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Protein

Tail spike protein

Gene
N/A
Organism
Enterobacteria phage K1F (Bacteriophage K1F)
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

Tail spike protein: Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.2 Publications
C-terminal chaperone protein: The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.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 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

  1. KM=71 µM for poly-alpha-2,8-sialosyl carbohydrates1 Publication
  2. KM=1.2 mM for oligo-alpha-2,8-sialosyl carbohydrates1 Publication
  3. KM=7.1 µM for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates1 Publication
  1. Vmax=19 µmol/min/mg enzyme for poly-alpha-2,8-sialosyl carbohydrates cleavage1 Publication
  2. Vmax=18 µmol/min/mg enzyme for oligo-alpha-2,8-sialosyl carbohydrates cleavage1 Publication
  3. Vmax=13 µmol/min/mg enzyme for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei542Binding to sialic acid1 Publication1
Sitei545Binding to sialic acid1 Publication1
Sitei549Binding to sialic acid1 Publication1
Sitei578Binding to sialic acid1 Publication1
<p>This subsection of the ‘Function’ 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 sitei5812 Publications1
Active sitei5961 Publication1
Sitei598Binding to sialic acid1 Publication1
Sitei599Binding to sialic acid1 Publication1
Active sitei6472 Publications1

<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

  • endo-alpha-(2,8)-sialidase activity Source: UniProtKB
  • identical protein binding Source: IntAct

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 functionGlycosidase, Hydrolase
Biological processDegradation of host capsule during virus entry, Degradation of host cell envelope components during virus entry, Host-virus interaction, Viral attachment to host adhesion receptor, Viral attachment to host cell, Virus entry into host cell

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.129 716

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH58 Glycoside Hydrolase Family 58

MEROPS protease database

More...
MEROPSi
S74.001

<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:
Tail spike proteinCurated
Short name:
TSP
Alternative name(s):
Endo-N-acetylneuraminidase (EC:3.2.1.1293 Publications)
Short name:
Endo-N
Endo-alpha-sialidaseCurated
EndoNF
G102
Cleaved into the following chain:
<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>OrganismiEnterobacteria phage K1F (Bacteriophage K1F)
<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 identifieri344021 [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 lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7virus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiEscherichia coli [TaxID: 562]
<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
  • UP000001530 <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: Genome
  • UP000001722 Componenti: Genome

<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

Tail spike protein :

GO - Cellular componenti

Keywords - Cellular componenti

Viral tail fiber protein, Viral tail protein, Virion

<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

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>Mutagenesisi328W → R: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi350H → A, N or Q: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi410K → A: 80% loss of enzymatic activity. 1 Publication1
Mutagenesisi542H → A: 60% loss of enzymatic activity. 1 Publication1
Mutagenesisi549R → A: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi581E → A: Almost complete loss of enzymatic activity. 2 Publications1
Mutagenesisi596R → A: Complete loss of enzymatic activity; when associated with A-581. Complete loss of enzymatic activity; when associated with A-647. 1 Publication1
Mutagenesisi647R → A: Almost complete loss of enzymatic activity. 2 Publications1
Mutagenesisi911S → A: Complete loss of proteolytic processing. 190-fold reduced enzymatic activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03721 N-acetyl-alpha-neuraminic acid
DB04265 N-acetyl-beta-neuraminic acid

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by host1 Publication
<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_00000577092 – 1064Tail spike proteinAdd BLAST1063
ChainiPRO_0000438182912 – 1064C-terminal chaperone protein1 PublicationAdd BLAST153

<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

Proteolytic cleavage and release of the chaperone stabilizes the folded protein.2 Publications

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q04830

<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

Tail spike protein: Homotrimer (PubMed:3546309, PubMed:20124697). Interacts with sialic acid (PubMed:15608653, PubMed:20096705).4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-15829658,EBI-15829658

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-48774N

<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

11064
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q04830

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

More...
SMRi
Q04830

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q04830

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati360 – 371BNR 1Add BLAST12
Repeati496 – 503BNR 28
Repeati608 – 619BNR 3Add BLAST12
<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>Domaini911 – 1064Peptidase S74PROSITE-ProRule annotationAdd BLAST154

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi198 – 216Gly-rich (hinge)Add BLAST19

<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 glycosyl hydrolase 58 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

Database of Orthologous Groups

More...
OrthoDBi
VOG09000089

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.30.20, 1 hit
3.30.750.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023366 ATP_synth_asu-like_sf
IPR024428 Endosialidase_beta_prop
IPR024430 Endosialidase_C_dom
IPR024429 Endosialidase_N-extension
IPR037142 Endosialidase_N-extension_sf
IPR001724 Glycl_Hydrolase_58
IPR005604 Phage_T7_tail_fibre
IPR030392 S74_ICA
IPR036278 Sialidase_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12217 End_beta_propel, 1 hit
PF12218 End_N_terminal, 1 hit
PF12219 End_tail_spike, 1 hit
PF13884 Peptidase_S74, 1 hit
PF03906 Phage_T7_tail, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00849 GLHYDRLASE58

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50939 SSF50939, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51688 ICA, 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>.<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q04830-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF
60 70 80 90 100
LNPTMIEMLV DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA
110 120 130 140 150
IHIAEEGRDQ TVDLAKEYAD AAGSSAGNAK DSEDEARRIA ESIRAAGLIG
160 170 180 190 200
YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR WDGTLPKNVP AGSTPETSGG
210 220 230 240 250
IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD ARGWGAKGDG
260 270 280 290 300
VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP
310 320 330 340 350
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH
360 370 380 390 400
GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF
410 420 430 440 450
AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG
460 470 480 490 500
LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN
510 520 530 540 550
WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG YHQGDVAPRE
560 570 580 590 600
VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG
610 620 630 640 650
DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN
660 670 680 690 700
EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS
710 720 730 740 750
GVGVGSVVVK DNYIYYMFGG EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY
760 770 780 790 800
KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT NGVRTVPAPM EFTGDLGLGH
810 820 830 840 850
VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF CGGEGTSSTT
860 870 880 890 900
GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT
910 920 930 940 950
AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND
960 970 980 990 1000
ARIHFGVIAQ QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN
1010 1020 1030 1040 1050
EIVEHTDEEG NVTTTEEPVY TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK
1060
LERIEARLSA LEQK
Length:1,064
Mass (Da):118,905
Last modified:November 2, 2016 - v4
<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:i82FAB75EDC68DAB6
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC37340 differs from that shown. Reason: Frameshift at position 914.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti628H → R in AAC37340 (PubMed:8331067).Curated1

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
M63657 Unassigned DNA Translation: AAC37340.1 Frameshift.
AJ505988 Genomic DNA Translation: CAD44528.2
DQ111067 Genomic DNA Translation: AAZ73001.1
AM084414 Genomic DNA Translation: CAJ29390.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A36887

NCBI Reference Sequences

More...
RefSeqi
YP_338127.1, NC_007456.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3707741

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:3707741

<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
M63657 Unassigned DNA Translation: AAC37340.1 Frameshift.
AJ505988 Genomic DNA Translation: CAD44528.2
DQ111067 Genomic DNA Translation: AAZ73001.1
AM084414 Genomic DNA Translation: CAJ29390.1
PIRiA36887
RefSeqiYP_338127.1, NC_007456.1

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
1V0EX-ray1.90A/B/C/D/E/F246-910[»]
1V0FX-ray2.55A/B/C/D/E/F246-910[»]
3GVJX-ray1.48A246-910[»]
3GVKX-ray1.84A/B/C246-910[»]
3GVLX-ray1.41A246-910[»]
3GW6X-ray2.60A/B/C/D/E/F790-1064[»]
3JU4X-ray0.98A246-910[»]
ProteinModelPortaliQ04830
SMRiQ04830
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48774N

Chemistry databases

DrugBankiDB03721 N-acetyl-alpha-neuraminic acid
DB04265 N-acetyl-beta-neuraminic acid

Protein family/group databases

CAZyiGH58 Glycoside Hydrolase Family 58
MEROPSiS74.001

Proteomic databases

PRIDEiQ04830

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3707741
KEGGivg:3707741

Phylogenomic databases

OrthoDBiVOG09000089

Enzyme and pathway databases

BRENDAi3.2.1.129 716

Miscellaneous databases

EvolutionaryTraceiQ04830

Family and domain databases

Gene3Di2.40.30.20, 1 hit
3.30.750.60, 1 hit
InterProiView protein in InterPro
IPR023366 ATP_synth_asu-like_sf
IPR024428 Endosialidase_beta_prop
IPR024430 Endosialidase_C_dom
IPR024429 Endosialidase_N-extension
IPR037142 Endosialidase_N-extension_sf
IPR001724 Glycl_Hydrolase_58
IPR005604 Phage_T7_tail_fibre
IPR030392 S74_ICA
IPR036278 Sialidase_sf
PfamiView protein in Pfam
PF12217 End_beta_propel, 1 hit
PF12218 End_N_terminal, 1 hit
PF12219 End_tail_spike, 1 hit
PF13884 Peptidase_S74, 1 hit
PF03906 Phage_T7_tail, 1 hit
PRINTSiPR00849 GLHYDRLASE58
SUPFAMiSSF50939 SSF50939, 1 hit
PROSITEiView protein in PROSITE
PS51688 ICA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiFIBER_BPK1F
<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: Q04830
Secondary accession number(s): Q2WC71, Q858B1
<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: February 1, 1995
Last sequence update: November 2, 2016
Last modified: December 5, 2018
This is version 103 of the entry and version 4 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 programViral 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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