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Entry version 120 (11 Dec 2019)
Sequence version 2 (01 Jun 1998)
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Protein

Bifunctional NADP phosphatase/NAD kinase

Gene

MJ0917

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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

Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the physiological phosphoryl donor. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor. Phosphatase can use NADP or NADPH as phosphoryl donor, but NADP is the preferred substrate. Phosphatase also has an activity toward the terminal phosphate group at C-2 of adenosine in 2'-AMP and toward the phosphate group at C-1 of fructose 1,6-bisphosphate, but not toward inositol 1-phosphate.1 Publication

Miscellaneous

The phosphatase is inert toward the substrates of NAD kinase (NAD, NADH, ATP, and poly(P)). This demonstrates that the phosphatase activity never interferes with the NAD kinase activity by degrading its substrates (PubMed:16192277).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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>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

Mg2+1 PublicationNote: Mg2+. NAD and pNPPase kinase show maximum activities at 50 and 20 mM magnesium, respectively.1 Publication

<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

Phosphatase activity is slightly inhibited by ADP, NADPH and ATP, and moderately inhibited by NAD and 5'-AMP. Kinase activity is slightly inhibited by ADP and NADP.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 399 sec(-1) for kinase activity with ATP as substrate. Kcat is 424 sec(-1) for kinase activity with NAD as substrate. Kcat is 906 sec(-1) for phosphatase activity with fructose 1,6-bisphosphate and NADP as substrates. Kcat is 1007 sec(-1) for phosphatase activity with NADPH as substrate.
  1. KM=0.35 mM for ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  2. KM=3 mM for NAD (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  1. Vmax=93.4 µmol/min/mg enzyme toward ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  2. Vmax=99.2 µmol/min/mg enzyme toward NAD (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  3. Vmax=212 µmol/min/mg enzyme toward NADP (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  4. Vmax=212 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  5. Vmax=236 µmol/min/mg enzyme toward NADPH (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 100 degrees Celsius for phosphatase and kinase activies. Both are inactive below 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi69Magnesium 1By similarity1
Metal bindingi87Magnesium 1By similarity1
Metal bindingi87Magnesium 2By similarity1
Metal bindingi90Magnesium 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei90SubstrateBy similarity1
Metal bindingi243Magnesium 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei362Proton acceptorUniRule annotation1
Binding sitei367NADUniRule annotation1
Binding sitei447NADUniRule annotation1
Binding sitei464NADUniRule annotation1
Binding sitei466NADUniRule annotation1
Binding sitei474NAD; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi362 – 363NADUniRule annotation2
Nucleotide bindingi436 – 437NADUniRule annotation2
Nucleotide bindingi477 – 482NADUniRule annotation6

<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 functionHydrolase, Kinase, Multifunctional enzyme, Transferase
LigandATP-binding, Magnesium, Metal-binding, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.1.23 3260

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q58327

<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:
Bifunctional NADP phosphatase/NAD kinase
Including the following 2 domains:
NAD kinaseUniRule annotation (EC:2.7.1.23UniRule annotation)
Alternative name(s):
ATP-dependent NAD kinaseUniRule annotation
Poly(P)-dependent NAD kinase
Short name:
PPNK
NADP phosphatase (EC:3.1.3.-)
Short name:
NADPase
Short name:
pNPPase
<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
Ordered Locus Names:MJ0917
<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>OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
<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 identifieri243232 [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 lineageiArchaeaEuryarchaeotaMethanomada groupMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000805 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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_00001207001 – 574Bifunctional NADP phosphatase/NAD kinaseAdd BLAST574

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243232.MJ_0917

<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

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SMRi
Q58327

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

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 – 297NADP phosphataseAdd BLAST297
Regioni302 – 574NAD kinaseAdd BLAST273

<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

In the N-terminal section; belongs to the inositol monophosphatase superfamily.Curated
In the C-terminal section; belongs to the NAD kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
arCOG01348 Archaea
COG0061 LUCA
COG0483 LUCA

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q58327

KEGG Orthology (KO)

More...
KOi
K00858

Identification of Orthologs from Complete Genome Data

More...
OMAi
VIVPICP

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.200.30, 1 hit
3.40.50.10330, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00361 NAD_kinase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017438 ATP-NAD_kinase_N
IPR017437 ATP-NAD_kinase_PpnK-typ_C
IPR021175 Bifunctional_PpnK_predicted
IPR020583 Inositol_monoP_metal-BS
IPR000760 Inositol_monophosphatase-like
IPR016064 NAD/diacylglycerol_kinase_sf
IPR002504 NADK

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00459 Inositol_P, 2 hits
PF01513 NAD_kinase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036641 Bifunctional_PpnK_predicted, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00377 IMPHPHTASES

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF111331 SSF111331, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00629 IMP_1, 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_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.

Q58327-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVIMEGFKIA MKVIDEIDKK IKPLIGWEKA DEVVKIGADG TPTKRIDVIA
60 70 80 90 100
ENMAINILEK FSGGILISEE IGLKVVGDEL EYIFILDPID GTYNALKSIP
110 120 130 140 150
IYSTSIAVAK IKGEDKKLIR ENINNIDWIK SFIANKYTIN DLYVGIVKNL
160 170 180 190 200
ATGDLYYAIK GEGSFLEKDG EKIKIETKNI KDLKEASVGL FVYGLSNDLL
210 220 230 240 250
EFLKERKVRR VRLFGSMALE MCYVVSGALD AYINVNENSR LCDIAGAYVI
260 270 280 290 300
CREGNAIVTN KNGKPLNMKL HLMERTSLIV SNKYLHKKLI ALFGNRWIIK
310 320 330 340 350
PVKFGIVVRE DKEEAINLAI EICKYLKDKN IPFCVEDFLR ERVGGDKFDI
360 370 380 390 400
SAISHIIAIG GDGTILRASR LVNGETIPII AVNMGKVGFL AEFCKDEVFE
410 420 430 440 450
IIDKVIYGEY EIEKRSKLSC KIIKDNRVIK TPSALNEMVV ITKNPAKILE
460 470 480 490 500
FDVYVNDTLV ENVRADGIIV STPTGSTAYS LSAGGPIVEP NVDCFIISPI
510 520 530 540 550
CPFKLSSRPL VISASNRIKL KLKLEKPALL VIDGSVEYEI NKDDELIFEK
560 570
SDSYAYFVKG QSFYNKLSRC LGIK
Length:574
Mass (Da):64,119
Last modified:June 1, 1998 - 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:i89A1AF944BD99DB1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L77117 Genomic DNA Translation: AAB98922.1

Protein sequence database of the Protein Information Resource

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PIRi
E64414

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAB98922; AAB98922; MJ_0917

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mja:MJ_0917

<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
L77117 Genomic DNA Translation: AAB98922.1
PIRiE64414

3D structure databases

SMRiQ58327
ModBaseiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0917

Genome annotation databases

EnsemblBacteriaiAAB98922; AAB98922; MJ_0917
KEGGimja:MJ_0917

Phylogenomic databases

eggNOGiarCOG01348 Archaea
COG0061 LUCA
COG0483 LUCA
InParanoidiQ58327
KOiK00858
OMAiVIVPICP

Enzyme and pathway databases

BRENDAi2.7.1.23 3260
SABIO-RKiQ58327

Family and domain databases

Gene3Di2.60.200.30, 1 hit
3.40.50.10330, 1 hit
HAMAPiMF_00361 NAD_kinase, 1 hit
InterProiView protein in InterPro
IPR017438 ATP-NAD_kinase_N
IPR017437 ATP-NAD_kinase_PpnK-typ_C
IPR021175 Bifunctional_PpnK_predicted
IPR020583 Inositol_monoP_metal-BS
IPR000760 Inositol_monophosphatase-like
IPR016064 NAD/diacylglycerol_kinase_sf
IPR002504 NADK
PfamiView protein in Pfam
PF00459 Inositol_P, 2 hits
PF01513 NAD_kinase, 1 hit
PIRSFiPIRSF036641 Bifunctional_PpnK_predicted, 1 hit
PRINTSiPR00377 IMPHPHTASES
SUPFAMiSSF111331 SSF111331, 1 hit
PROSITEiView protein in PROSITE
PS00629 IMP_1, 1 hit

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 nameiNPPNK_METJA
<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: Q58327
<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: May 4, 2001
Last sequence update: June 1, 1998
Last modified: December 11, 2019
This is version 120 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 programProkaryotic 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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