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Entry version 33 (22 Apr 2020)
Sequence version 1 (18 Sep 2013)
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Protein

Beauvericin nonribosomal cyclodepsipeptide synthetase BEA1

Gene

BEA1

Organism
Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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

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:25543026, PubMed:27750383, PubMed:28125067). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (By similarity). 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 similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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 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%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:
Beauvericin nonribosomal cyclodepsipeptide synthetase BEA11 Publication
Short name:
BEASBy similarity
Alternative name(s):
Beauvericin biosynthesis cluster protein 11 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%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:BEA11 Publication
Synonyms:NRPS221 Publication
ORF Names:FFUJ_09296
<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 fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
<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 identifieri1279085 [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
  • UP000016800 <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: Chromosome 9

<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

Leads to complete loss of beauvericin biosynthesis (PubMed:27750383).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_00004421451 – 3135Beauvericin nonribosomal cyclodepsipeptide synthetase BEA1Add BLAST3135

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 residuei1058O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2543O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2637O-(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 highly repressed by the histone deacetylase HDA1 and the beauvericin cluster-specific repressor BEA4 (PubMed:27750383). BEA biosynthesis is also repressed by the activity of the H3K27 methyltransferase KMT6 (PubMed:27750383).1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
S0EN43

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>Domaini1021 – 1097Carrier 1PROSITE-ProRule annotation1 PublicationAdd BLAST77
Domaini2509 – 2583Carrier 2PROSITE-ProRule annotation1 PublicationAdd BLAST75
Domaini2603 – 2677Carrier 3PROSITE-ProRule annotation1 PublicationAdd 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 analysis1 PublicationAdd BLAST389
Regioni499 – 896Adenylation 1Sequence analysis1 PublicationAdd BLAST398
Regioni1115 – 1542Condensation 2Sequence analysis1 PublicationAdd BLAST428
Regioni1571 – 1974Adenylation 2Sequence analysis1 PublicationAdd BLAST404
Regioni2042 – 2182S-adenosyl-L-methionine-dependent N-methyltransferaseSequence analysis1 PublicationAdd BLAST141
Regioni2721 – 3127Condensation 3Sequence analysis1 PublicationAdd 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:28125067). 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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000022_60_1_1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 2 hits
3.30.559.10, 3 hits
3.40.50.12780, 2 hits
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010071, AA_adenyl_domain
IPR029058, AB_hydrolase
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, 2 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

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01733, AA-adenyl-dom, 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%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.

S0EN43-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSLNTKSGT PVVPLLLRSD DASHTDTLVE EVSCSLGLGR DRIENILPST
60 70 80 90 100
AFQQDVIDCA GSEKQRSIGH VAYEISNDID ISKLAAAWKD TINRTPALRT
110 120 130 140 150
CAFTSSSGET YQVILKDSFV FSWMFSTSAD QKDAVVKDEA AAAASGPRCN
160 170 180 190 200
RFVLLDDPIQ KKILIWTFSH ALVDTSFQER ILGRVLKAYT HGHDELSNRP
210 220 230 240 250
YTPESSDPED DGLSLTPTDG SKTPETEGLH PATQYWKNYL SDLNASAFPH
260 270 280 290 300
LTSPLAVPYP NAKSEHRITF TASSSSTWPS VAVCRTALAI LLSRYTHSQE
310 320 330 340 350
ALFGVVTEQQ QLLVNGPTRT VVPFRVHCAS DQSLSDIIDV VNANDDAIRQ
360 370 380 390 400
FADVGLRSIS STGDDGVAAS GFQTVLLVTE GDNEQSSSTF EILQKTEESE
410 420 430 440 450
LFMPCTNRAL LLHCQIASDG LSIIARYDKS LIHSQQIARL LRQLGQLIQR
460 470 480 490 500
LRGSPDKLPS AGELDISTSE DQAEIQSWNS HPIPSQPTLI HKEMLKTASL
510 520 530 540 550
SPSKVAICAW NGEWTYSELD NITSRLAALI KFSTPDQEHA ILPIYFEKSK
560 570 580 590 600
WVVASMLAVI KAGHAFALID PNDPPARVSQ VVGQTGATVA LTSKLYRSKV
610 620 630 640 650
QGIIERCIIV DDDLVQSLIC TCALKPDPTL AKVTPEDLAY VIFTSGSTGD
660 670 680 690 700
PKGIMIEHRA FSSCALQFGS ALGINSDTRA LQFGSHAFGA CLLEIMTTLI
710 720 730 740 750
HGGCVCIPSD DDRMNNVPAF VNRANVNWMM ATPSYMGTFQ PDDVPGLKTL
760 770 780 790 800
VLVGEQMSPS VNAIWAPRVQ VLDGYGQSES SSICFVGKIS SSGADPNNIG
810 820 830 840 850
HSVGAHSWII DPSDPNRLVP IGAIGELVIE SPGIARDYII PPPTENSPFF
860 870 880 890 900
STVPPWYPFK ELPNGIKFYR TGDLARYASD GTVVCLGRMD SQVKIRGQRV
910 920 930 940 950
ELGAVETHLR QQLPDDMSIV VEAVKPSDLP TSTVLVAFLI TEATKSVRDA
960 970 980 990 1000
TILDLAATKA MSVKLEHVLP RHSIPSCYIS MQHLPRTATG KVDRRKLRSI
1010 1020 1030 1040 1050
GRDMLAQQLQ GTSFRPSQLS STTTSSQSKL EEVWRQCLGL EPGAANINST
1060 1070 1080 1090 1100
FFELGGHSIT AIKMVNMARS AGIDLKVSDI YQNPTLAGLE AIVNGSAEPY
1110 1120 1130 1140 1150
AIIPTTTRDG PVEQSYSQGR LWFLDQLEVG ALWYLIPYAV RMRGLVDIDA
1160 1170 1180 1190 1200
LSRALMALEQ RHETLRTTFE DCDGAGVQII HKILSKKLRV VDAPDSDYLD
1210 1220 1230 1240 1250
LLKQEQTTPF DLTSEAGWRA LLIRLNDTDY ILSIVMHHIV SDGWSIDVLR
1260 1270 1280 1290 1300
HDLSQLYAAA LQGRDLASAM NPLPIQYSDF AMWQKQEAQA LEHEKQLDYW
1310 1320 1330 1340 1350
KRQLADCSPA KLPTDFPRPA LLSGEAGVVP VSIDRQLYQN LRDFCNENNT
1360 1370 1380 1390 1400
TSFAVLLAAF RAAHYRLTGV DDAVIGTPIA NRNRWELENI IGFFVNTQCM
1410 1420 1430 1440 1450
RITVDDQDTF GSLVSQVRAT TTAAFENEDV PFERVVSTML PGSRDLSRTP
1460 1470 1480 1490 1500
LAQLIFAVHS QKDLGRFELQ GLESEVVASK AYTRFDIEFH LFQEADGLRG
1510 1520 1530 1540 1550
SCNFATDLFR PETVENMVSV FFQILRNGLE KPNIPISVLP LTDGIEELRR
1560 1570 1580 1590 1600
LDLLRIKKVE YPRDASLVDI FRTQVAAYPD SLAVVDSSSR LTYTELDLQS
1610 1620 1630 1640 1650
DRLAARLRRQ GMPAETLVGV LAPRSCEAIV AIIGILKANL AYLPFDVKSP
1660 1670 1680 1690 1700
SARLEDILSS IPGQTIVLLG SDVPVPELSI PGLEFMRIVD AIECCDTNNL
1710 1720 1730 1740 1750
NGHAHVDNSN PTATSLAYVL FTSGSTGRPK GVMVEHRVIV RLMTSNIIPD
1760 1770 1780 1790 1800
FPVQPRSAHM FNIAFDGATY EIFFTLLNGG TLVCIDYMTT LDVKALQDVF
1810 1820 1830 1840 1850
LKEKINAACM APALLKLYLT DARDALRGLD FLMAAGDRFD GQDAIEAQSL
1860 1870 1880 1890 1900
VRGQCYNGYG PTENGIMSTR YPIAVGDSFI NGVPIGRAVN NSGAYVTDLN
1910 1920 1930 1940 1950
QQLVGVGVMG ELVVTGDGLA RGYFDPALNE NRFIHIEVDG QRVRAYRTGD
1960 1970 1980 1990 2000
RVRYRVGDGL IEFFGRMDTQ FKIRGNRIES AEVEAAMLGH GSVRDAAVVV
2010 2020 2030 2040 2050
QKDDGEKADL VGFVVIDHDH SLEGDANDNQ VEGWQDHFET EMYADIGDID
2060 2070 2080 2090 2100
PFTIGKDFKG WTSMYDGSEI DKVEMQEWLD DTIKTLRDGQ APGHVLEVGT
2110 2120 2130 2140 2150
GSGMILFNLG DGLQSYRGLE PSKSAAAFTN SVIKSVPSLA SKAEVHVGTA
2160 2170 2180 2190 2200
QDVSQLTDLH PDLVVINSVA QYFPSPEYLA QVADTLIHIP GVKRLFFGDM
2210 2220 2230 2240 2250
RTNATNKHFL AARAIRTLGD TATKDFVRQK MAELEEREEE LLVEPAFFTA
2260 2270 2280 2290 2300
LQDRFPDLVH HVEILPKNMH ATNELSAYRY AAVVHIRDSD SVPVHTIEKS
2310 2320 2330 2340 2350
TWVDFGASRM DRTSLLQFLR RSKGSPTVAI SNIPFAKTIF ERQIVESLEA
2360 2370 2380 2390 2400
EDESKLDGAV WISAVGSDAD SRASLSVPDL RRLAEEAGFR LEVSAARQWS
2410 2420 2430 2440 2450
QSGALDAVFH HLPSPSDTRR TLIKFPNDNH LRSSATLSNR PLQGLQRRRA
2460 2470 2480 2490 2500
TLQVRERLQS LLPSYMIPSS IVVLDQMPLN PNGKVDRKEL ARQARIMPKQ
2510 2520 2530 2540 2550
QTALPVQAVP ISDIEAILCD EATATFGMKV DISDDFFKLG GHSLLATKLI
2560 2570 2580 2590 2600
SRVEQRFNVR VTVKDVFDNP VFANLAVVIR EGLASRTTLT NSQDKQGWSA
2610 2620 2630 2640 2650
RVAPRTETEI TLCDEASKLL GIEVGITDNF FDLGGHSMMA TKLAMRLGRR
2660 2670 2680 2690 2700
LDTTIVVKDI FDYPVLFQLS KKLESTDSGT DNEEVQVDDY TPFELLSLEN
2710 2720 2730 2740 2750
PQDFIQRQIC SQLNVSLESI QDMYQSTQMQ KSFLFSPGTG SPRPLTPFYI
2760 2770 2780 2790 2800
DFPVDSDPPT LVNACHSLVQ HIDMFRTVFV LASEQLYQVV LKHLEVPIET
2810 2820 2830 2840 2850
IVTNQNVNTA TNDFLVEHAQ DPIRLGESLI RIAILKQSSS VRVLLRLSHA
2860 2870 2880 2890 2900
LYDGLSLEPI VRNLHILFNG MSLLPPTQFR RYMEYTANSQ EKGFEFWRDV
2910 2920 2930 2940 2950
IGDSPMTILS DAGNGAYHRE VSPSKALHLS KVVSVPSQAI RSSIATQATV
2960 2970 2980 2990 3000
FNSACALVLS KESRSSDVVF GRIVSGRQGL PVNCQDIIGP CTNAVPVRAH
3010 3020 3030 3040 3050
IGTDGNHHQM LRDMQDQYLR SLPFETLGFE EIKRNCTDWP DSTTNFACCV
3060 3070 3080 3090 3100
TYHNFEYHPE SEVEQQRVEM GVLSKHVELR KDEPLYDLAI AGEVEPDGMS
3110 3120 3130
LKVTIIARAH LFEEERVQYF LEEVCNTFQT LNFSL
Length:3,135
Mass (Da):346,309
Last modified:September 18, 2013 - 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:i82A8B2E7B86EF1FC
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
HF679031 Genomic DNA Translation: CCT73878.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
CCT73878; CCT73878; FFUJ_09296

<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
HF679031 Genomic DNA Translation: CCT73878.1

3D structure databases

SMRiS0EN43
ModBaseiSearch...

Genome annotation databases

EnsemblFungiiCCT73878; CCT73878; FFUJ_09296

Phylogenomic databases

HOGENOMiCLU_000022_60_1_1

Family and domain databases

Gene3Di1.10.1200.10, 2 hits
3.30.559.10, 3 hits
3.40.50.12780, 2 hits
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR010071, AA_adenyl_domain
IPR029058, AB_hydrolase
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, 2 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
TIGRFAMsiTIGR01733, AA-adenyl-dom, 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

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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 nameiBEA1_GIBF5
<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: S0EN43
<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 25, 2017
Last sequence update: September 18, 2013
Last modified: April 22, 2020
This is version 33 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. SIMILARITY comments
    Index of protein domains and families
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