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Entry version 36 (08 May 2019)
Sequence version 1 (16 Nov 2011)
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Protein

Beauvericin nonribosomal cyclodepsipeptide synthetase BEA1

Gene
N/A
Organism
Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum)
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

Beauvericin nonribosomal cyclodepsipeptide synthetase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:23832252). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (PubMed:23832252). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclisation of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (By similarity).By similarity1 Publication

<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 functionIsomerase, Ligase, Methyltransferase, Multifunctional enzyme, Transferase
LigandS-adenosyl-L-methionine

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:
Beauvericin nonribosomal cyclodepsipeptide synthetase BEA11 Publication
Short name:
BEAS1 Publication
Including the following 2 domains:
Nonribosomal peptide synthetaseBy similarity (EC:6.1.2.-By similarity)
S-adenosyl-L-methionine-dependent N-methyltransferaseBy similarity (EC:2.1.1.-By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 intermedia (Bulb rot disease fungus) (Fusarium proliferatum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri948311 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 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

Impairs the production of beauvericin (PubMed:23832252).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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004421471 – 3092Beauvericin nonribosomal cyclodepsipeptide synthetase BEA1Add BLAST3092

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 residuei1059O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2500O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2594O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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_and_domains_section">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>Domaini1022 – 1098Carrier 1PROSITE-ProRule annotationAdd BLAST77
Domaini2466 – 2540Carrier 2PROSITE-ProRule annotationAdd BLAST75
Domaini2560 – 2634Carrier 3PROSITE-ProRule annotationAdd BLAST75

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>Regioni70 – 458Condensation 1Sequence analysisBy similarityAdd BLAST389
Regioni499 – 896Adenylation 1Sequence analysisBy similarityAdd BLAST398
Regioni1116 – 1543Condensation 2Sequence analysisBy similarityAdd BLAST428
Regioni1572 – 1931Adenylation 2Sequence analysisBy similarityAdd BLAST360
Regioni1999 – 2139S-adenosyl-L-methionine-dependent N-methyltransferaseSequence analysisBy similarityAdd BLAST141
Regioni2678 – 3084Condensation 3Sequence analysisBy similarityAdd BLAST407

<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

NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains required for further modifications are also present. Beauvericin synthetas has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (PubMed:23832252). During catalysis, C3 and C2 take turns to incorporate the two biosynthetic precursors into the growing depsipeptide chain that swings between T1 and T2a/T2b with C3 cyclizing the chain when it reaches the full length (By similarity).By similarity1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NRP synthase family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 3 hits
3.30.559.10, 3 hits
3.40.50.12780, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR029063 SAM-dependent_MTases

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501 AMP-binding, 3 hits
PF00668 Condensation, 3 hits
PF00550 PP-binding, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00823 PKS_PP, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336 SSF47336, 3 hits
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455 AMP_BINDING, 2 hits
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 3 hits

<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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

G3GBU7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSLNTKSGT PVIPLLLRSD DASHTDTLVE EVSCSLGLGR DRIENILPST
60 70 80 90 100
AFQQDVIDCA GSEKQRSIGH VAYEISNDID ISKLAAAWKD TIHRTPALRT
110 120 130 140 150
CAFTSSSGET YQVILKDSFV FSWMFSTSAD QKDAVTKDEA AAAAYGPRCN
160 170 180 190 200
RFVLLDDPIE KRKLLIWTFS HALVDTSFQE RILERVLKAY THGHDEVPNR
210 220 230 240 250
PYTPESSDPE DDDLSLTPTD GSKTPETEGL HPATQYWKNY LSDLNASAFP
260 270 280 290 300
HLTSPLAVPY PNAKSEHRFT FTASAQSTWP SLAICRTALA ILLSRYTHSQ
310 320 330 340 350
EALFGVVTEQ HQLLVNGPTR TVVPFRVHCA SDQSLSDIIG AVYANDDAIR
360 370 380 390 400
QFSDVGLRSI SSTGDDGVAA CGFQTVLSVT EGDNEQSSSC EILQKTGESE
410 420 430 440 450
LFMPCTNRAL LLHCQMASDG LSMIARYDKS LIDSQQIARL LRQLGQLIQR
460 470 480 490 500
LRVSPDELPS AGELDILTSE DQAEIQSWNS HPIPSQPTLI HKEMLKAASL
510 520 530 540 550
SPSKVAICAW DGEWTYSELD NITSRLAALI RFSTPDQEHA ILPIYFEKSK
560 570 580 590 600
WVVASMLAVM KAGHAFTLID PNDPPARVAQ VVGQTGATVA LTSKLYRKKV
610 620 630 640 650
QGIIERCIIV DDDLVQSLIC TCALKPDPTL AKVAPEDLAY VIFTSGSTGD
660 670 680 690 700
PKGIMIEHRA FSSCALKFGS ALGINSDTRA LQFGSHAFGA CLLEIMTTLI
710 720 730 740 750
HGGCVCIPSD DDRMNNVPAF VNRANVNWMM ATPSYMGTFQ PDDVPGLKTL
760 770 780 790 800
VLVGEQMSPS VNAIWAPRVQ LLDGYGQSES SSICFVGKIS SSGADPNNIG
810 820 830 840 850
HSVGAHSWII DPSDPNRLVP IGGIGELVIE SPGIARDYII PLPTEKSPFF
860 870 880 890 900
STVPPWYPFK ELPNGIRFYR TGDLARYASD GTVVCLGRMD SQVKIRGQRV
910 920 930 940 950
ELGAVETYLR QQLPEDMSIV VEAIKPSDSP TSSVLVAFLI ASEAAESIED
960 970 980 990 1000
AAILDLAATK AMSVKLEQVL PRHSIPSCYI SMQYIPRTAT GKVDRRKLRS
1010 1020 1030 1040 1050
IGRDMLAQQL QGSSSRPSQS SSPTTSSPSR LEEVWCQCLG LETGAANVGS
1060 1070 1080 1090 1100
TFFELGGHSI TAIKMVNMAR SAGIDLKVSD IYQNPTLAGL EAIVNGSAVP
1110 1120 1130 1140 1150
YAIIPTTTRD GPVEQSYSQG RLWFLDQLEV GALWYLIPYA VRMRGMVDIY
1160 1170 1180 1190 1200
ALSRALMALE QRHETLRTTF EDRDGAGVQI IHQTLFKDLR VVDTTDGNYL
1210 1220 1230 1240 1250
QLLKQEQTTP FNLTSEAGWR VLLIRLNDTD YVLSIVMHHI VSDGWSIDVL
1260 1270 1280 1290 1300
RHDLSALYAA ALQGRDLASA MNPLPIQYSD FAMWQKQEAQ ALEHEKQLDY
1310 1320 1330 1340 1350
WKRQLADCSP AKLPTDFPRP ALLSGEAGVV PVSIDGQLYQ NLRDFCNENN
1360 1370 1380 1390 1400
TTSFAVLLAA FRAAHYRLTG VEDAVIGTPI ANRNRWELEN IIGFFVNTQC
1410 1420 1430 1440 1450
MRITVDDQDT FGSLVRQVRA TTTAAFENED VPFERVVSTM LPGSRDLSRT
1460 1470 1480 1490 1500
PLAQLIFAVH SQKDLGRFEL QGLESEIVAS KAYTRFDIEF HLFQEADGLK
1510 1520 1530 1540 1550
GSCNFATDLF KPETVENVVS VFFQILRNGL EKPNIPISVL PLTDGIEELR
1560 1570 1580 1590 1600
RLDLLRIKKV EYPRDASLVD IFRTQVAAYP DSLAVVDSSS RLTYTELDRQ
1610 1620 1630 1640 1650
SDRLAARLRR QGMPAETLVG VLAPRSCEAI VAIIGILKAN LAYLPFDVKS
1660 1670 1680 1690 1700
PFARLEDILS SIPGQTIVLL GSDVPVPELS IPGLEFMRIV DAIESYDTND
1710 1720 1730 1740 1750
LNGHAHVDDS NPTATSLAYV LFTSGSTGRP KGVMVEHRVI VRLMTSNIIP
1760 1770 1780 1790 1800
DFPVQPRSAH MFNIAFDGAT YEIFFTLLNG GTLVCIDYMT TLDVKALQDV
1810 1820 1830 1840 1850
FIKEQINAAC MAPALLKLYL TDARDALRGL DFLMAAGDRF DGQDAIEAQS
1860 1870 1880 1890 1900
LVRGQCYNGL LALVSWGELV VTGDGLARGY FDPALNENRF IHIEVDGQRV
1910 1920 1930 1940 1950
RAYRTGDRVR YRVGDGLIEF FGRMDTQFKI RGNRIESAEV EAAMLSHGSV
1960 1970 1980 1990 2000
RDAAVVVQKD DGEKSDLVGF VVIDHDHSLE GDANDNQVEG WQDHFETEMY
2010 2020 2030 2040 2050
ADIGDIDPST IGKDFKGWTS MYDGSEIDKA EMQEWLDDTI KTLCDVQAPG
2060 2070 2080 2090 2100
HVLEVGTGSG MILFNLGDGL QSYRGLEPSK SAAAFTNSVI KSVPSLAGKA
2110 2120 2130 2140 2150
EVHVGTAQDI SQLTNLHPDL VVINSVAQYF PSPEYLAQVA DTLVHLSGVK
2160 2170 2180 2190 2200
RLFFGDMRTN ATNKHFLAAR AIRTLGDTAT KDSVRQKMAE LEEREEELLV
2210 2220 2230 2240 2250
EPAFFTTLQD RFPDLVHHVE ILPKNMHATN ELSAYRYAAV VHIRDHDSVP
2260 2270 2280 2290 2300
VHTIEKGSWV DFGASRMNRT SLLQFLRRSK GSSTVAITNI PFAKTVFERQ
2310 2320 2330 2340 2350
IVESLEAEED SKLDGAAWTS AVRSDAESRA SLSVPDLHRL AEEAGFRLEI
2360 2370 2380 2390 2400
SVARQWSQSG TLDAVFHHLP SPSNTGRTLI KFPTDNHLRS SATLANRPLQ
2410 2420 2430 2440 2450
GLQRRRAALQ VRERLQSLLP SYMIPSSIVV LDQMPLNPNG KVDRKELARQ
2460 2470 2480 2490 2500
ARIIPKQQTA LPVQAVPISD IEAILCDEAT ATFGMKVDIS DDFFKLGGHS
2510 2520 2530 2540 2550
LLATKLISRV EQRFNVRASV KDVFDNPVFA HLAVVIREGL ASRTTLTNGQ
2560 2570 2580 2590 2600
DKQGWSARVA PRTETEIILC DEASKLLGIE VGITDNFFDL GGHSMMATKL
2610 2620 2630 2640 2650
AMRLGRRLDT TIVVKDIFDY PVLFQLSKKL ESAGSGADSE EVHVDDYNPF
2660 2670 2680 2690 2700
ELLSLEDPKE FIQREICSQL NVSLESIQDM YKSTQMQNSF LFSPGTGSPR
2710 2720 2730 2740 2750
PLTPFYIDFP VDSDPPTLVN ACHSLVQHID MFRTVFVLAS GQLYQVVLKH
2760 2770 2780 2790 2800
LDVPIETIVT NQNVNTATND FLDEHAQDPI RLGESLIRVA ILKQSSSVRV
2810 2820 2830 2840 2850
LLRLSHALYD GLSREPIVRN LHILFNGMSL LPPTQFRRYM EYTANSQEKG
2860 2870 2880 2890 2900
FEFWRDVIGD SPMTILSDAN NGAYRREVSP SKALHLSKVV SVPSQAIRSS
2910 2920 2930 2940 2950
IATQATVFNS ACALVLSKES GSSNVVFGRI VSGRQGLLVN CQDIIGPCTN
2960 2970 2980 2990 3000
AVPVRAHIGT DENHHQMLRD MQDQYLRSLP FETLGFEEIK RNCTDWPDST
3010 3020 3030 3040 3050
TNFACCVTYH NFEYHPESEV EQQRVEMGVL SKHVELRKDE PLYDLAIAGE
3060 3070 3080 3090
VEPDGMSLKV TIIARAHLFE EERVQYFLEE VCDTFQTLNF SL
Length:3,092
Mass (Da):341,855
Last modified:November 16, 2011 - 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:i15CC2BE390F0F25B
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
JF826561 Genomic DNA Translation: AEN14638.1

<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
JF826561 Genomic DNA Translation: AEN14638.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

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

Family and domain databases

Gene3Di1.10.1200.10, 3 hits
3.30.559.10, 3 hits
3.40.50.12780, 3 hits
InterProiView protein in InterPro
IPR036736 ACP-like_sf
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR042099 AMP-dep_Synthh-like_sf
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF00501 AMP-binding, 3 hits
PF00668 Condensation, 3 hits
PF00550 PP-binding, 3 hits
SMARTiView protein in SMART
SM00823 PKS_PP, 3 hits
SUPFAMiSSF47336 SSF47336, 3 hits
SSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 2 hits
PS50075 CARRIER, 3 hits
PS00012 PHOSPHOPANTETHEINE, 3 hits

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 nameiBEA1_GIBIN
<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: G3GBU7
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2017
Last sequence update: November 16, 2011
Last modified: May 8, 2019
This is version 36 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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