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Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os04g52600.1 |
Family | CBM57 |
Protein Properties | Length: 1026 Molecular Weight: 111603 Isoelectric Point: 7.4389 |
Chromosome | Chromosome/Scaffold: 4 Start: 31274470 End: 31282411 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 427 | 599 | 2.4e-27 |
FAVDCGSNRLISASDNLRYQTDDASLGPASYSVTGAPTWGVSNVGKFVDAPNGSYIIYSSRQFQNTLDSELFQTSRMSPSSLRYYGIGLENGNYTVTLQF AEFGIEDTQTWKSLGRRVFDIYLQGERQEKNFDIRKAAGDKSYTVVKKSYKVPVTKNFLEIHLFWAGKGTCCI |
Full Sequence |
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Protein Sequence Length: 1026 Download |
MRVMSHLLLH GGVLLLLLAA AAVQAQRVAT KTDPTEAAAL NAVFAKLGQQ ASLSTATWNI 60 SGDPCTGAAT DGTPIDDNPN FNPAIKCDCT FQNNTVCRIT KLKIYALDVP GTIPQELRNL 120 TRLTHLNLGQ NTLTGPLPSF IGELTNMQNM TFRINSLSGP IPKELGNLTN LVSLGLGSNR 180 FNGSLPSELG NLDKLQELYI DSAGLSGPLP SSFSKLTRMQ TLWASDNDFT GQIPDYIGNW 240 NLTDLRFQGN SFQGPIPSAL SNLVQLSSLR IGDIENGSSS SLAFIGNMTS LSILILRNCK 300 ISDNLASIDF SKFASLNLLD LSFNNITGQV PTALLGLNLL NSLFLGNNSL SGSLPSSKGP 360 SLSTLDFSYN QLSGNFPPWA SGKNLQLNLV ANNFVIDSSN NSILPSGLAC LQRNTPCFLG 420 SPQSSSFAVD CGSNRLISAS DNLRYQTDDA SLGPASYSVT GAPTWGVSNV GKFVDAPNGS 480 YIIYSSRQFQ NTLDSELFQT SRMSPSSLRY YGIGLENGNY TVTLQFAEFG IEDTQTWKSL 540 GRRVFDIYLQ GERQEKNFDI RKAAGDKSYT VVKKSYKVPV TKNFLEIHLF WAGKGTCCIP 600 GQGYYGPTIS ALSVTPADFT PTVGIVAEQN KSTSKTGVIV GVVVGVAVLG LVALVGIFMW 660 RQKRRKLTLE QQELYSIVGR PNVFSYSELR SATENFSSSN RLGEGGYGAV YKGKLNDGRV 720 VAVKQLSQTS HQGKKQFATE IETISRVQHR NLVKLYGCCL EGNNPLLVYE YMENGSLDKA 780 LFGIEKLNID WPARFDICLG IARGLAYLHE ESSIRVVHRD IKASNVLLDA NLNPKISDFG 840 LAKLYDDKKT HVSTKVAGTF GYLAPEYAMR GHMTEKVDVF AFGVVLLETL AGRPNYDDTL 900 EEDKIYIFEW AWELYENNNP LGIVDPNLRE FNRAEVLRAI HVALLCTQGS PHQRPPMSRV 960 VSMLTGDTEV TDVLMKPSYI TEWQIKGGNT SFANSAVRGQ SSSAPGSTSQ QASSVFLNSI 1020 IQEGR* 1080 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 5.0e-53 | 700 | 965 | 290 | + Catalytic domain of Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers. | ||
cd00180 | PKc | 5.0e-55 | 702 | 888 | 191 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
pfam00069 | Pkinase | 2.0e-55 | 701 | 909 | 213 | + Protein kinase domain. | ||
smart00221 | STYKc | 1.0e-56 | 702 | 964 | 279 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
smart00219 | TyrKc | 1.0e-56 | 702 | 964 | 279 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
Gene Ontology | |
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GO Term | Description |
GO:0000166 | nucleotide binding |
GO:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0005886 | plasma membrane |
GO:0006464 | cellular protein modification process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAD41882.2 | 0 | 1 | 1025 | 1 | 1025 | OSJNBa0093O08.1 [Oryza sativa (japonica cultivar-group)] |
EMBL | CAD41884.2 | 0 | 2 | 984 | 4 | 987 | OSJNBa0093O08.3 [Oryza sativa (japonica cultivar-group)] |
EMBL | CAJ86313.1 | 0 | 27 | 1025 | 26 | 917 | H0525G02.10 [Oryza sativa (indica cultivar-group)] |
GenBank | EAY95562.1 | 0 | 27 | 1025 | 26 | 917 | hypothetical protein OsI_17410 [Oryza sativa Indica Group] |
GenBank | EEE61686.1 | 0 | 1 | 1025 | 1 | 1001 | hypothetical protein OsJ_16159 [Oryza sativa Japonica Group] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 678 | 967 | 14 | 309 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 3uim_A | 0 | 678 | 967 | 14 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 678 | 967 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 678 | 967 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 678 | 967 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |