Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 32 (22 Apr 2020)
Sequence version 1 (04 Mar 2015)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Polyketide synthase 1

Gene

Pks1

Organism
Metarhizium majus (strain ARSEF 297)
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 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

Polyketide synthase; part of the Pks1 gene cluster that mediates the biosynthesis of an anthraquinone derivative pigment that contributes to conidial pigmentation that provides protection from UV radiation, heat and cold stress (PubMed:29958281). The polyketide synthase Pks1 produces 1-acetyl-2,4,6,8-tetrahydroxy-9,10-anthraquinone though condensation of acetyl-CoA with malonyl-CoA (By similarity). The dehydratase EthD and the laccase Mlac1 further convert the anthraquinone derivative into the final conidial pigment (By similarity).By similarity1 Publication

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 sitei566For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei1018For acyl/malonyl transferase activityPROSITE-ProRule annotation1
Active sitei1973For thioesterase activityBy 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 functionMultifunctional enzyme, Transferase

<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:
Polyketide synthase 11 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Conidial pigment biosynthesis polyketide synthase1 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:Pks11 Publication
ORF Names:MAJ_09462
<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>OrganismiMetarhizium majus (strain ARSEF 297)
<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 identifieri1276143 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesClavicipitaceaeMetarhiziumMetarhizium majus
<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
  • UP000031176 <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 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

Results in red conidia.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_00004457451 – 2149Polyketide synthase 1Add BLAST2149

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 residuei1712O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei1830O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Highly expressed during conidiation (PubMed:29958281). A conserved conidiation regulatory pathway containing BrlA, AbaA and WetA regulates expression. During conidiation BlrA up-regulates AbaA, which in turn controls WetA. Moreover, the Hog1 MAPK regulates fungal conidiation by controlling the conidiation regulatory pathway, and that all three pigmentation genes Pks1, EthD and Mlac1 exercise feedback regulation of conidiation (By similarity).By similarity1 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
A0A0B4H4F0

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>Domaini1678 – 1752Carrier 1PROSITE-ProRule annotation1 PublicationAdd BLAST75
Domaini1793 – 1870Carrier 2PROSITE-ProRule annotation1 PublicationAdd 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>Regioni19 – 261N-terminal acylcarrier protein transacylase domain (SAT)Sequence analysis1 PublicationAdd BLAST243
Regioni397 – 832Ketosynthase (KS) domainSequence analysis1 PublicationAdd BLAST436
Regioni929 – 1233Malonyl-CoA:ACP transacylase (MAT) domainSequence analysis1 PublicationAdd BLAST305
Regioni1310 – 1624Product template (PT) domainSequence analysis1 PublicationAdd BLAST315
Regioni1882 – 2147Thioesterase (TE) domainSequence analysis1 PublicationAdd BLAST266

<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 starter unit:ACP transacylase (SAT) that selects the starter unit; 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 product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.1 Publication
The release of the polyketide chain from the non-reducing polyketide synthase is mediated by the thioesterase (TE) domain localized at the C-ter of the protein.1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000022_6_0_1

Database of Orthologous Groups

More...
OrthoDBi
68112at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 2 hits
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR020801, PKS_acyl_transferase
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR030918, PT_fungal_PKS
IPR032088, SAT
IPR001031, Thioesterase
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF00550, PP-binding, 2 hits
PF14765, PS-DH, 1 hit
PF16073, SAT, 1 hit
PF00975, Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 2 hits
SSF52151, SSF52151, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04532, PT_fungal_PKS, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 2 hits
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.

A0A0B4H4F0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNHVTIKQSD TRADPFRVFI FGDQSSCNLS NLQLLLFKKS NVYLASFIDQ
60 70 80 90 100
VNLTLRHEIA RLTAAERQSF PAFSSIQNLV ARALKKDTSV ALESTLATIY
110 120 130 140 150
HLCCFLNYFG DGQEAYPTGP TTHVSGLCIG ALAAAAVSSS KSLAELVQAG
160 170 180 190 200
IDAVRVSLKV GLLVARTAAL FSHQESNGTS SSPWSYAVPD SQLPLALAEE
210 220 230 240 250
AIESYQAKTN IPPLSLPYIS AKGQNSWTVS GPPAIVQHFL ETSQFEKTLR
260 270 280 290 300
LTRLAVHAPY HAPHIFSAID VQHIIRAVGP VSSFSSKLSF ISSSSSRNLP
310 320 330 340 350
TGLNFQDLLC RAVEDILILP LDLREAAENI RLVLEATDNV QQCALFPIST
360 370 380 390 400
GVCPSLKQSF SPATASRVSI VDCIMERATA DAGPKSTSGP KPSESKIAII
410 420 430 440 450
GMSGRFPESA DVEAFWDLLH QGLDVHRPVP PDRYNGELYY DVTGKRKNTC
460 470 480 490 500
KVMHGCWINE PGLFDAKFFN ISPKEAEQSD PGQRLALATA YEALEAAGVV
510 520 530 540 550
ADRTPSTQRD RVGVFYGMTS DDYREVSCGQ NVDTYFIPGG NRAFTPGKIN
560 570 580 590 600
YFFKYCGPSV SVDTACSSSL AAIHLACNSI WRNECDTAIA GGTNVMSNPD
610 620 630 640 650
SFVGLDRGYF LSRTGNCHTF DDEADGYCRA DAVGTVILKR LEDAIADHDP
660 670 680 690 700
ILGVISGALT NHSADAVSIT RPHSGAQEEI FSKLLTESGV HPHQVSYIEM
710 720 730 740 750
HGTGTQAGDA TEMTSVLNCF APSTSPRRLP HESLHLGSTK ANVGHSESAS
760 770 780 790 800
GVSALIKVLL MMEKNIIPPH CGIKGKINHK FPTDLDQRNV HIARTATQWN
810 820 830 840 850
RRNEFNNIRR AFVNNFSAAG GNTALLVEDY PLLIADSSQQ DARTAHVVTV
860 870 880 890 900
SAKCIKSLKG NLENLKKFVQ KQASTQGFLP KLSYTTTARR MHHPFRVAIP
910 920 930 940 950
AANSEQLLSA LDEELKHDGY TCSSESPVAF VFSGQGSQYS AMGQHLLHFT
960 970 980 990 1000
IFRDEVHAYD ILARRHGFPS IMPLIDGSVD IEDLEPLVVQ LGTVCVQMAL
1010 1020 1030 1040 1050
ASLWMALGMR PAYVVGHSLG HYAALKVAGV LTASDTIYLV AMRARLLQNK
1060 1070 1080 1090 1100
CSRGSHAMLA IRSSADEIQA HLDEGIHDIA CISGPQDTVV SGCIDDIDRL
1110 1120 1130 1140 1150
SQKLTDKGIK ATRVNVPFAF HSAQVDPILD ELEATASQVE FHAPRVAIGC
1160 1170 1180 1190 1200
PLLGKTFKAG ETPSLEANHI RRHCRETVNF LDVLRSAKDD GFVSEKTAWI
1210 1220 1230 1240 1250
EIGPHTVCSK LVKANISQDI VAVPSLMRNK DGWQVLASSV AALYRHGSSV
1260 1270 1280 1290 1300
AWDEYHHDFE ACKQVLRLPA YSWDNKVYWI DYVHDWLLTR GDPPVQAAAS
1310 1320 1330 1340 1350
LPAPPSSFST ASVHRIVHES VDKGKLTLTA ECEFTNEQLR EVVYGHVVNG
1360 1370 1380 1390 1400
NRVCSSSLYT DFGVTLGSYI LEKYRPDLQD HAVDVQDMVV NKALVHKEGP
1410 1420 1430 1440 1450
TMLLRIDVVL DMTDSKAASM SIYSVNSKGN KTAEHAQSSL HFERPKVWLK
1460 1470 1480 1490 1500
SWDSTQYYVE RSIEWLKEKA DQGLNSRMSS GVIYKLFSSL VDYSTAYKGM
1510 1520 1530 1540 1550
QEAIVNTEDF EATALVRFQV DEGNFRCNPM WVDSCGQLAG FLMNGHAKTP
1560 1570 1580 1590 1600
KDQVFINHGW QSFRTVRKFS KDKTYRTYVR MRCIEGTTYA GDVYIFDDEG
1610 1620 1630 1640 1650
IVGVCGSITF QGIPRKVLNT AMPPPKSQNE APVRSAPAKP AAKPPKSASS
1660 1670 1680 1690 1700
EHSGHFARHS NIEPLKLDAA LKSATTARNP MLAVFKIVSE EIGIPSASVD
1710 1720 1730 1740 1750
NGLVFADYGV DSLLSLSISG RLREELDLDV ESSAFETCAT LADLATHLGL
1760 1770 1780 1790 1800
DTFSSDQSSG QSSSSGGLSP RSDSIGEITS SATTPPSLSP RGSVSGSQCK
1810 1820 1830 1840 1850
DVCAILAEEI GVSMSEITND TDLGALGMDS LMSLAVLSRL REELELDLEG
1860 1870 1880 1890 1900
DFFVSHPNFS SFKHMFQQGH GDEVESEPSA ELKQYRATST LLQGNPKSAL
1910 1920 1930 1940 1950
YTLFLLPDGS GSSFSYAPIN AVRKDVCVFG LNCPWLKSAE KLVQFGLKGL
1960 1970 1980 1990 2000
ATLYVEEIRR RAPHGPYNLG GWSAGGICAY EAAIQFTREG ETVERLILLD
2010 2020 2030 2040 2050
SPNPIGLEKL PARLFDFVNG LGLFGDGKAP DWLLAHFLAF IDALDEWKPV
2060 2070 2080 2090 2100
PWDKALGGGN SPPPRTYILW AEDGICKDTD ARPEYRDDDP REMKWLLENR
2110 2120 2130 2140
TNFGGNNWDV LLGQQSLAIE RIQDANHFTM LRKGKNSERV AAFIRSTFG
Length:2,149
Mass (Da):234,890
Last modified:March 4, 2015 - 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:i1AB182F334661140
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
AZNE01000110 Genomic DNA Translation: KID94570.1

NCBI Reference Sequences

More...
RefSeqi
XP_014573564.1, XM_014718078.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
KID94570; KID94570; MAJ_09462

<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
AZNE01000110 Genomic DNA Translation: KID94570.1
RefSeqiXP_014573564.1, XM_014718078.1

3D structure databases

SMRiA0A0B4H4F0
ModBaseiSearch...

Genome annotation databases

EnsemblFungiiKID94570; KID94570; MAJ_09462

Phylogenomic databases

HOGENOMiCLU_000022_6_0_1
OrthoDBi68112at2759

Family and domain databases

Gene3Di1.10.1200.10, 2 hits
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR020801, PKS_acyl_transferase
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR030918, PT_fungal_PKS
IPR032088, SAT
IPR001031, Thioesterase
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF00550, PP-binding, 2 hits
PF14765, PS-DH, 1 hit
PF16073, SAT, 1 hit
PF00975, Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 2 hits
SUPFAMiSSF47336, SSF47336, 2 hits
SSF52151, SSF52151, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
TIGRFAMsiTIGR04532, PT_fungal_PKS, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 2 hits
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 nameiPKS1_METMF
<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: A0A0B4H4F0
<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: December 5, 2018
Last sequence update: March 4, 2015
Last modified: April 22, 2020
This is version 32 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again