Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a000913m |
Family | CBM57 |
Protein Properties | Length: 945 Molecular Weight: 105278 Isoelectric Point: 5.4329 |
Chromosome | Chromosome/Scaffold: 12 Start: 2255032 End: 2260367 |
Description | receptor-like kinase in flowers 1 |
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 | 343 | 508 | 8.3e-26 |
HVNCGGADVEIEESKRRVIYEGDTGDNPAKYLSNNYWGFISTGDFLDEPNYQNTHQIRPTTTTNLSELYTSARISPLSLTYFHYCLEDGNYNIALHFAEI LFTNDETYSSLGRRMFDIYIQEILVSKDFNIENEAGGSGRPVIKYFNATVRDNNILEIRFYWASKG |
Full Sequence |
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Protein Sequence Length: 945 Download |
MGAKYWKFNG GLCEVESVGV SAAPPSGSEG YVECNCNYNN NTICHVTKIV LKGYNLPGIL 60 SANFVKLRYL QEIDFAYNFL SGAIPIQWAS LQLTSISVLV NRLSGEIPSE LGNITSLTYL 120 NLEANNFSGN IPSDVGKLIN LKTMILSSNR LTGQLPMSFS QLVNLNDFRI NDNNLSGRIP 180 DFIQNWKQLD RLEMQASGME GPIPLNISLL NVLTDLRLSD LRGPLQEFPL LRSITGLTTL 240 ILRNCNISGE IPAYIWRFRV LQMLFVTANM LSGDIPDTIL KDGSNIDLSY NNFTWQGPDE 300 AACLPNTNQN INLFNGSSNG NTLQRILPCS RNVACPKYKC SLHVNCGGAD VEIEESKRRV 360 IYEGDTGDNP AKYLSNNYWG FISTGDFLDE PNYQNTHQIR PTTTTNLSEL YTSARISPLS 420 LTYFHYCLED GNYNIALHFA EILFTNDETY SSLGRRMFDI YIQEILVSKD FNIENEAGGS 480 GRPVIKYFNA TVRDNNILEI RFYWASKGTT RIPNRGDYGS LISAISVNPN FKVCSDGNEK 540 NITAYIVGAV VIVCIIFLIL GILWWKGLLQ GKKKIRKGFE GVELQTIAFS LKQIKIATND 600 FDASNKIGEG GFGPVYKGLL PDRTVIAVKK LSSGSRQGNR EFLNEIGMIS CVQHPNLVKL 660 YGCCIEGDQL LLVYEYMENN SLANVLFDSN KSQLILDWAT RFKICIGIAR GLAYLHEESR 720 LKIVHRDIKA TNVLLDKDLN PKISDFGLAR LNEDEKTHIS TKVAGTIGYM APEYALWGYL 780 TDKVDVYSYG VVLLEIVSGK SNNSYMPSDS FICLLDWASH LQESKKVDEL IDERLMGTEI 840 DKDEVERMVR VALLCTNATP SIRPTMSEVV LMIEGNMDIP NNNAVSEGSS DVRFKAIKEF 900 QRERRSQSTS SRGRIEKSTV LVPGDVGFSS FASDIYESTS DSVV* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00180 | PKc | 4.0e-50 | 607 | 796 | 194 | + 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. | ||
pfam07714 | Pkinase_Tyr | 2.0e-50 | 606 | 873 | 277 | + Protein tyrosine kinase. | ||
cd00192 | PTKc | 6.0e-51 | 605 | 874 | 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. | ||
smart00221 | STYKc | 5.0e-53 | 606 | 870 | 274 | + 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-53 | 606 | 870 | 273 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
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 | NP_174268.7 | 0 | 1 | 902 | 57 | 982 | RKF1 (RECEPTOR-LIKE KINASE IN FLOWERS 1); ATP binding / kinase/ protein serine/threonine kinase/ receptor signaling protein serine/threonine kinase [Arabidopsis thaliana] |
RefSeq | XP_002264679.1 | 0 | 1 | 930 | 16 | 992 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264717.1 | 0 | 1 | 910 | 1 | 854 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305711.1 | 0 | 1 | 908 | 11 | 908 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522277.1 | 0 | 1 | 903 | 1 | 878 | ATP binding protein, 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 | 3ulz_A | 0 | 585 | 876 | 16 | 309 | A Chain A, Crystal Structure Of A Human Tcf-4 BETA-Catenin Complex |
PDB | 3uim_A | 0 | 585 | 876 | 16 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 585 | 876 | 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 | 585 | 876 | 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 | 585 | 876 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |