| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM5G869532_T02 |
| Family | GT43 |
| Protein Properties | Length: 283 Molecular Weight: 31143.3 Isoelectric Point: 6.6199 |
| Chromosome | Chromosome/Scaffold: 2 Start: 176830891 End: 176834570 |
| Description | Nucleotide-diphospho-sugar transferases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT43 | 3 | 111 | 6.2e-25 |
| LPVHGPACNSSGHLIGWHTFNSLPFSGKTATVVGEAAPVLPRDLEWAGFVLNSRMLWKEADGKPDWVKDLDAVGENGEEIENPLTLLNDPSSVEPLGNYG KKVLLWWLC | |||
| Full Sequence |
|---|
| Protein Sequence Length: 283 Download |
| MPLPVHGPAC NSSGHLIGWH TFNSLPFSGK TATVVGEAAP VLPRDLEWAG FVLNSRMLWK 60 EADGKPDWVK DLDAVGENGE EIENPLTLLN DPSSVEPLGN YGKKVLLWWL CVEARADSKF 120 PEGFILLTPA DIGLLIHTKI DSYLALNLKM LIRFCQKLQK SWYVSWPGGH PKIIHRDIKA 180 SNILLDFKFE AKVADFGLAK CTTDNNTHVS TRVMGTFGYL APEYATSGKL TEKSDVFSFG 240 VMLLELITGQ RPIDTTQLAM LAISTYVLPF ACCIILIPIA KL* 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00219 | TyrKc | 1.0e-20 | 172 | 252 | 82 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00180 | PKc | 3.0e-22 | 172 | 246 | 77 | + 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 | 4.0e-23 | 172 | 262 | 96 | + Protein kinase domain. | ||
| smart00220 | S_TKc | 2.0e-23 | 172 | 252 | 81 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
| cd06606 | STKc_MAPKKK | 1.0e-23 | 172 | 265 | 98 | + Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase. Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004672 | protein kinase activity |
| GO:0005524 | ATP binding |
| GO:0006468 | protein phosphorylation |
| GO:0015018 | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity |
| GO:0016020 | membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACF84622.1 | 0 | 1 | 132 | 171 | 302 | unknown [Zea mays] |
| EMBL | CAI93190.1 | 0 | 1 | 132 | 344 | 475 | glycosyltransferase [Saccharum officinarum] |
| RefSeq | NP_001058411.1 | 0 | 1 | 132 | 82 | 213 | Os06g0687900 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001105784.1 | 0 | 1 | 123 | 342 | 464 | glycosyltransferase [Zea mays] |
| RefSeq | XP_002437486.1 | 0 | 1 | 132 | 171 | 302 | hypothetical protein SORBIDRAFT_10g027970 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 2e-31 | 171 | 259 | 153 | 241 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 3uim_A | 2e-31 | 171 | 259 | 153 | 241 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 4e-31 | 171 | 259 | 161 | 249 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 4e-31 | 171 | 259 | 161 | 249 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 4e-31 | 171 | 259 | 161 | 249 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
