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Entry version 9 (02 Dec 2020)
Sequence version 1 (08 May 2019)
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Protein

Highly reducing polyketide synthase VdtX

Gene

VdtX

Organism
Byssochlamys spectabilis (Paecilomyces variotii)
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>
-Protein inferred from homologyi <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

Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity (PubMed:31304040).

The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin (PubMed:31304040).

The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis (PubMed:31304040).

The short-chain dehydrogenase/reductase VdtF is involved in the reduction of the C3-C4 double bond (PubMed:31304040).

The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin (PubMed:31304040).

Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling (PubMed:31304040).

The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet (PubMed:31304040).

1 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 sitei170PROSITE-ProRule annotation1

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

GO - Biological processi

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

Molecular functionAcyltransferase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP

<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:
Highly reducing polyketide synthase VdtX1 Publication (EC:2.3.1.-1 Publication)
Short name:
HR-PKS VdtX1 Publication
Alternative name(s):
Viriditoxin biosynthesis cluster protein X1 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:VdtX1 Publication
ORF Names:C8Q69DRAFT_515060
<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>OrganismiByssochlamys spectabilis (Paecilomyces variotii)
<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 identifieri264951 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesThermoascaceaeByssochlamys
<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
  • UP000283841 <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

Does not affect the production of viriditoxin.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_00004483421 – 2193Highly reducing polyketide synthase VdtXAdd BLAST2193

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 residuei2143O-(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
A0A443HK66

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>Domaini2102 – 2183CarrierPROSITE-ProRule annotationAdd BLAST82

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>Regioni1 – 420Ketosynthase (KS) domainSequence analysisAdd BLAST420
Regioni513 – 809Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST297
Regioni877 – 1128Dehydrogenase (DH) domainSequence analysisAdd BLAST252
Regioni1256 – 1390Methyltransferase (CMet) domainSequence analysisAdd BLAST135
Regioni1575 – 1783Enoyl reductase (ER) domainSequence analysisAdd BLAST209
Regioni1807 – 1981Ketoreductase (KR) domainSequence analysisAdd BLAST175

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Multidomain protein; including a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a methyltransferase (CMeT) domain responsible for the incorporation of methyl groups; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.1 Publication

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
3.40.47.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH_C
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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.

A0A443HK66-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAICGIAVRL PGGISNDAQL WDFLLAKRDA RSQVPGSRYN ISGYHSDSGK
60 70 80 90 100
HGTSKSKYGY FLDESVDLGT LDTSFFSFTK LELEYIDPCQ RQLLEVVREC
110 120 130 140 150
FESAGEVNYR GKDIGCFVGS FGDDWTENLT HDEQTSAKYP LMVGGDFATP
160 170 180 190 200
NRVSYEYNLH GPSVSIRTAC SSSLVALHSA CLSIQNGDCS AAIVAGFNLI
210 220 230 240 250
LTPTMTMIMS SKGVLSADGS SKSFDADADG YGRGEAVNAV YIKPLHDAIR
260 270 280 290 300
DGNPIRAVIR GTATNSDGKS AGFTVPSADA QEDVIRKAYK AAGISDLSQT
310 320 330 340 350
AFVECHGTGT TVGDPIEVAA IANTFGGDMY IGSVKPNVGH SEGASGLTSL
360 370 380 390 400
IKAVLAVENR TIPPNIKFNT PNPKIPFEAK KITVPVEATP WPWNRCVRAS
410 420 430 440 450
VNSFGMGGVN AHVIIESADN FTPPTSEVIE EHDSTPQLLL FSANTQDSLE
460 470 480 490 500
AMIQRNLAYL RENTDSLRDL VYTMGARREH LSFRAASIVH SDMSVTTASF
510 520 530 540 550
GKAPSSPPDI VMVFAGQGAQ WPGMGVELFK SNATFRRSIL EMDSVLQSLP
560 570 580 590 600
DAPAWSIADE ISKEHQTSML YLSSYSQPIC TALQVALVNT LFELNIRPYA
610 620 630 640 650
VIGHSSGELA AAYAAGRLTA SQAVTLAYYR GIVAGKVAQA GYYPFLRPGV
660 670 680 690 700
VVACENSPSS VTISGDIDQV QYVMQEISLA HPEILCRQIK SDTAYHSHHM
710 720 730 740 750
KSVGDTYHSF INPFFRGETE VNCQPVHFFS TVTGDELSDG DHVGPKYWQQ
760 770 780 790 800
NLESRVLFQG ALENIISRQR SRHLLFLDVS PHSTLAGPIR QTLEQAEVAH
810 820 830 840 850
PYVPCLIRFK NCAESFLSTI GQLYSHRQPL DFNMLTNPDR TAKVLTDVPT
860 870 880 890 900
YPWQHGYSNL YTTRQNNEWL FRKQPKHELL GTRVVDSTDN EPCWRNVLYL
910 920 930 940 950
EHVTWLRDHK VSGNIVFPAA GYVMMAGEAV RQIGSTASGF IVRQMVLDTA
960 970 980 990 1000
MVLNQSNPTE IVTSLRKHRR DRWYSFTISS HNGVKWIEHC YGEVAQENLS
1010 1020 1030 1040 1050
RDINVSNWYK TLSRGGVEFG PAFQCVESQS CSVTSNTVSG RIVSKLDSVL
1060 1070 1080 1090 1100
HIVYGAIYKG FDWQVESLPV PTSIGEIMIG ECVSDLDVTM WADVSRNSNI
1110 1120 1130 1140 1150
LVNGEAFGSD GCLLIRIKDI VLRPLGANQA CFEEDESHAG ARLLWKPSMQ
1160 1170 1180 1190 1200
FLNLADLIQT PVNWTKQTML LNDFTSLCIE RALCLLHAQG DWLQRQPKPS
1210 1220 1230 1240 1250
SEQSMESLVE KILATSAAPC ARAMIKVLDN IVPICKGEID ALEVLMGDDT
1260 1270 1280 1290 1300
LYELYNYLNE PQQRILEIGA GTGGTTAKIL PRTKYSTYTF TDISAAFFPA
1310 1320 1330 1340 1350
AKDRFQCHAN VVYRTLDITK DPLDQANVLH ATPNLYETLS NLLLEELCGD
1360 1370 1380 1390 1400
AKFTNFIVGV LPGWWAGESD GRADEPYISP DRWDSILKAA APPLHSLAFM
1410 1420 1430 1440 1450
LASPSCVPES PLKRNVTLLS DVTSSEIAVR MQKQLLSRGY SVGVQSLDQS
1460 1470 1480 1490 1500
LMDGEDVIIL VDTVSPFFHN LDSRKLSTFQ NLLRELQRSH SGALWVTRSI
1510 1520 1530 1540 1550
QIDCRDPRYS PTLGVARTVR SEFGLDFGTC EVDTLKYTSI GLVIDVFEAF
1560 1570 1580 1590 1600
HGRRHGQNAY PEYEYAIRED TADAGQQVQL LGDDEVELQV DTAGVNFLTV
1610 1620 1630 1640 1650
LINSASDGVG LAAIQISKMI GATIYATVIG EDKVEYLTAS HGIPRDHIFN
1660 1670 1680 1690 1700
SRDSSFLDGI MRVTNGRGVD LVLTSLSADF IQASCDCVAN FGKLVNLSKP
1710 1720 1730 1740 1750
TAANQGQFPI DSFHPNMSYA SVDIIDYIKR RPKESKRLLE EIVELYKQGH
1760 1770 1780 1790 1800
IQPITPVKTF TATDIRQCFD YMQSGQHIGQ LRLSLKSQDT FIEAVCSPKT
1810 1820 1830 1840 1850
MIFQSDASYL LVGGLGGLGA EIARWMAEHG ARNLIFLSRS ADAESNIRLF
1860 1870 1880 1890 1900
RELESQGCSV QAIKGSVCNA SDVKRAISAA RIKLKGIFNM SMVLQDASLL
1910 1920 1930 1940 1950
KMSSDEWNAA TGPKIQGTWN LHDASLDQDL DFFLLFSSMG GILGIPGQAN
1960 1970 1980 1990 2000
YASANTFMDA FVQFRHSSHL PASVIDIGEV QGIGHVANNP EILNRLKLLE
2010 2020 2030 2040 2050
CARMSQKDLF HAITIAISHS LPPQTLDYSR YENPAQFITG LRDTTGMLDS
2060 2070 2080 2090 2100
TGGKSMLLDS RLAAYVGNSA AVTAPTETKT SANKLNNFVS SAATDSAILS
2110 2120 2130 2140 2150
EPSATQFVSL EIARWVFDLL MKPVDDDSEI DLSRSLVDVG LDSLAAVEMR
2160 2170 2180 2190
SWLKSSLGLD ISVLEIMASP SLAAMGEHVI RELVRKFGGD NKN
Length:2,193
Mass (Da):240,602
Last modified:May 8, 2019 - 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:i59E0F629D99E78B1
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
RCNU01000014 Genomic DNA Translation: RWQ92174.1

<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
RCNU01000014 Genomic DNA Translation: RWQ92174.1

3D structure databases

SMRiA0A443HK66
ModBaseiSearch...

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.47.10, 1 hit
InterProiView protein in InterPro
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH_C
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
PROSITEiView protein in PROSITE
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 1 hit

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 nameiVDTX1_BYSSP
<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: A0A443HK66
<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 16, 2019
Last sequence update: May 8, 2019
Last modified: December 2, 2020
This is version 9 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
UniProt is an ELIXIR core data resource
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