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Entry version 101 (12 Aug 2020)
Sequence version 1 (01 Nov 1998)
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Protein

Dolichyl-phosphooligosaccharide-protein glycotransferase 1

Gene

aglB1

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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 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

Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl2GlcAMan2GalNAc in Pyrococcus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.By similarity

<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

  • An archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.By similarity EC:2.4.99.21

<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

Mn2+By similarity, Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi57ManganeseBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei57Target acceptor peptideBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei160Important for catalytic activityBy similarity1
Metal bindingi167ManganeseBy similarity1
Metal bindingi169ManganeseBy similarity1
Binding sitei350Target acceptor peptideBy similarity1
Binding sitei420Lipid-linked oligosaccharideBy similarity1
Binding sitei518Lipid-linked oligosaccharideBy similarity1
Binding sitei576Target acceptor peptideBy similarity1

<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 functionGlycosyltransferase, Transferase
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.99.18, 5244

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

More...
UniPathwayi
UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT66, Glycosyltransferase Family 66

<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:
Dolichyl-phosphooligosaccharide-protein glycotransferase 1 (EC:2.4.99.21)
Alternative name(s):
Archaeal glycosylation protein B
Short name:
AglB-L
Short name:
AglB-Long
Oligosaccharyl transferase
Short name:
OST
Short name:
OTase
<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:aglB1
Ordered Locus Names:PH0242
<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>OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
<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 identifieri70601 [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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
<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
  • UP000000752 <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

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 21CytoplasmicCuratedAdd BLAST21
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei22 – 42HelicalSequence analysisAdd BLAST21
Topological domaini43 – 112ExtracellularCuratedAdd BLAST70
Transmembranei113 – 133HelicalSequence analysisAdd BLAST21
Topological domaini134 – 135CytoplasmicCurated2
Transmembranei136 – 156HelicalSequence analysisAdd BLAST21
Topological domaini157 – 165ExtracellularCurated9
Transmembranei166 – 186HelicalSequence analysisAdd BLAST21
Topological domaini187 – 193CytoplasmicCurated7
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21
Topological domaini215ExtracellularCurated1
Transmembranei216 – 236HelicalSequence analysisAdd BLAST21
Topological domaini237 – 247CytoplasmicCuratedAdd BLAST11
Transmembranei248 – 268HelicalSequence analysisAdd BLAST21
Topological domaini269ExtracellularCurated1
Transmembranei270 – 290HelicalSequence analysisAdd BLAST21
Topological domaini291 – 306CytoplasmicCuratedAdd BLAST16
Transmembranei307 – 327HelicalSequence analysisAdd BLAST21
Topological domaini328 – 360ExtracellularCuratedAdd BLAST33
Transmembranei361 – 381HelicalSequence analysisAdd BLAST21
Topological domaini382 – 396CytoplasmicCuratedAdd BLAST15
Transmembranei397 – 417HelicalSequence analysisAdd BLAST21
Topological domaini418ExtracellularCurated1
Transmembranei419 – 439HelicalSequence analysisAdd BLAST21
Topological domaini440 – 453CytoplasmicCuratedAdd BLAST14
Transmembranei454 – 474HelicalSequence analysisAdd BLAST21
Topological domaini475 – 976ExtracellularCuratedAdd BLAST502

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

<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_00004455921 – 976Dolichyl-phosphooligosaccharide-protein glycotransferase 1Add BLAST976

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
70601.3256631

<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

Secondary structure

1976
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O74088

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Regioni513 – 515Target acceptor peptide bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi55 – 57DXD motif 1By similarity3
Motifi167 – 169DXD motif 2By similarity3
Motifi347 – 350TIXE motifBy similarity4
Motifi513 – 517WWDYG motifBy similarity5
Motifi573 – 580DK motifBy similarity8

<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

Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.By similarity

<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 STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG02044, Archaea

KEGG Orthology (KO)

More...
KOi
K21306

Identification of Orthologs from Complete Genome Data

More...
OMAi
GYWIESS

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003674, Oligo_trans_STT3
IPR041530, OST_IS
IPR041152, OST_P2

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18246, OST_IS, 1 hit
PF18235, OST_P2, 1 hit
PF02516, STT3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

O74088-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVKSKVKKVE KGKEGEEKRS TYVLLKKVLI PILVFGFAIY AFYLRHLTAG
60 70 80 90 100
KYFPDPDTFY HFEIYKLVLK EGLPRYYPMS DAPFGSLIGE PLGLYLLPAA
110 120 130 140 150
FYKVVSLFGY NELQAFLLWP PFVGFLGVIA VYLLGRKVLN EWTGLWGAVV
160 170 180 190 200
LTVSTANFSR TFSGNARGDG PFMALFIFAS VAMLYYLKES NKTRKIIYGT
210 220 230 240 250
LFVLLTVISL GAWNGSPFGL MVLLGFASLQ TIILFIFGKL EELKKFVKEF
260 270 280 290 300
YPAYLAILAF GYALTFPGIV KIGGFIRFAF EVFLGLIFLL VIMLYGGRYL
310 320 330 340 350
NYSDKKHRFL VVTIIVLLGF GGAYAYVGPK LFRLMGGAYQ STQVYETVQE
360 370 380 390 400
LAKTTIGDVK AYYGVESGNG LIFFLSIPGL LILLTKYLYD LFKKAKSDNE
410 420 430 440 450
TLFALVFYTM SLYLLYLAVR FLFLASYAVA LFFGIFIGFS MDVIEKMKEN
460 470 480 490 500
IGIKAALGIV LSLMILVIPF VHAPVLARSA RALKNTEIEV TGWEQALKWL
510 520 530 540 550
RSNTSKYATA TSWWDYGYWI ESSLLGNRRA SADGGHARDR DHILALFLAR
560 570 580 590 600
DGNISEVDFE SWELNYFIIY LNDWAKFNAI SYLGGAITRK EYNGDENGRG
610 620 630 640 650
RVTTILLTQA AGNVYVNPYA RIVIKVIQQN KTRRIAVNIG QLECSPILSV
660 670 680 690 700
AFPGNIKIKG SGRCSDGSPF PYVVYLTPSL GVLAYYKVAT SNFVKLAFGI
710 720 730 740 750
PTSSYSEFAE KLFSNFIPVY QYGSVIVYEF RPFAIYKIED FINGTWREVG
760 770 780 790 800
KLSPGKHTLR LYISAFGRDI KNATLYVYAL NGTKIIKRIK VGEIKYMNHL
810 820 830 840 850
EEYPIIVNVT LPTAQKYRFI LAQKGPVGVL TGPVRVNGKI TNPAYIMREG
860 870 880 890 900
ESGRLELKVG VDKEYTADLY LRATFIYLVR KGGKSNEDYD ASFEPHMDTF
910 920 930 940 950
FITKLKEGIK LRPGENEIVV NAEMPKNAIS SYKEKLEKEH GDKLIIRGIR
960 970
VEPVFIVEKE YTMIEVSASA PHHSSE
Length:976
Mass (Da):109,970
Last modified:November 1, 1998 - 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:iBF5FB82FBADC60A9
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
BA000001 Genomic DNA Translation: BAA29314.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C71248

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAA29314; BAA29314; BAA29314

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pho:PH0242

<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
BA000001 Genomic DNA Translation: BAA29314.1
PIRiC71248

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VU1X-ray2.70A/B482-976[»]
SMRiO74088
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi70601.3256631

Protein family/group databases

CAZyiGT66, Glycosyltransferase Family 66

Genome annotation databases

EnsemblBacteriaiBAA29314; BAA29314; BAA29314
KEGGipho:PH0242

Phylogenomic databases

eggNOGiarCOG02044, Archaea
KOiK21306
OMAiGYWIESS

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.99.18, 5244

Family and domain databases

InterProiView protein in InterPro
IPR003674, Oligo_trans_STT3
IPR041530, OST_IS
IPR041152, OST_P2
PfamiView protein in Pfam
PF18246, OST_IS, 1 hit
PF18235, OST_P2, 1 hit
PF02516, STT3, 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 nameiAGLB1_PYRHO
<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: O74088
<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 10, 2018
Last sequence update: November 1, 1998
Last modified: August 12, 2020
This is version 101 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 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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