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Entry version 35 (12 Aug 2020)
Sequence version 1 (16 Apr 2014)
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Protein

Reducing polyketide synthase FUB1

Gene

FUB1

Organism
Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
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

Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).By similarity2 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: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in Mycotoxin 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 sitei230For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei699For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei1026For 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

<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, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-19345

<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:
Reducing polyketide synthase FUB11 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Fusaric acid biosynthesis protein 11 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:FUB11 Publication
ORF Names:FVEG_12523
<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>OrganismiGibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
<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 identifieri334819 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium fujikuroi species complex
<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
  • UP000009096 <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> Componentsi: Chromosome 3, 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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Fusaric acid is phytotoxic to plants such as cotton and banana (PubMed:20955724, PubMed:23922960). It has been shown to induce programmed cell death in plants (PubMed:16868776, PubMed:23838885). In addition to a mild toxicity to animals, fusaric acid exhibits acanthamoebicidal, antioomycete, and antimycobacterial activities (PubMed:17927749, PubMed:22864988, PubMed:21811925).7 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

Impairs the production of fusaric acid (PubMed:22652150).1 Publication

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:3387

<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_00004373081 – 2409Reducing polyketide synthase FUB1Add BLAST2409

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 residuei2365O-(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

Expression is positively regulated by the fusaric acid cluster specific transcription factor FUB10 (PubMed:25372119). Expression is also positively regulated by the secondary metabolism regulator LAE1 (PubMed:22713715).2 Publications

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
117187.FVEG_12523T0

<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
W7MT31

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>Domaini2328 – 2405CarrierPROSITE-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>Regioni60 – 482Ketosynthase (KS) domainSequence analysisAdd BLAST423
Regioni608 – 929Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST322
Regioni995 – 1302Dehydrogenase (DH) domainSequence analysisAdd BLAST308
Regioni1713 – 2025Enoyl reductase (ER) domainSequence analysisAdd BLAST313
Regioni2049 – 2225Ketoreductase (KR) domainSequence analysisAdd BLAST177

<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.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1202, Eukaryota

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, 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
IPR013154, ADH_N
IPR011032, GroES-like_sf
IPR032821, KAsynt_C_assoc
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR020801, PKS_acyl_transferase
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
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08240, ADH_N, 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
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
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.

W7MT31-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTLSNGSNGA NGTSNGHGAH PSANGFHNAA NGGANNGTPN GGAEYNASLP
60 70 80 90 100
QVDGDISSAI AVIGVSGRFP GDATSPRHLW DLLKEGRNAL SDVPESRFNI
110 120 130 140 150
DGFYHPDGGR AGTLNTKQGY FLKSDVDKFD AGFFSITPEE ARGMDPTQRI
160 170 180 190 200
LLELAYEGLE NAGLKIDEVA NQHMSCYIGA CQHDYWDLQA YDMDSAPKYT
210 220 230 240 250
ATGTGPALLS NRISWFFNLK GPSVTIDTAC SSTLTALHLA GQSIRNGESD
260 270 280 290 300
SALVGGLGLH LLPNFGVFMS SMSFLSADNK CHSFDASANG YARAEGGGFV
310 320 330 340 350
VLKRLDKALA DGDTIRAVLR STGSNQDGRT LGITQPSASR QEELIRATYA
360 370 380 390 400
SAGLTFDKTN FFEAHGTGTK VGDPIECSVI GNVFGKTRER PVYVGSVKSN
410 420 430 440 450
IGHLEGASGL AGLVKTIYSL ESGVISPTYG LENVNPKIKL DEWKINLPTE
460 470 480 490 500
KIKWPAGLRR ASINSFGYGG ANAHAVLDDA YHFLKTHNLE GHHNTKAEDV
510 520 530 540 550
PATGLIGNGS QDIIEKTDKK PRLFLISSHE ESGIARLSQT LQAYLADPAA
560 570 580 590 600
RDLPEDQFLH RLAYTLSEKR SSLPWKTYAA ASTIEELQQA LDGAPTKAAR
610 620 630 640 650
VPRSQALTFI FTGQGAQWFA MGRELQKYPI FRQSLHACSQ YLKDFGSTWD
660 670 680 690 700
LVEELNRDAK ESIIDLPYVS QPSCTALQLS IIDLLASWGI HPQVTVGHSS
710 720 730 740 750
GEIAAAYAKG AFDKEAAMRI AYFRGHLTGN ITKTGSMAAV GLGPERVSEY
760 770 780 790 800
LSRVTAGKIV VACINSPASV TLSGDVEGID EVLTFLQADD IFARKLRVTT
810 820 830 840 850
AYHSHHMQQI SEEYLNSLSG KWELKPGNPK VRMFSSVSAK PIDGTELGPA
860 870 880 890 900
YWVANLVSPV NFSGAVTAAA NAGALGKRKA SGKKGSADAM VEIGPHAALQ
910 920 930 940 950
GPLKQILDSI GDKGASPKYF SAIKRKQDAI QTTLEVVGEL LVLGHQVNVP
960 970 980 990 1000
LVNAYTETTS ALVDLPPYAW NTTNSYWHES AAVTAYKQRK HPRLELLGVR
1010 1020 1030 1040 1050
DPRSTKAEPA WHNYLRISEQ PWIEHHQFQN TNIYPMAGMI VMAIEGLRQV
1060 1070 1080 1090 1100
ETRTDVEGYT IRDVNIGSAL VVPLDQTIET RLQLTPWRSG PNVSWSHWTE
1110 1120 1130 1140 1150
FTVSSRNESG SWTTNCTGLV STSYKRETNS TFLDEEAAAN ALLSQEYKAI
1160 1170 1180 1190 1200
SNSDLPSVDP TVFYTKLDES GFSLGPAFRG VKELNLFDHK AHFSMEVIDT
1210 1220 1230 1240 1250
KDFYPKKWEP AHLIHPAVLD VFVHLLISST GDAAEIKARV PVSTASLYIS
1260 1270 1280 1290 1300
ADFDSTSGTK YHGFSTSKKH GATNMLSNVI AFAEGGSKPL IALEGCKTVP
1310 1320 1330 1340 1350
LRGASDPSSG DGQSLGHVPV VPKKVVDVDI SDAVTLEKLL QGTDFASKLG
1360 1370 1380 1390 1400
SYLSLLGQKR PGLSVLEYSS STSSILLRAL TAQAEELQGS ITSVALTTPL
1410 1420 1430 1440 1450
DGPADEETSV PEAWKNKVQQ EKLDLTQDPS TQGFEDVALD VIFIDVEEQG
1460 1470 1480 1490 1500
DISLVLKNAK KILKPSGILL ITNHASAIST DLLTSTDLTS TTVSELIIAR
1510 1520 1530 1540 1550
HKPDTDPSDH QVLIVTPPSP SSGLSKLIAQ AENDLTSQGY EVNKADFANI
1560 1570 1580 1590 1600
PEQTTPFLTL SALDVDTPFL ESFHHETFTK LRSLFLASRG TLWLTLDTAS
1610 1620 1630 1640 1650
RGLVNGLGRT IRAEHPDISF TVLSLDALTS LDSALNTKTI SSIIENMSRK
1660 1670 1680 1690 1700
TFGETSDSEY VIRNNQVLVE RLIPNPDLKA LLDSSKTGNN LSAVKVPLKQ
1710 1720 1730 1740 1750
VNKPLQLSIR DPGLLDTLEY LSVPDLFEPL GDNQIEIEVG SVGLNFRDVM
1760 1770 1780 1790 1800
VAMGQMEDNT LGIECAGVVA KVGAGVQKFK VGDRVFGMHA GCFQTRVRVD
1810 1820 1830 1840 1850
PRTFQRTPEH LGDEEAASLM CTSATVVHSL IDVARLQRGE SVLIHSAAGG
1860 1870 1880 1890 1900
VGQAAIRLAK YLGAEIFATV SSEKKKRLLI EDYGVKESHI FNSRDYSFAD
1910 1920 1930 1940 1950
GILRLTNQRG VDVVINSLAG EALRRTWLCV APFGRFIELG KRDIYDNSGL
1960 1970 1980 1990 2000
DMRPFLDNIT FSGLDILTQV ISYPDRFEAI GNQVVELLSK NAISPLNNLA
2010 2020 2030 2040 2050
RYSFGEVSKA FRLMQSGGHV GKIVLYPRPD DIVPIVPEGL ESFCLPHDAT
2060 2070 2080 2090 2100
YVLIGGLGGI GRSVTRLLVE RGARHLVFLS RSAAARPEAQ ALLDELHAQG
2110 2120 2130 2140 2150
VQAKAFAVDV AEKSQLEPVI NDVKQSFPAI KGLIHCAMDL RDAVYSNMTA
2160 2170 2180 2190 2200
DDWNASLRPK LLATRNLHDL LPTDLDFFIC LSSIAGIIGS RGQANYNAGN
2210 2220 2230 2240 2250
TYQDALAHHR AASGLAATSI NLSLVVGIGV STERSEVFQL LKDGGLLGMD
2260 2270 2280 2290 2300
ENDVLNVIKA AISGCAPTQV ALGASTGGQL DKLAANDPYW FADSRFAVLN
2310 2320 2330 2340 2350
QLDRQGTGAV AGGQDWKKLL AAAASPDEVY EIVLQQLLEG VSKIIKADVE
2360 2370 2380 2390 2400
DMDSRKSLPA LGIDSLVAIE IRTWLLKEFQ ADLSVFDIVS NDPLTGFAKK

VMAKSVLIA
Length:2,409
Mass (Da):260,134
Last modified:April 16, 2014 - 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:i2183CC2D58BCF720
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DS022261 Genomic DNA Translation: EWG54266.1

NCBI Reference Sequences

More...
RefSeqi
XP_018760457.1, XM_018901864.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
30069957

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
fvr:FVEG_12523

<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
DS022261 Genomic DNA Translation: EWG54266.1
RefSeqiXP_018760457.1, XM_018901864.1

3D structure databases

SMRiW7MT31
ModBaseiSearch...

Protein-protein interaction databases

STRINGi117187.FVEG_12523T0

Genome annotation databases

GeneIDi30069957
KEGGifvr:FVEG_12523

Phylogenomic databases

eggNOGiKOG1202, Eukaryota
OrthoDBi19161at2759

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19345

Miscellaneous databases

PHI-baseiPHI:3387

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
IPR013154, ADH_N
IPR011032, GroES-like_sf
IPR032821, KAsynt_C_assoc
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR020801, PKS_acyl_transferase
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
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF08240, ADH_N, 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
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
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 nameiFUB1_GIBM7
<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: W7MT31
<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: October 5, 2016
Last sequence update: April 16, 2014
Last modified: August 12, 2020
This is version 35 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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