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Entry version 111 (23 Feb 2022)
Sequence version 1 (05 Sep 2006)
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Protein

O-GlcNAcase NagJ

Gene

nagJ

Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
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

Binds carbohydrates (PubMed:16990278).

Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.

3 Publications

Miscellaneous

Metal-binding observed in X-ray crystal structures is artifactual.Curated

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Inhibited by O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) and streptozotocin.2 Publications

<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=2.9 µM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide (4MU-NAG)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei187Substrate; via carbonyl oxygen1 Publication1
Binding sitei218Substrate1 Publication1
Binding sitei297Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei298Proton donor1 Publication1
Binding sitei335Substrate1 Publication1
Binding sitei401Substrate1 Publication1
Binding sitei429Substrate1 Publication1

<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 functionGlycosidase, Hydrolase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.169, 1503

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q0TR53

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM32, Carbohydrate-Binding Module Family 32
GH84, Glycoside Hydrolase Family 84

<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:
O-GlcNAcase NagJ (EC:3.2.1.1693 Publications)
Alternative name(s):
Beta-N-acetylglucosaminidase
Beta-N-acetylhexosaminidase
Beta-hexosaminidase
GH84C1 Publication
Hexosaminidase B
N-acetyl-beta-D-glucosaminidase
<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:nagJ
Ordered Locus Names:CPF_1442
<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>OrganismiClostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
<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 identifieri195103 [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 lineageiBacteriaFirmicutesClostridiaEubacterialesClostridiaceaeClostridium
<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
  • UP000001823 <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 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi297D → A: 99% decrease in activity for 4MU-NAG. 1 Publication1
Mutagenesisi298D → N: 99% decrease in activity for 4MU-NAG. 2 Publications1
Mutagenesisi335Y → F: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication1
Mutagenesisi390N → A: No change in activity for 4MU-NAG. 1 Publication1
Mutagenesisi396N → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication1
Mutagenesisi401D → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication1
Mutagenesisi490W → A: Strongly decreases affinity for 4MU-NAG. 97% decrease in activity for 4MU-NAG. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 30Sequence analysisAdd BLAST30
<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_000025798531 – 1001O-GlcNAcase NagJAdd BLAST971

<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
195103.CPF_1442

<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

11001
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q0TR53

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

More...
SMRi
Q0TR53

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q0TR53

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini916 – 1001Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST86

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>Regioni179 – 469Catalytic domainSequence analysisAdd BLAST291
Regioni394 – 396Substrate binding1 Publication3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili515 – 543Sequence analysisAdd BLAST29
Coiled coili573 – 597Sequence analysisAdd BLAST25

<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 84 family.Sequence analysis

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3291, Bacteria
COG3525, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001501_2_0_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
ARMEEAC

Database of Orthologous Groups

More...
OrthoDBi
1158117at2

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063, FN3, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
3.30.379.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011496, Beta-N-acetylglucosaminidase
IPR008965, CBM2/CBM3_carb-bd_dom_sf
IPR002102, Cohesin_dom
IPR000421, FA58C
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR017853, Glycoside_hydrolase_SF
IPR029018, Hex-like_dom2
IPR015882, HEX_bac_N
IPR013783, Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00963, Cohesin, 1 hit
PF00754, F5_F8_type_C, 1 hit
PF00041, fn3, 1 hit
PF02838, Glyco_hydro_20b, 1 hit
PF07555, NAGidase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00060, FN3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265, SSF49265, 1 hit
SSF49384, SSF49384, 1 hit
SSF49785, SSF49785, 1 hit
SSF51445, SSF51445, 1 hit
SSF55545, SSF55545, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853, FN3, 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.

<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 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.

Q0TR53-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP
60 70 80 90 100
ENLEVVGDGF KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN
110 120 130 140 150
STTLIIGEVD DDIPELDEAL NGTTAENLKE EGYALVSNDG KIAIEGKDGD
160 170 180 190 200
GTFYGVQTFK QLVKESNIPE VNITDYPTVS ARGIVEGFYG TPWTHQDRLD
210 220 230 240 250
QIKFYGENKL NTYIYAPKDD PYHREKWREP YPESEMQRMQ ELINASAENK
260 270 280 290 300
VDFVFGISPG IDIRFDGDAG EEDFNHLITK AESLYDMGVR SFAIYWDDIQ
310 320 330 340 350
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRAYT
360 370 380 390 400
RIFAETVDPS IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT
410 420 430 440 450
DYFKGKLALG PMHGLDKGLN QYVDFFTVNP MEHAELSKIS IHTAADYSWN
460 470 480 490 500
MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN HSTRMDNKTW AKSGREDAPE
510 520 530 540 550
LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK ANLPEVALEE
560 570 580 590 600
CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS
610 620 630 640 650
FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD
660 670 680 690 700
GDMNTFWHSK WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG
710 720 730 740 750
YKVSVSLDGE NFTEVKTGTL EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ
760 770 780 790 800
ANGRGKFATA AEVNVHGKLK ENAEVTGSVS LEALEEVQVG ENLEVGVGID
810 820 830 840 850
ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE DGKVRVLVSS
860 870 880 890 900
LTGEPLPAKE VLAKVVLRAE AKAEGSNLSV TNSSVGDGEG LVHEIAGTEK
910 920 930 940 950
TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK
960 970 980 990 1000
DGKKVAEIGK DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA

R
Length:1,001
Mass (Da):111,080
Last modified:September 5, 2006 - 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:i3B918C7DB544A2DC
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
CP000246 Genomic DNA Translation: ABG84519.1

NCBI Reference Sequences

More...
RefSeqi
WP_003456570.1, NC_008261.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABG84519; ABG84519; CPF_1442

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29571445

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cpf:CPF_1442

<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
CP000246 Genomic DNA Translation: ABG84519.1
RefSeqiWP_003456570.1, NC_008261.1

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
2CBIX-ray2.25A/B31-624[»]
2CBJX-ray2.35A/B31-624[»]
2J1AX-ray1.49A625-767[»]
2J1EX-ray2.40A625-767[»]
2J62X-ray2.26A/B31-624[»]
2J7MX-ray2.30A625-767[»]
2JH2X-ray2.50A/B/C768-909[»]
2O4ENMR-A768-909[»]
2OZNX-ray1.60A768-909[»]
2V5CX-ray2.10A/B31-624[»]
2V5DX-ray3.30A31-767[»]
2VURX-ray2.20A/B31-624[»]
2W1NX-ray1.80A765-1001[»]
2WB5X-ray2.31A/B31-624[»]
2X0YX-ray2.25A/B31-624[»]
2XPKX-ray2.40A/B31-624[»]
2YDQX-ray2.60A31-618[»]
2YDRX-ray2.75A31-618[»]
2YDSX-ray2.55A31-618[»]
4ZXLX-ray2.60A39-617[»]
5OXDX-ray2.60A31-618[»]
6RHEX-ray3.10A31-619[»]
7KHVX-ray2.30A/B/C/D/E/F31-624[»]
BMRBiQ0TR53
SMRiQ0TR53
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi195103.CPF_1442

Protein family/group databases

CAZyiCBM32, Carbohydrate-Binding Module Family 32
GH84, Glycoside Hydrolase Family 84

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4202790

Genome annotation databases

EnsemblBacteriaiABG84519; ABG84519; CPF_1442
GeneIDi29571445
KEGGicpf:CPF_1442

Phylogenomic databases

eggNOGiCOG3291, Bacteria
COG3525, Bacteria
HOGENOMiCLU_001501_2_0_9
OMAiARMEEAC
OrthoDBi1158117at2

Enzyme and pathway databases

BRENDAi3.2.1.169, 1503
SABIO-RKiQ0TR53

Miscellaneous databases

EvolutionaryTraceiQ0TR53

Family and domain databases

CDDicd00063, FN3, 1 hit
Gene3Di2.60.40.10, 1 hit
3.30.379.10, 1 hit
InterProiView protein in InterPro
IPR011496, Beta-N-acetylglucosaminidase
IPR008965, CBM2/CBM3_carb-bd_dom_sf
IPR002102, Cohesin_dom
IPR000421, FA58C
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR017853, Glycoside_hydrolase_SF
IPR029018, Hex-like_dom2
IPR015882, HEX_bac_N
IPR013783, Ig-like_fold
PfamiView protein in Pfam
PF00963, Cohesin, 1 hit
PF00754, F5_F8_type_C, 1 hit
PF00041, fn3, 1 hit
PF02838, Glyco_hydro_20b, 1 hit
PF07555, NAGidase, 1 hit
SMARTiView protein in SMART
SM00060, FN3, 1 hit
SUPFAMiSSF49265, SSF49265, 1 hit
SSF49384, SSF49384, 1 hit
SSF49785, SSF49785, 1 hit
SSF51445, SSF51445, 1 hit
SSF55545, SSF55545, 1 hit
PROSITEiView protein in PROSITE
PS50853, FN3, 1 hit

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 nameiOGA_CLOP1
<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: Q0TR53
<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 31, 2006
Last sequence update: September 5, 2006
Last modified: February 23, 2022
This is version 111 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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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