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Entry version 11 (11 Dec 2019)
Sequence version 1 (07 Sep 2016)
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Protein

O-methyltransferase lcsG

Gene

lcsG

Organism
Purpureocillium lilacinum (Paecilomyces lilacinus)
Status
Reviewed-Annotation score:

Annotation score:3 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

O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic (PubMed:27416025). Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC, have been identified in the cluster and it is not clear which is the one that assembles 4-methylhex-2-enoic acid since both contain KS, AT, DH, cMT, ER, KR and ACP domains (Probable). The polyketide residue might be transferred to the NRPS lcsA, mediated by two additional enzymes, the acyl-CoA ligase lcsD and the thioesterase lcsE. The linear polyketide carboxylic acid, which is released from PKS, is converted to a CoA thioester by lcsD, and then lcsE hydrolyzes the thiol bond and shuttles the polyketide intermediate to lcsA (Probable). The C domain of the first module catalyzed the condensation of 4-methylhex-2-enoic acid and MePro carried by domain A1, followed by successive condensations of nine amino acids to trigger the elongation of the linear peptide. A5 and A6 domains of lcsA are proposed to incorporate leucine, A2 AHyMeOA, and A3 incorporates HyLeu. A4, A7 and A8 incorporate AIB (Probable). The AHyMeOA in leucinostatin A activated by the A2 might be produced by the second PKS (lcsB or lcsC) present within the cluster (Probable). The MePro is probably produced via leucine cyclization and may originate from a separate pathway, independent of the cluster. Another nonproteinogenic amino acid, beta-Ala, could be produced by an aspartic acid decarboxylase also localized outside of the cluster. Two candidates are VFPBJ_01400 and VFPBJ_10476 (Probable). The final peptide scaffold may be released by the NAD(P)H-dependent thioester reductase (TE) at the C-terminal region of lcsA (Probable). Transamination of the lcsA product by the transaminase lcsP may produce DPD at the C-terminus (Probable). Further hydroxylation steps performed alternatively by the cytochrome P450 monooxygenases lcsI, lcsK and lcsN then yield the non-methylated leucinostatins precursor. It is also possible that leucines can be hydroxylated prior to their incorporation into the peptide (Probable). Varying extents of methylation then lead to the formation of leucinostatins A and B (Probable).1 Publication1 Publication

<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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei321S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei363S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

<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:
O-methyltransferase lcsG1 Publication (EC:2.1.1.-PROSITE-ProRule annotation)
Alternative name(s):
Leucinostatins biosynthesis cluster protein G1 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:lcsG1 Publication
ORF Names:VFPBJ_02521
<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>OrganismiPurpureocillium lilacinum (Paecilomyces lilacinus)
<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 identifieri33203 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesOphiocordycipitaceaePurpureocillium
<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
  • UP000078240 <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

<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_00004466081 – 468O-methyltransferase lcsGAdd BLAST468

<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 leucinostatins biosynthesis cluster-specific transcription regulator lcsF.1 Publication

<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

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>Regioni298 – 299S-adenosyl-L-methionine bindingBy similarity2
Regioni348 – 349S-adenosyl-L-methionine bindingBy similarity2

<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

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016461 O-MeTrfase_COMT
IPR001077 O_MeTrfase_dom
IPR029063 SAM-dependent_MTases

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00891 Methyltransf_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51683 SAM_OMT_II, 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.

A0A179H2P2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDNVQSDTT AAQAGITDAP TAPTSAPVSL KERLEKLIES SQQLIKRMDE
60 70 80 90 100
NNIPDPTFAP ECQEDYSKLP PETITERFAL LDLLNDVTFL VHGASQSITD
110 120 130 140 150
VAQNAMADSA TLNILNYFNF WDVIPLDGDA SFAEIAKAVR LPQEAVEAIL
160 170 180 190 200
PYAFSNRIFE PVTIGDPNSR IRHTSRSAAM IKDPTLRIIV NLTIDGLAGP
210 220 230 240 250
LSILNRALEK NFLGKEKLTN EISETPFGML YNKGGPLGEY KDYYDWLDRD
260 270 280 290 300
GEGERKGWRQ RDMVESLRLA KEKMGAESAL LEALDWAGAG KATVVDLGGS
310 320 330 340 350
GGHDDVPLAE KFPDLKIIVQ DLPSCQPKFD DGYISDELKK RVSFLAHDFF
360 370 380 390 400
TPQPVQADIY LFKWVFYDWS NKDIVKIIKA LVPALRPGAR VLVLDLMVDV
410 420 430 440 450
GPEAAAVMPR SLLKYSNVIS LKTLSLFGHT KQATKKMTDL FKAADDRFEI
460
VRDEVAGTFM TFEAVWRG
Length:468
Mass (Da):51,937
Last modified:September 7, 2016 - 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:i3F4D04C0D59240F5
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
LSBH01000002 Genomic DNA Translation: OAQ83753.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
OAQ83753; OAQ83753; VFPBJ_02521

<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
LSBH01000002 Genomic DNA Translation: OAQ83753.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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

Genome annotation databases

EnsemblFungiiOAQ83753; OAQ83753; VFPBJ_02521

Family and domain databases

InterProiView protein in InterPro
IPR016461 O-MeTrfase_COMT
IPR001077 O_MeTrfase_dom
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF00891 Methyltransf_2, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51683 SAM_OMT_II, 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 nameiLCSG_PURLI
<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: A0A179H2P2
<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 10, 2019
Last sequence update: September 7, 2016
Last modified: December 11, 2019
This is version 11 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
  2. SIMILARITY comments
    Index of protein domains and families
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