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Entry version 99 (18 Sep 2019)
Sequence version 1 (30 May 2006)
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Protein

Receptor kinase-like protein Xa21

Gene

XA21

Organism
Oryza sativa subsp. indica (Rice)
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

Receptor kinase-like protein Xa21: Receptor kinase that detects X.oryzae pv. oryzae protein Ax21 to promote innate immunity (PubMed:20118235). Following X.oryzae pv. oryzae protein Ax21 detection, undergoes cleavage, releasing the processed protein kinase Xa21 chain (By similarity).By similarity1 Publication
Receptor kinase-like protein Xa21, processed: The processed protein kinase Xa21 chain released by protein cleavage after X.oryzae pv. oryzae protein Ax21 detection translocates into the nucleus where it can bind and regulate WRKY62, a transcription factor (By similarity). Confers resistance to the bacterial pathogen X.oryzae pv. oryzae (Xoo) (PubMed:8525370, PubMed:19825552, PubMed:20118235).By similarity3 Publications

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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+1 Publication, Mg2+1 PublicationNote: Enzymatic activity is fifteen time stronger with Mn2+ than with Mg2+.1 Publication

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

  1. KM=0.3 µM for ATP1 Publication
  1. Vmax=8.4 nmol/min/mg enzyme with ATP as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei736ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei842Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi714 – 722ATPPROSITE-ProRule annotation9

<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 functionKinase, Receptor, Serine/threonine-protein kinase, Transferase
Biological processPlant defense
LigandATP-binding, Nucleotide-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_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:
Receptor kinase-like protein Xa211 Publication (EC:2.7.11.1PROSITE-ProRule annotation1 Publication)
Cleaved into the following chain:
Receptor kinase-like protein Xa21, processedBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:XA211 Publication
<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>OrganismiOryza sativa subsp. indica (Rice)Imported
<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 identifieri39946 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryzaOryza sativa

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 domaini24 – 653ExtracellularCuratedAdd BLAST630
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei654 – 674HelicalSequence analysisAdd BLAST21
Topological domaini675 – 1025CytoplasmicCuratedAdd BLAST351

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Nucleus

<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>Mutagenesisi680T → A: Increased autophosphorylation. 1 Publication1
Mutagenesisi686 – 689SRTS → ARAA: Normal autophosphorylation but reduced stability leading to increased proteolytic cleavage and compromised resistance to X.oryzae pv. oryzae (Xoo). 2 Publications4
Mutagenesisi697S → A or D: Slight reduction in autophosphorylation. 1 Publication1
Mutagenesisi699S → A: Increased autophosphorylation. 1 Publication1
Mutagenesisi705T → A or E: Abolished autophosphorylation and loss of interactions with target proteins (e.g. WRKY62/XB10, XB3, XB15 and XB24). Loss of positive impact on innate immunity toward X.oryzae pv. oryzae (Xoo). 1 Publication1
Mutagenesisi736K → E: Kinase-deficient mutant lacking autophosphorylation, impaired interaction with WRKY62. Reduced stability leading to increased proteolytic cleavage. 4 Publications1

<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 – 23Sequence analysisAdd BLAST23
<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_500593076124 – 1025Receptor kinase-like protein Xa21Add BLAST1002
ChainiPRO_0000436963? – 1025Receptor kinase-like protein Xa21, processed

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi55N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi90N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi101N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi198N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi235N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi246N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi295N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi322N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi349N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi373N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi435N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi446N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi470N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi483N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi503N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi580N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi599N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 residuei686Phosphoserine; by autocatalysis1 Publication1
Modified residuei688Phosphothreonine; by autocatalysis1 Publication1
Modified residuei689Phosphoserine; by autocatalysis1 Publication1
Modified residuei705Phosphothreonine; by autocatalysis1 Publication1

<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

Undergoes protein cleavage upon X.oryzae pv. oryzae protein Ax21 detection, thus releasing the processed protein kinase Xa21 chain.By similarity
Autophosphorylated on serine and threonine residues; these phosphorylation prevents proteolytic degradation.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q1MX30

<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

Binds to XB3, XB15 and XB24 (PubMed:20118235). Receptor kinase-like protein Xa21, processed:

Interacts with WRKY62/XB10 in the nucleus (PubMed:19825552, PubMed:20118235).

2 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...
SMRi
Q1MX30

Database of comparative protein structure models

More...
ModBasei
Search...

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

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>Repeati78 – 101LRR 1Sequence analysisAdd BLAST24
Repeati102 – 126LRR 2Sequence analysisAdd BLAST25
Repeati127 – 150LRR 3Sequence analysisAdd BLAST24
Repeati152 – 174LRR 4Sequence analysisAdd BLAST23
Repeati176 – 199LRR 5Sequence analysisAdd BLAST24
Repeati200 – 223LRR 6Sequence analysisAdd BLAST24
Repeati224 – 247LRR 7Sequence analysisAdd BLAST24
Repeati248 – 271LRR 8Sequence analysisAdd BLAST24
Repeati273 – 296LRR 9Sequence analysisAdd BLAST24
Repeati298 – 319LRR 10Sequence analysisAdd BLAST22
Repeati320 – 343LRR 11Sequence analysisAdd BLAST24
Repeati350 – 373LRR 12Sequence analysisAdd BLAST24
Repeati375 – 399LRR 13Sequence analysisAdd BLAST25
Repeati400 – 423LRR 14Sequence analysisAdd BLAST24
Repeati425 – 447LRR 15Sequence analysisAdd BLAST23
Repeati448 – 470LRR 16Sequence analysisAdd BLAST23
Repeati471 – 495LRR 17Sequence analysisAdd BLAST25
Repeati497 – 520LRR 18Sequence analysisAdd BLAST24
Repeati521 – 544LRR 19Sequence analysisAdd BLAST24
Repeati545 – 568LRR 20Sequence analysisAdd BLAST24
Repeati569 – 592LRR 21Sequence analysisAdd BLAST24
Repeati594 – 617LRR 22Sequence analysisAdd BLAST24
<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>Domaini708 – 979Protein kinasePROSITE-ProRule annotationAdd BLAST272

<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 protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.10.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR013210 LRR_N_plant-typ
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00560 LRR_1, 1 hit
PF13855 LRR_8, 3 hits
PF08263 LRRNT_2, 1 hit
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00369 LRR_TYP, 12 hits
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

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

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

<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.

Q1MX30-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MISLPLLLFV LLFSALLLCP SSSDDDGDAA GDELALLSFK SSLLYQGGQS
60 70 80 90 100
LASWNTSGHG QHCTWVGVVC GRRRRRHPHR VVKLLLRSSN LSGIISPSLG
110 120 130 140 150
NLSFLRELDL GDNYLSGEIP PELSRLSRLQ LLELSDNSIQ GSIPAAIGAC
160 170 180 190 200
TKLTSLDLSH NQLRGMIPRE IGASLKHLSN LYLYKNGLSG EIPSALGNLT
210 220 230 240 250
SLQEFDLSFN RLSGAIPSSL GQLSSLLTMN LGQNNLSGMI PNSIWNLSSL
260 270 280 290 300
RAFSVRENKL GGMIPTNAFK TLHLLEVIDM GTNRFHGKIP ASVANASHLT
310 320 330 340 350
VIQIYGNLFS GIITSGFGRL RNLTELYLWR NLFQTREQDD WGFISDLTNC
360 370 380 390 400
SKLQTLNLGE NNLGGVLPNS FSNLSTSLSF LALELNKITG SIPKDIGNLI
410 420 430 440 450
GLQHLYLCNN NFRGSLPSSL GRLKNLGILL AYENNLSGSI PLAIGNLTEL
460 470 480 490 500
NILLLGTNKF SGWIPYTLSN LTNLLSLGLS TNNLSGPIPS ELFNIQTLSI
510 520 530 540 550
MINVSKNNLE GSIPQEIGHL KNLVEFHAES NRLSGKIPNT LGDCQLLRYL
560 570 580 590 600
YLQNNLLSGS IPSALGQLKG LETLDLSSNN LSGQIPTSLA DITMLHSLNL
610 620 630 640 650
SFNSFVGEVP TIGAFAAASG ISIQGNAKLC GGIPDLHLPR CCPLLENRKH
660 670 680 690 700
FPVLPISVSL AAALAILSSL YLLITWHKRT KKGAPSRTSM KGHPLVSYSQ
710 720 730 740 750
LVKATDGFAP TNLLGSGSFG SVYKGKLNIQ DHVAVKVLKL ENPKALKSFT
760 770 780 790 800
AECEALRNMR HRNLVKIVTI CSSIDNRGND FKAIVYDFMP NGSLEDWIHP
810 820 830 840 850
ETNDQADQRH LNLHRRVTIL LDVACALDYL HRHGPEPVVH CDIKSSNVLL
860 870 880 890 900
DSDMVAHVGD FGLARILVDG TSLIQQSTSS MGFIGTIGYA APEYGVGLIA
910 920 930 940 950
STHGDIYSYG ILVLEIVTGK RPTDSTFRPD LGLRQYVELG LHGRVTDVVD
960 970 980 990 1000
TKLILDSENW LNSTNNSPCR RITECIVWLL RLGLSCSQEL PSSRTPTGDI
1010 1020
IDELNAIKQN LSGLFPVCEG GSLEF
Length:1,025
Mass (Da):111,339
Last modified:May 30, 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:iB55D4FD938229D9B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB212798 Genomic DNA Translation: BAE93933.1
AB212799 Genomic DNA Translation: BAE93934.1

<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
AB212798 Genomic DNA Translation: BAE93933.1
AB212799 Genomic DNA Translation: BAE93934.1

3D structure databases

SMRiQ1MX30
ModBaseiSearch...

PTM databases

iPTMnetiQ1MX30

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.80.10.10, 3 hits
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR013210 LRR_N_plant-typ
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00560 LRR_1, 1 hit
PF13855 LRR_8, 3 hits
PF08263 LRRNT_2, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00369 LRR_TYP, 12 hits
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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 nameiXA21_ORYSI
<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: Q1MX30
<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: September 7, 2016
Last sequence update: May 30, 2006
Last modified: September 18, 2019
This is version 99 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 programPlant 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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