Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s244_27V6.2 |
Family | CBM57 |
Protein Properties | Length: 1014 Molecular Weight: 110427 Isoelectric Point: 6.8407 |
Chromosome | Chromosome/Scaffold: 244 Start: 294497 End: 301707 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 416 | 571 | 1.4e-29 |
LAVNVGGSVHGKYEEDTATLGSTAFAAKKHWAASSTGFVPGASFTSLVKSGTPVSGTADQTVYATARTSLGSLRYYATQLRNGDYNVVLSFAEIVYTRDD NLARRVFDIYLQGQLMKKDFDIGETAGGSFVAHEEKFQVAVTTGVLDIHLFYAGKG |
Full Sequence |
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Protein Sequence Length: 1014 Download |
MEPHRTTRRH RFFGPVSIIT LLVLNYCAAG ESQSTAILDP TEAALIKNVA LSYHLENLVF 60 PDSDPCTTWN PQKVKCDCYF ADNTGQPNTL CRITRIDFSM AGMEGPFPKD LTKLTYLTSL 120 QLYNNNMTGP IPPEIGLLTR LNSLSLGTNG FSGTIPRELG NLQALQLLHL DSNQLNGTIP 180 SEIGTIQTVR QLWLSDNNLS GPIPDVFGNF TGLLEVRIHG NPLLQGPIPS SLFNSPSIEA 240 IYIGELSEGK ALPATFTTPL SNLSVLYLRN CRLTGSIPST INMLSKLQYL DLSFNNLSGE 300 IPSQLSEITS LKTLYLGSNS LTGRLPEGLG ALSFLTEVDV SYNFLNGTLP SWVDKPTVTT 360 ILGSNYFSTI TAVNSQVQPQ LSLLNCQNQK TPCVISALGN VFGTNVRSGL ATVTSLAVNV 420 GGSVHGKYEE DTATLGSTAF AAKKHWAASS TGFVPGASFT SLVKSGTPVS GTADQTVYAT 480 ARTSLGSLRY YATQLRNGDY NVVLSFAEIV YTRDDNLARR VFDIYLQGQL MKKDFDIGET 540 AGGSFVAHEE KFQVAVTTGV LDIHLFYAGK GTCCLPQPSN WSFGPLLSAI SVDNVLSGGQ 600 TQVSGGKNSK GSSVGLIVGL TVAAIVLVIL VLCCICGLVV RRRKNRTTLR LEDQLEIQKF 660 QVQPNLFSYA ELKAATRSFD PGNKLGEGGY GVVYKGVLAD GTEVAVKTLS AKSYQGKHEF 720 LNEAALITAV QHRSLVKLKG CCLERDHRIL VYEFMENKSL HQTLFGARAM PMDWPTRFII 780 ALGTARGLAY LHEESEARIV HRDIKASNIL LDRNFNPKIA DFGMARLFED HQSHVSTRVA 840 GTLGYVAPEY ALLGQLTEKA DVFSYGIVLL ELVSGRFNIR TDIRGEQAYL LEWAWKLEAE 900 DNLLYVMDGK LLDTYVEDEV LRVLHVALLC TQAVASTRPC MTRVVAMLLG DIELPPITSG 960 PGFMVGLMHS ETPSHSTSSS FLTNSSGFRG KESAPLIQLS ETRTKTDMEM YPR* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 3.0e-42 | 702 | 948 | 262 | + 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. | ||
pfam00069 | Pkinase | 3.0e-42 | 700 | 877 | 182 | + Protein kinase domain. | ||
smart00221 | STYKc | 1.0e-42 | 702 | 948 | 250 | + 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 | 4.0e-43 | 703 | 948 | 249 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 1.0e-43 | 700 | 872 | 176 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005515 | protein binding |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001778728.1 | 0.00003 | 91 | 183 | 159 | 241 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001778728.1 | 0 | 121 | 1013 | 9 | 886 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001778728.1 | 0.003 | 283 | 353 | 1 | 71 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002267672.1 | 0 | 32 | 1005 | 34 | 1019 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 663 | 951 | 16 | 309 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
PDB | 3uim_A | 0 | 663 | 951 | 16 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 663 | 951 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 663 | 951 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 663 | 951 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |