Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_026_00352.1 |
Family | CBM57 |
Protein Properties | Length: 876 Molecular Weight: 97279.6 Isoelectric Point: 5.6577 |
Chromosome | Chromosome/Scaffold: 26 Start: 2334515 End: 2338034 |
Description | hercules receptor kinase 2 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 223 | 378 | 2.4e-22 |
VYRLNVGGPEIKPDRDQDLWRIWESDISYMFTSYAGSEIKNASNITYSSVNDSSVAPLLVYETARTMTNNEVLEKRFNMSWKLEVDPNFDYLVRLHFCEL VYDKDNQRVFRIYVNNKTASENFDVFARAGGMNKAYHQDYVDVVSSQIDTLWIQLG |
Full Sequence |
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Protein Sequence Length: 876 Download |
MKVCVLICMV LLSGFIKSGE AQTKPFLVNC GVTSSVNIDG RRWIGDLDTG DNFTLSYPGI 60 AASTPNISEE SIYETLYKTA RFFTESSNYT FGVDPGNYYL RLHFYPFSFE DNDVSKSLFT 120 IMANNLKLVS GFSVTTEISR KNSYMETLGS NSSSSSLMKE YFVNVNSAEL VIEVIPDEGT 180 FAFVNAIEVI PVLSKLFEGS VSKVGENGAD NSLNLGERGI ETVYRLNVGG PEIKPDRDQD 240 LWRIWESDIS YMFTSYAGSE IKNASNITYS SVNDSSVAPL LVYETARTMT NNEVLEKRFN 300 MSWKLEVDPN FDYLVRLHFC ELVYDKDNQR VFRIYVNNKT ASENFDVFAR AGGMNKAYHQ 360 DYVDVVSSQI DTLWIQLGPD TAAGATGTDA LLNGLEIFKL SRRGDLSRIS DRSGSGGKSG 420 GLKSRALWLG IGAGVASIAV IAFLCAMFVR RRNTMAPNKS HPPGWRPFFL HGTFGNSTNN 480 AQGSKFPGGT LTLNGSMATI RTGKYFTLAE MRLATNNFDD SLVIGVGGFG KVYKGEIDDG 540 SLVAIKRAHP QSQQGLREFE TEIEMLSKLR HRHLVSMIGF CQEQNEMILV YEYMANGTLR 600 THLFGSDLPP LTWKQRLDAC IGAARGLHYL HTGAERSIIH RDVKTTNILL DENFVAKMAD 660 FGLSKTGPAL DHTHVSTAVK GSFGYLDPEY FRRQHLTEKS DVYSFGVVLF EVVCARPVIN 720 PSLPKDQINL AEWAIRWQRQ GSLESIVDPK LRKCYSLDSF KKFGEIAEKC LADEGKNRPT 780 MGEVLWHLEY VLQLHEASLR RNSVEDSFSS TQIPANPDNP EVGNENNADH NLVEGRETVI 840 DLNLGEDEEN TRGSSISNGT AGVEEFSQLV HPQGR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00180 | PKc | 4.0e-49 | 524 | 711 | 192 | + 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. | ||
smart00219 | TyrKc | 5.0e-50 | 523 | 788 | 274 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00221 | STYKc | 3.0e-51 | 523 | 788 | 277 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00192 | PTKc | 4.0e-53 | 523 | 789 | 285 | + 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. | ||
pfam12819 | Malectin_like | 6.0e-54 | 28 | 376 | 361 | + Carbohydrate-binding protein of the ER. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. The domain is found on a number of plant receptor kinases. |
Gene Ontology | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
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 |
EMBL | CBI31024.1 | 0 | 1 | 839 | 1 | 838 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264211.1 | 0 | 1 | 839 | 46 | 883 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299052.1 | 0 | 5 | 812 | 13 | 809 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330599.1 | 0 | 5 | 812 | 13 | 815 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523186.1 | 0 | 2 | 812 | 8 | 812 | kinase, putative [Ricinus communis] |
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 | 2qkw_B | 0 | 483 | 799 | 2 | 321 | A Chain A, Structural Basis For Activation Of Plant Immunity By Bacterial Effector Protein Avrpto |
PDB | 3hgk_D | 0 | 483 | 799 | 2 | 321 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_C | 0 | 483 | 799 | 2 | 321 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_B | 0 | 483 | 799 | 2 | 321 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_A | 0 | 483 | 799 | 2 | 321 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
Transmembrane Domains | ||||
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Start | End | |||
427 | 449 |
Signal Peptide | ||||
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Cleavage Site | ||||
21 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES805185 | 324 | 464 | 784 | 0 |
EX357602 | 257 | 528 | 784 | 0 |
DY971329 | 314 | 481 | 794 | 0 |
GT050217 | 320 | 478 | 797 | 0 |
DN217707 | 258 | 528 | 785 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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