLPLS TALQIALVRL LWSWNIQPVA VTSHSSGEAA AAYAIGALTA
660 670 680 690 700
RSAIGISYIR GALTARDRLA SVHKGGMLAV GLSRSEVGIY IRQVPLQSEE
710 720 730 740 750
CLVVGCVNSP SSVTVSGDLS AIAKLEELLH ADRIFARRLK VTQAFHSSHM
760 770 780 790 800
NSMTDAFRAG LTELFGADPS DAANASKDVI YASPRTGARL HDMNRLRDPI
810 820 830 840 850
HWVECMLHPV EFESAFRRMC LDENDHMPKV DRVIEIGPHG ALGGPIKQIM
860 870 880 890 900
QLPELATCDI PYLSCLSRGK SSLSTLRLLA SELIRAGFPV DLNAINFPRG
910 920 930 940 950
CEAARVQVLS DLPPYPWNHE TRYWKEPRIS QSARQRKGPV HDLIGLQEPL
960 970 980 990 1000
NLPLARSWHN VLRVSDLPWL RDHVVGSHIV FPGAGFVCMA VMGISTLCSS
1010 1020 1030 1040 1050
DHESDDISYI LRDVNFAQAL ILPADGEEGI DLRLTICAPD QSLGSQDWQR
1060 1070 1080 1090 1100
FLVHSITADK NDWTEHCTGL VRAEMDQPPS SLSNQQRIDP RPWSRKTAPQ
1110 1120 1130 1140 1150
ELWDSLHRVG IRHGPFFRNI TCIESDGRGS WCTFAIADTA SAMPHAYESQ
1160 1170 1180 1190 1200
HIVHPTTLDS AVQAAYTTLP FAGSRIKSAM VPARVGCMKI SSRLADLEAR
1210 1220 1230 1240 1250
DMLRAQAKMH SQSPSALVTD VAVFDEADPV GGPVMELEGL VFQSLGASLG
1260 1270 1280 1290 1300
TSDRDSTDPG NTCSSWHWAP DISLVNPGWL EKTLGTGIQE HEISLILELR
1310 1320 1330 1340 1350
RCSVHFIQEA MESLSVGDVE RLSGHLAKFY AWMQKQLACA QNGELGPESS
1360 1370 1380 1390 1400
SWTRDSEQAR CSLRSRVVAG STNGEMICRL GSVLPAILRR EVDPLEVMMD
1410 1420 1430 1440 1450
GHLLSRYYVD ALKWSRSNAQ ASELVRLCCH KNPRARILEI GGGTGGCTQL
1460 1470 1480 1490 1500
VVDSLGPNPP VGRYDFTDVS AGFFEAARKR FAGWQNVMDF RKLDIEDDPE
1510 1520 1530 1540 1550
AQGFVCGSYD VVLACQVLHA TSNMQRTLTN VRKLLKPGGK LILVETTRDE
1560 1570 1580 1590 1600
LDLFFTFGLL PGWWLSEEPE RQSTPSLSPT MWRSMLHTTG FNGVEVEARD
1610 1620 1630 1640 1650
CDSHEFYMIS TMMSTAVQAT PMSCSVKLPE VLLVYVDSST PMSWISDLQG
1660 1670 1680 1690 1700
EIRGRNCSVT SLQALRQVPP TEGQICVFLG EVEHSMLGSV TNDDFTLLTS
1710 1720 1730 1740 1750
MLQLAGGTLW VTQGATMKSD DPLKALHLGL LRTMRNESHG KRFVSLDLDP
1760 1770 1780 1790 1800
SRNPWTGDSR DAIVSVLDLI SMSDEKEFDY AERDGVIHVP RAFSDSINGG
1810 1820 1830 1840 1850
EEDGYALEPF QDSQHLLRLD IQTPGLLDSL HFTKRNVDTY EPDKLPDDWV
1860 1870 1880 1890 1900
EIEPRAFGLN FRDIMVAMGQ LESNVMGFEC AGVVTSLSET ARTIAPGLAV
1910 1920 1930 1940 1950
GDRVCALMNG HWASRVTTSR TNVVRIPETL SFPHAASIPL AFTTAYISLY
1960 1970 1980 1990 2000
TVARILPGET VLIHAGAGGV GQAAIILAQL TGAEVFTTAG SETKRNLLID
2010 2020 2030 2040 2050
KFHLDPDHVF SSRDSSFVDG IKTRTRGKGV DVVLNSLAGP LLQKSFDCLA
2060 2070 2080 2090 2100
RFGRFVEIGK KDLEQNSRLD MSTFVRNVSF SSVDILYWQQ AKPAEIFQAM
2110 2120 2130 2140 2150
SEVILLWERT AIGLIHPISE YPMSALEKAF RTMQSGQHVG KIVVTVAPDD
2160 2170 2180 2190 2200
AVLVRQERMP LFLKPNVSYL VAGGLGGIGR RICEWLVDRG ARYLIILSRT
2210 2220 2230 2240 2250
ARVDPVVTSL QERGCTVSVQ ACDVADESQL EAALQQCRAE EMPPIRGVIQ
2260 2270 2280 2290 2300
GAMVLKDALV SQMTADGFHA ALRPKVQGSW NLHRIASDVD FFVMLSSLVG
2310 2320 2330 2340 2350
VMGGAGQANY AAAGAFQDAL AEHRMAHNQP AVTIDLGMVQ SIGYVAETDS
2360 2370 2380 2390 2400
AVAERLQRIG YQPLHEEEVL DVLEQAISPV CSPAAPTRPA VIVTGINTRP
2410 2420 2430 2440 2450
GPHWAHADWM QEARFAGIKY RDPLRDNHGA LSLTPAEDDN LHARLNRAIS
2460 2470 2480 2490 2500
QQESIAVIME AMSCKLISMF GLTDSEMSAT QTLAGIGVDS LVAIELRNWI
2510 2520 2530
TAKFNVDISV FELMEGRTIA KVAEVVLQRY KA
Length:2,532
Mass (Da):276,641
Last modified:November 1, 1999 - 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:iC486622B89D58B2E
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
AF141925 Genomic DNA Translation: AAD34559.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAD34559

<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
AF141925 Genomic DNA Translation: AAD34559.1

3D structure databases

SMRiQ9Y7D5
ModBaseiSearch...

Proteomic databases

PRIDEiQ9Y7D5

Genome annotation databases

KEGGiag:AAD34559

Enzyme and pathway databases

UniPathwayiUPA00875
BioCyciMetaCyc:MONOMER-18789

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
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, 1 hit
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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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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 nameiLOVF_ASPTE
<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: Q9Y7D5
<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: September 3, 2014
Last sequence update: November 1, 1999
Last modified: December 2, 2020
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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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