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Entry version 35 (12 Aug 2020)
Sequence version 2 (16 Oct 2019)
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Protein

Bifunctional sulfatase/alpha-L-rhamnosidase

Gene

BN863_22250

Organism
Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901)
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

Bifunctional enzyme containing sulfatase and alpha-L-rhamnosidase activities involved in ulvan degradation (PubMed:31285597). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). The sulfatase specifically desulfates L-rhamnose at the 3-position and can act on the motif Rha3S-Xyl-Rha3S in an exolytic mode of action, producing Rha-Xyl-Rha3S. Also desulfates Rha3S monosaccharides, which are produced by the action of unsaturated glucuronyl hydrolases acting on ulvan oligomers (PubMed:31285597).1 Publication1 Publication

<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

  • Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides.By similarity EC:3.2.1.40

<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

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.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 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 bindingi38Calcium1 Publication1
Metal bindingi39Calcium1 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 sitei78Nucleophile; for sulfatase activityBy similarity1
Metal bindingi78Calcium; via 3-oxoalanineBy similarity1
Metal bindingi304Calcium1 Publication1
Metal bindingi305Calcium1 Publication1
Active sitei766Proton donor; for alpha-L-rhamnosidase activityBy similarity1
Active sitei1044Proton acceptor; for alpha-L-rhamnosidase activityBy 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 sitei1058L-rhamnoseBy 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

<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
LigandCalcium, Metal-binding

<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:
Bifunctional sulfatase/alpha-L-rhamnosidaseCurated
Alternative name(s):
P36_GH78/S1_251 Publication
Including the following 2 domains:
Ulvan-active sulfatase (EC:3.1.6.-1 Publication)
Alternative name(s):
Sulfatase family S1 subfamily 25 protein P36Curated
Short name:
P36_S1_251 Publication
Alpha-L-rhamnosidase (EC:3.2.1.40By similarity)
Alternative name(s):
Glycosyl hydrolase 78 family protein P36Curated
Short name:
P36_GH781 Publication
Polysaccharide utilization locus H protein P361 Publication
Short name:
PUL H protein P36
<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
ORF Names:BN863_22250
<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>OrganismiFormosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901)
<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 identifieri1347342 [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 lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFormosa
<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
  • UP000016160 <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

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<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 – 22Sequence analysisAdd BLAST22
<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_000044833923 – 1174Bifunctional sulfatase/alpha-L-rhamnosidaseAdd BLAST1152

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei783-oxoalanine (Cys)By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD).By similarity

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By ulvan and rhamnose.1 Publication

<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
1347342.BN863_22250

<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

11174
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
T2KM26

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>Regioni22 – 568Ulvan-active sulfataseAdd BLAST547
Regioni569 – 1174Alpha-L-rhamnosidaseAdd BLAST606
Regioni764 – 766L-rhamnose bindingBy similarity3

<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 sulfatase family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 78 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3119, Bacteria
COG3408, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_270303_0_0_10

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 1 hit
3.40.720.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008928, 6-hairpin_glycosidase_sf
IPR012341, 6hp_glycosidase-like_sf
IPR017850, Alkaline_phosphatase_core_sf
IPR035396, Bac_rhamnosid6H
IPR035398, Bac_rhamnosid_C
IPR032506, DUF4976
IPR008979, Galactose-bd-like_sf
IPR013783, Ig-like_fold
IPR008902, Rhamnosid_concanavalin
IPR000917, Sulfatase_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05592, Bac_rhamnosid, 1 hit
PF17389, Bac_rhamnosid6H, 1 hit
PF17390, Bac_rhamnosid_C, 1 hit
PF16347, DUF4976, 1 hit
PF00884, Sulfatase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48208, SSF48208, 1 hit
SSF53649, SSF53649, 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.

T2KM26-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIKYKAIINL VFIAVFFNNA MSQTVKKEKP NIIFILTDDQ RFDAIGYAGN
60 70 80 90 100
KFVNTPEMDK LAQQGTYFDH AIVTTPICAA SRASLWTGLH ERSHNFNFQT
110 120 130 140 150
GNVREEYMNN AYPKLLKNNG YYTGFYGKYG VRYDNLESQF DEFESYDRNN
160 170 180 190 200
RYKDKRGYYY KTINNDTVHL TRYTGQQAID FIDKNATNTQ PFMLSLSFSA
210 220 230 240 250
PHAHDGAPEQ YFWQTTTDAL LQDTTLPGPD LADEKYFLAQ PQAVRDGFNR
260 270 280 290 300
LRWTWRYDDP EKYQHSLKGY YRMISGIDLE IKKIRDKLKE KGVDKNTVII
310 320 330 340 350
VMGDNGYFLG ERQLAGKWLM YDNSIRVPLI VFDPRVNKHQ DISEMVLNID
360 370 380 390 400
VTQTIADLAG VKAPESWQGK SLLPLVKQET STISRDTILI EHLWDFENIP
410 420 430 440 450
PSEGVRTEEW KYFRYVNDKT IEELYNIKKD PKEINNLIGK KKYQNVAKAL
460 470 480 490 500
REKLDELIAK NSDEFRAGPS DLTVELIRQP ESEVKIFDLK PEFGWTVPLS
510 520 530 540 550
SKYQSAYQLL VASSETIINA NNGDVWDSGQ VRSSQSTNVD FGGKPLKIGE
560 570 580 590 600
TYYWKVRIWD EENRLVDYSK AQKFTIGESD NYIISTENKF VTDKIKPSKF
610 620 630 640 650
ENRDGVYFID FGKAAFATME FNYQAKTPHT LTIRVGEMID ENGNVNRTPP
660 670 680 690 700
AKSNIRYQEL KVEVKPGQTR YRIPIQTDER NTRPNKAIPL PKGFPPLLPF
710 720 730 740 750
RYAEIEGAQS SINANDVEQL AYHTFWDEKA SSFKSDNNIL NQVWDLSKYS
760 770 780 790 800
IKATTFNGLY VDGDRERIPY EADAYLNQLS HYTTDREYAM ARRTIEYFMK
810 820 830 840 850
NPTWPTEWQQ HVALLLYADY MYTGNTELVE RYYEALKHKS LYELSNEDGL
860 870 880 890 900
ITSTKVDAEF MKKLGFPEGY KKPLTDIVDW PGANFNGSKT PGERDGFVFQ
910 920 930 940 950
PYNTVINSFF YENMKIMAQF AKILGKTDEV LDFELRAAKA KKAVNEQMFD
960 970 980 990 1000
KKRGIYVDGI GTDHASLHAN MMPLAFGLVP QEHVDTVVEF VKSRGMACSV
1010 1020 1030 1040 1050
YGAQFLLDGL YNVGEADYAL DLLASTSERS WYNMIRIGST ITLEAWDNKY
1060 1070 1080 1090 1100
KNNLDWNHAW GAVPANAIPR GLWGIKPKTA GFGIASIKPQ MGKLKSSQIT
1110 1120 1130 1140 1150
VPTVRGAIHA TFTHNGPRSQ TYEIEIPGNM VAEFSLDDID GKDLIHNGQK
1160 1170
VPAAFGAVQL SPGKHIIELK INSF
Length:1,174
Mass (Da):134,503
Last modified:October 16, 2019 - 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:iAF4C49970929AB52
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 CDF79937 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.1 Publication

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
HG315671 Genomic DNA Translation: CDF79937.1 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
WP_038530548.1, NZ_HG315671.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CDF79937; CDF79937; BN863_22250

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1347342.6.peg.2232

<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
HG315671 Genomic DNA Translation: CDF79937.1 Different initiation.
RefSeqiWP_038530548.1, NZ_HG315671.1

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
6HR5X-ray2.91A28-463[»]
SMRiT2KM26
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1347342.BN863_22250

Genome annotation databases

EnsemblBacteriaiCDF79937; CDF79937; BN863_22250
PATRICifig|1347342.6.peg.2232

Phylogenomic databases

eggNOGiCOG3119, Bacteria
COG3408, Bacteria
HOGENOMiCLU_270303_0_0_10

Family and domain databases

Gene3Di1.50.10.10, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 1 hit
3.40.720.10, 1 hit
InterProiView protein in InterPro
IPR008928, 6-hairpin_glycosidase_sf
IPR012341, 6hp_glycosidase-like_sf
IPR017850, Alkaline_phosphatase_core_sf
IPR035396, Bac_rhamnosid6H
IPR035398, Bac_rhamnosid_C
IPR032506, DUF4976
IPR008979, Galactose-bd-like_sf
IPR013783, Ig-like_fold
IPR008902, Rhamnosid_concanavalin
IPR000917, Sulfatase_N
PfamiView protein in Pfam
PF05592, Bac_rhamnosid, 1 hit
PF17389, Bac_rhamnosid6H, 1 hit
PF17390, Bac_rhamnosid_C, 1 hit
PF16347, DUF4976, 1 hit
PF00884, Sulfatase, 1 hit
SUPFAMiSSF48208, SSF48208, 1 hit
SSF53649, SSF53649, 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 nameiPLH36_FORAG
<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: T2KM26
<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 16, 2019
Last sequence update: October 16, 2019
Last modified: August 12, 2020
This is version 35 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

3D-structure, Reference proteome

Documents

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