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Entry version 29 (02 Dec 2020)
Sequence version 2 (05 Oct 2016)
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Protein

Reducing polyketide synthase FUB1

Gene

FUB1

Organism
Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)
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: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 similarity1 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: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.1 Publication
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

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, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-19346

<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:FOXG_15248
<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>OrganismiFusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935 / NRRL 34936) (Fusarium vascular wilt of tomato)
<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 identifieri426428 [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 oxysporum 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
  • UP000009097 <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: Unplaced

<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

Reduces to 5% the production of fusaric acid (PubMed:25372119).1 Publication

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:6936

<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_00004373091 – 2410Reducing polyketide synthase FUB1Add BLAST2410

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 residuei2366O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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
A0A0D2YG10

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>Domaini2329 – 2406CarrierPROSITE-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
Regioni1714 – 2026Enoyl reductase (ER) domainSequence analysisAdd BLAST313
Regioni2050 – 2226Ketoreductase (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

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
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
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
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
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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

A0A0D2YG10-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTLFNGSNGA NGTSSGHGAH PSANGFHNAA NGGANNGTAN GGVEHDASLP
60 70 80 90 100
QVDGDISSAI AVIGVSGRFP GDGTSPRHLW DLLKEGRNAL SDVPESRFNI
110 120 130 140 150
DGFYHPDGGR AGTLNTKQGY FLQSDVDKFD 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
VLKRLDKALS DGDTIRAVLR STGSNQDGRT LGITQPSASR QEELIRATYA
360 370 380 390 400
SAGLSFDKTN FFEAHGTGTK VGDPIECSVI GNVFGKTREK PVYVGSVKSN
410 420 430 440 450
IGHLEGASGL AGLVKTIYSL ESGVISPTYG LENVNPKIKL DEWKINIPTE
460 470 480 490 500
EIKWPAGLRR ASINSFGYGG ANAHAVLDDA YHFLKTHNLK GHHNTKVEGV
510 520 530 540 550
LTTGLIGNGS QDASDKTDKK SRLFLLSSHE ESGIARLSQT LQAYLTEPAA
560 570 580 590 600
RELPEDQFLH RLAYTLSEKR SSLPWKTYAA ASTIEELQQA LDGAPTKAAR
610 620 630 640 650
VPRPQALTFI FTGQGAQWFA MGRELQKYPV FQQSLHACSQ YLKDFGSTWD
660 670 680 690 700
LVEELNRDAK ESIIDLPYVS QPSCTALQLS IIDLLASWGI HPQVTIGHSS
710 720 730 740 750
GEIAAAYAKG AFDKEAAMRI AYFRGHLTGN ITKTGSMAAV GLGPERVSEY
760 770 780 790 800
LSRVTAGKIV IACINSPASV 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 LVLGHPVNVP
960 970 980 990 1000
LANAYTETTS ALVDLPPYAW NTTNSYWHES AAVTAYKQRK HPRLELLGVR
1010 1020 1030 1040 1050
DPRSTKAEPA WHNYLRISEQ PWIEHHQFQN TNIYPMAGMI VMAIEGLRQV
1060 1070 1080 1090 1100
ETRTDVEGYT IRDVNIGSAL VVPLDQTVET RLQLTPWRSG PNVSWSHWTE
1110 1120 1130 1140 1150
FTVSSRNESG SWTTNCTGLV STSYKHETNS TFLDEEAAAN ALLNQEYKDI
1160 1170 1180 1190 1200
SQSDLPSVDP TVFYTKLDES GFSLGPAFRG VKQLNLFDHK AHFSMEVIDT
1210 1220 1230 1240 1250
KEFYPKKWEP AHLIHPAVLD VFVHLLISST GDAAEIKARV PVSTASLYIS
1260 1270 1280 1290 1300
ADFDSTSGTK YHGFSTSKKH GATNMLSDVI AFAENGTKPL IALKGCKTVP
1310 1320 1330 1340 1350
LRGASDSSSG DGQSLGHVPV VPKKVVDIEI SDAVTLEQLL RGTDLASKLG
1360 1370 1380 1390 1400
SYLSLLGQKL PGLNVLEYSS STSSTLLKAL TAQAEELQGS IASVTLTTPL
1410 1420 1430 1440 1450
DGPVDVEASV PEAWKNKIQQ EKLDLAQDPS SQGYEDATLD VIFLDVEEQQ
1460 1470 1480 1490 1500
GDISLILKNA KKILKPSGIL LIANHAAAIS TDLFSSSSFI STSVSDLIIA
1510 1520 1530 1540 1550
RHKPETEPSV RRVLIVTPSS PSSGLSQLVA QAESDLTSQG YEVAKTDFAN
1560 1570 1580 1590 1600
IPEQTTPFLT LSTLDIDTPF LENFDHETFT KLRSLFLASR GTLWLTLDTA
1610 1620 1630 1640 1650
SRGLVNGLGR TIRAEHPDIS FTTLGLDAST SLDSALNTKT ISTIVENISR
1660 1670 1680 1690 1700
KIFGETSDSE YVIRNNQVLV ERLIPNPDLK ALLDSSKTGN NLSAVKMPLK
1710 1720 1730 1740 1750
QVIKPLQLSI RDPGLLDTLE YLSVPDLSGP LGDNQIEIEV GSVGLNFRDV
1760 1770 1780 1790 1800
MVAMGQMEDN TLGIECAGVV SKVGAGVQKF KVGDRVFGMH AGCFQTRVRV
1810 1820 1830 1840 1850
DPRTFQRTPD HLGDEEAASL MCTSATVVHS LIDVARLQRG ESVLIHSAAG
1860 1870 1880 1890 1900
GVGQTAIRLA KYLGAEIFAT VSSEKKKRLL IEEYGIKESH IFNSRDYSFA
1910 1920 1930 1940 1950
DGVLRLTNQR GVDVVINSLA GEALRRTWLC VAPFGRFIEL GKRDIYDNSG
1960 1970 1980 1990 2000
LDMRPFLDNI TFSGLDILTQ VISYPDRFEA IGSQVVELLS KNAISPLNNL
2010 2020 2030 2040 2050
ARYSFGEVSK AFRLMQSGGH VGKIVLYPRP DDIVPVVPEG LESFCLPHDA
2060 2070 2080 2090 2100
TYVLIGGLGG IGRSVTRLLV ERGARHLIFL SRSAASRPEA QALLDELHAQ
2110 2120 2130 2140 2150
GVQAKAFAVD VAEKSQLEPV INGVKQSFPA IKGLIHCAMD LRDAVYSNMT
2160 2170 2180 2190 2200
ADDWNASLRP KLLATRNLHE LLPTDLDFFI CLSSIAGIIG SRGQANYNAG
2210 2220 2230 2240 2250
NTYQDALAHH RAASGLAATS INLSLVVGIG VSTERSEVFQ LLKDGGLLGM
2260 2270 2280 2290 2300
DENDVLNVIK AAISGRTPTQ VALGASTGGQ LDKLAANDPY WFADSRFAVL
2310 2320 2330 2340 2350
NQLDRQGTGA TAGGQDWKKL LAAAASPDEV YEIVLQQLLE GVSKIIKADV
2360 2370 2380 2390 2400
EDMDSRKSLP ALGIDSLVAI EIRTWLLKEF QADLSVFDIV SNDPLTGFAK
2410
KVMAKSALIA
Length:2,410
Mass (Da):260,094
Last modified:October 5, 2016 - v2
<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:i005B257306E4B43D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1D6QVK6A0A1D6QVK6_FUSO4
Carrier domain-containing protein
2,376Annotation score:

Annotation score:2 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>

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
DS231721 Genomic DNA Translation: KNB17122.1

NCBI Reference Sequences

More...
RefSeqi
XP_018255167.1, XM_018395332.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
KNB17122; KNB17122; FOXG_15248

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
28956322

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
fox:FOXG_15248

<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
DS231721 Genomic DNA Translation: KNB17122.1
RefSeqiXP_018255167.1, XM_018395332.1

3D structure databases

SMRiA0A0D2YG10
ModBaseiSearch...

Genome annotation databases

EnsemblFungiiKNB17122; KNB17122; FOXG_15248
GeneIDi28956322
KEGGifox:FOXG_15248

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19346

Miscellaneous databases

PHI-baseiPHI:6936

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
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
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
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
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 nameiFUB1_FUSO4
<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: A0A0D2YG10
Secondary accession number(s): A0A0J9WU41
<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: October 5, 2016
Last modified: December 2, 2020
This is version 29 of the entry and version 2 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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