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Entry version 102 (08 May 2019)
Sequence version 2 (01 Oct 2000)
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Protein

Enniatin synthase

Gene

ESYN1

Organism
Fusarium equiseti (Fusarium scirpi)
Status
Reviewed-Annotation score:

Annotation score:5 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

Nonribosomal peptide synthetase that synthesizes enniatin by coupling three D-hydroxycarboxylic acids and three L-amino acids via amide and ester bonds in an alternating fashion (PubMed:7601090, PubMed:10887181). Whereas ESYN1 can accept different amino acids as precursors (L -valine, L-isoleucine or L-leucine), only one species of D-hydroxycarboxylic acid can be found in natural enniatin isolates (D-hydroxyisovaleric acid, D-Hiv) (PubMed:7601090, PubMed:10887181). D-Hiv stems from L-valine deanimation by a valine aminotransferase to 2-keto-isovaleric acid (2-Kiv), which becomes subsequently reduced by a keto-isovaleric acid reductase (KivR) to D-Hiv (PubMed:7601090, PubMed:10887181). Peptide bond formation and N-methylation of the amino acid occur before three enzyme-bound dipeptidols are condensed to a hexapeptidol (PubMed:7601090, PubMed:10887181).2 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 6 phosphopantetheines covalently.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The N-methylation activity is inhibited by S-adenosyl-L-homocysteine and sinefugin.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: enniatin biosynthesis

This protein is involved in the pathway enniatin biosynthesis, which is part of Antibiotic biosynthesis.3 Publications
View all proteins of this organism that are known to be involved in the pathway enniatin biosynthesis and in Antibiotic biosynthesis.

<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 functionLigase, Methyltransferase, Multifunctional enzyme, Transferase

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00234

<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:
Enniatin synthase1 Publication
Alternative name(s):
Nonribosomal cyclopeptide synthetase ESYN11 Publication
Including the following 2 domains:
N-methylcyclopeptide synthetase1 Publication (EC:6.3.2.-)
S-adenosyl-L-methionine-dependent N-methyltransferase1 Publication (EC:2.1.1.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ESYN11 Publication
<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>OrganismiFusarium equiseti (Fusarium scirpi)
<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 identifieri61235 [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 incarnatum-equiseti 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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Enniatins have antimicrobial, antiviral and cytotoxic properties (PubMed:9170286, PubMed:16562855, PubMed:17326668). The bioactivity of enniatins can be linked to their inhibition of drug efflux pumps (PubMed:15707993).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2106Y → A, S or V: Reduces S-adenosyl-L-methionine binding. 1 Publication1
Mutagenesisi2106Y → F: Has minimal effect on S-adenosyl-L-methionine binding. 1 Publication1

<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_00001803061 – 3131Enniatin synthaseAdd BLAST3131

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 residuei1047O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2538O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2632O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q00869

<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
Q00869

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_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>Domaini1010 – 1086Carrier 1PROSITE-ProRule annotationAdd BLAST77
Domaini2504 – 2578Carrier 2PROSITE-ProRule annotationAdd BLAST75
Domaini2598 – 2671Carrier 3PROSITE-ProRule annotationAdd BLAST74

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>Regioni53 – 466Condensation 1Sequence analysisBy similarityAdd BLAST414
Regioni495 – 887Adenylation 1Sequence analysisBy similarityAdd BLAST393
Regioni1105 – 1534Condensation 2Sequence analysisBy similarityAdd BLAST430
Regioni1563 – 1960Adenylation 2Sequence analysisBy similarityAdd BLAST398
Regioni2021 – 2177S-adenosyl-L-methionine-dependent N-methyltransferaseSequence analysisBy similarity3 PublicationsAdd BLAST157
Regioni2718 – 3123Condensation 3Sequence analysisBy similarityAdd BLAST406

<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 (Probable). Enniatin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (Probable). The precursors D-hydroxycarboxylic acids and L-amino acids become activated at the A1 and the A2 domains. N-methylation of the amino acid takes place at the MT-domain. The building blocks are transferred from one module to another by means of T-domains and are ultimately stored at the waiting position T2b. Condensation of the building blocks and final cyclization and release from the enzyme is catalyzed by the C-domains (Probable).Curated

<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

Keywords - Domaini

Repeat

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
IPR013216 Methyltransf_11
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
PF08241 Methyltransf_11, 1 hit
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, 2 hits

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.

Q00869-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLHTPSDGQ QDPALASKTL CEQISRALGL GQDKIENIFP GTPFQRDVID
60 70 80 90 100
CAADDKQRAV GHAVFEIPKD IDAARLAAAW KETVLHTPAL RTCTFTSKSG
110 120 130 140 150
DVLQVVLRDS FVFSWMSGPS VDLKEAVVQD EAAAALAGPR CNRFVLLEDP
160 170 180 190 200
DTKERQLIWT FSHALVDSTF QERILRRVLK AYKDANDEHP RQFETPDSSQ
210 220 230 240 250
ATPEEDLQPN PSKMLKIPQA ADMDRAVEFW KDHLSGLKCF CLPAFVLSSV
260 270 280 290 300
YAHPDAKAEH RISYSSSAQQ KMSSATICRT ALAILLSRYT HSPEALFGIV
310 320 330 340 350
TEQTPLLEEQ LMLDGPTRTV VPIRVSCASE QSVSDIMSTI DSYDQTMRQF
360 370 380 390 400
AHAGLRNIAS AGDDESAACG FQTVLLVSDG DAQPASTWEI LKKTEEPEGF
410 420 430 440 450
IPCTNRALLL SCQMTSSGAH LTARYDQSII DAEQMARLLR QLGHLIQNLQ
460 470 480 490 500
TSTDLPVEKV DMMTQEDWLE IERWNSDSID AQDTLIHSEM LKWTSQSPNK
510 520 530 540 550
AAVAAWDGEW TYAELDNVSS RLAQHINSID LGKEHAIVPI YFEKSKWVVA
560 570 580 590 600
SMLAVLKAGH AFTLIDPSDP PARTAQVVQQ TSATVALTSK LHRETVQSTV
610 620 630 640 650
GRCIVVDEEF VKSLPQSSEL SASVKAHDLA YVIFTSGSTG IPKGIMIEHR
660 670 680 690 700
SFSSCAIKFG PALGITSDTR ALQFGSHAFG ACILEIMTTL IHGGCVCIPS
710 720 730 740 750
DDDRMNNVLE FINRTNVQLG HATPSYMGTF QPEVVPGLKT LVLVGEQMSA
760 770 780 790 800
SVNEVWAPRV QLLNGYGQSE SSSICCVAKI SPGSSEPNNI GHAVGAHSWI
810 820 830 840 850
VDPEDPNRLA PIGAVGELVI ESAGIARDYI VAPTQDKSPF IKTAPTWYPA
860 870 880 890 900
KQLPDGFKIY RTGDLACYAS DGSIVCLGRM DSQVKIRGQR VELGAVETHL
910 920 930 940 950
RQQMPDDMTI VVEAVKFSDS SSTTVLTAFL IGAGEKNSHI LDQRATREIN
960 970 980 990 1000
AKMEQVLPRH SIPAFYISMN NLPQTATGKV DRRKLRIMGS KILSQKTHST
1010 1020 1030 1040 1050
PSQQSQAAIS SGTDTYTKLE SIWITSLDLE PGSANMSATF FEMGGNSIIA
1060 1070 1080 1090 1100
IKMVNMARSN GIELKVSDIY QNPTLAGLKA IVIGTSLPYS LIPKVTRQGP
1110 1120 1130 1140 1150
VSEQSYAQNR MWFLDQLSEG ASWYLIPFAV RMRGPVDVDA LTRALLALEQ
1160 1170 1180 1190 1200
RHETLRTTFE NQDGVGVQII HDRLSKELQV IDALDGDEGG LKTLYKVETT
1210 1220 1230 1240 1250
TFDITSEAGW SSTLIRLGKD DHILSIVMHH IISDGWSIDV LRRELIQLYA
1260 1270 1280 1290 1300
AALQGKDPSS ALTPLPIQYS DFAVWQKQEA QAAEHERQLQ YWKKQLADSS
1310 1320 1330 1340 1350
PAKIPTDFPR PDLLSGDAGV VPVAIDGELY QKLRGFCNKH NSTAFSILLA
1360 1370 1380 1390 1400
AFRAAHYRLT AVDDAVIGIP IANRNRWELE NMIGFFVNTQ CMRIAVDETD
1410 1420 1430 1440 1450
TFESLVRQVR STTTAAFAHE DVPFERVVSA LQPGHRDLSR TPLAQIMFAV
1460 1470 1480 1490 1500
HSQKDLGRFE LEGIQSEPIA SKAYTRFDVE FHLFQQADGL KGSCNFATDL
1510 1520 1530 1540 1550
FKPETIQNVV SVFFQILRHG LDQPETCISV LPLTDGVEEL RRLDLLEIKR
1560 1570 1580 1590 1600
TNYPRDSSVV DVFREQAAAN PEVIAVTDSS SRLTYAELDN KSELLSRWLR
1610 1620 1630 1640 1650
RRNLTPETLV SVLAPRSCET IVAYVGILKA NLAYLPLDVR SPVTRMKDIL
1660 1670 1680 1690 1700
SSVSGNTIVL MGSGVEDPGF DLPQLELVRI TDTFDETIED VQDSPQPSAT
1710 1720 1730 1740 1750
SLAYVVFTSG STGKPKGVMI EHRAIVRLVK SDNFPGFPSP ARMSNVFNPA
1760 1770 1780 1790 1800
FDGAIWEINW MLLNGGTVVC IDYLTTLDGK ELAAVFAKER VNAAFFAPAM
1810 1820 1830 1840 1850
LKLYLVDARE ALKNLDFLIV GGERFDTKEA VEAMPLVRGK IANIYGPTEA
1860 1870 1880 1890 1900
GIISTCYNIP KDEAYTNGVP IGGSIYNSGA YVMDPNQQLV GLGVMGELVV
1910 1920 1930 1940 1950
TGDGVGRGYT NPELNKNRFI DITIEGKTFK AYRTGDRMRA RVGDGLLEFF
1960 1970 1980 1990 2000
GRMDNQFKIR GNRIEAGEVE SAMLSLKNVL NAAIVVRGGG EDEGPLEMVG
2010 2020 2030 2040 2050
FIVADDKNDT TEEEETGNQV EGWQDHFESG MYSDISTAVD QSAIGNDFKG
2060 2070 2080 2090 2100
WTSMYDGKDI DKGEMQEWLD DAIHTLHNGQ IPRDVLEIGT GSGMILFNLN
2110 2120 2130 2140 2150
PGLNSYVGLD PSKSAVEFVN RAVESSPKFA GKAKVHVGMA TDVNKLGEVH
2160 2170 2180 2190 2200
PDLVVFNSVV QYFPTPEYLA EVIDGLIAIP SVKRIFLGDI RSYATNGHFL
2210 2220 2230 2240 2250
AARAIHTLGT NNNATKDRVR QKIQELEDRE EEFLVEPAFF TTLKERRPDV
2260 2270 2280 2290 2300
VKHVEIIPKN MKATNELSAY RYTAVVHLRD ETDEPVYHIE KDSWVDFEAK
2310 2320 2330 2340 2350
QMDKTALLDH LRLSKDAMSV AVSNITYAHT AFERRIVESL DEDSKDDTKG
2360 2370 2380 2390 2400
TLDGAAWLSA VRSEAENRAS LTVPDILEIA KEAGFRVEVS AARQWSQSGA
2410 2420 2430 2440 2450
LDAVFHHFPP SSTDRTLIQF PTDNELRSSL TLANRPLQKL QRRRAALQVR
2460 2470 2480 2490 2500
EKLQTLVPSY MVPPNIVVLD TMPLNTNGKI DRKELTRRAR TLPKQQTAAP
2510 2520 2530 2540 2550
VPDFPISDIE ITLCEEATEV FGMKVEISDH FFQLGGHSLL ATKLISRIQH
2560 2570 2580 2590 2600
RLHVRVTVKD VFDSPVFADL AVIIRQGLAM QNPVAEGQDK QGWSSRVAPR
2610 2620 2630 2640 2650
TEVEKMLCEE FAAGLGVPVG ITDNFFDLGG HSLMATKLAV RIGRRLIRHH
2660 2670 2680 2690 2700
SQGHLRLPCA FQLAKKLESS HSKSYEESGD DIQMADYTAF QLLDLEDPQD
2710 2720 2730 2740 2750
FVQSQIRPQL DSCYGTIQDV YPSTQMQKAF LFDPTTGEPR GLVPFYIDFP
2760 2770 2780 2790 2800
SNADAETLTK AIGALVDKLD MFRTVFLEAA GDLYQVVVEH LNLPIETIET
2810 2820 2830 2840 2850
EKNVNTATGD YLDVHGKDPV RLGHPCIQFA ILKTASSVRV LLRMSHALYD
2860 2870 2880 2890 2900
GLSFEYIVRG LHVLYSGRNL PPPTQFARYM QYAAHSREEG YPFWREVLQN
2910 2920 2930 2940 2950
APMTVLHDTN NGMSEQEMPA SKAVHLSEVV NVPAQAIRNS TNTQATVFNT
2960 2970 2980 2990 3000
ACALVLAKES GSQDVVFGRI VSGRQGLPVV WQDIIGPCTN AVPVHARVDD
3010 3020 3030 3040 3050
GNPQRIIRDL RDQYLRTLPF ESLGFEEIKR NCTDWPEELT NFSVCVTYHN
3060 3070 3080 3090 3100
FEYHPESEVD NQKVEMGVLA KYVELSENEP LYDLAIAGEV EADGVNLKVT
3110 3120 3130
VVAKARLYNE ARIRHVLEEV CKTFNGLNEA L
Length:3,131
Mass (Da):346,499
Last modified:October 1, 2000 - 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:iAD7663E91FAB67C4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z18755 Genomic DNA Translation: CAA79245.2

Protein sequence database of the Protein Information Resource

More...
PIRi
S39842

<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
Z18755 Genomic DNA Translation: CAA79245.2
PIRiS39842

3D structure databases

SMRiQ00869
ModBaseiSearch...

Proteomic databases

PRIDEiQ00869

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00234

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
IPR013216 Methyltransf_11
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
PF08241 Methyltransf_11, 1 hit
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, 2 hits
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 nameiESYN_FUSEQ
<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: Q00869
<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: November 15, 2002
Last sequence update: October 1, 2000
Last modified: May 8, 2019
This is version 102 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

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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