Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma05g29530.2 |
Family | CBM57 |
Protein Properties | Length: 985 Molecular Weight: 110568 Isoelectric Point: 7.0425 |
Chromosome | Chromosome/Scaffold: 05 Start: 35115271 End: 35127074 |
Description | receptor-like kinase in flowers 1 |
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 | 410 | 580 | 2.1e-24 |
HVNCGGKNVKVMENDENIQYVGDDGALGSSAAKYFIDYENHWGFSSTGDFLDDGDYLNSRYIRSLPSSNLPELYKTARVAPISLTYFRYCMENGKYTVKL HFAEIQFSNDNTYSSLGRRLFDIYVQGALFRKDFNIEGETHVAQKPYILSLYNVNVTDNILEIQFYWAGKG |
Full Sequence |
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Protein Sequence Length: 985 Download |
MMLPRTFFAF LLFALSCFRW LEYAESKLPK LPQEEVDALK EITSTMGATY WEFDSDSCHS 60 KMLRLTPEPP KGSQSSIDCD CTSEINTCHV VGITFKRLNL PGMLPPYLAK LPNLTQVDFA 120 LNYLSGTIPK EWGSTKLTNI SLFVNRIFGE IPKELGSITT LTYLNLEANQ FSGVVPHELG 180 SLSNLKTLIL SSNKLSGKLP VTFAKLQNLT DFRISDNSFN GEIPSFIQNW KSLERLDMLA 240 SGMEGRIPSN ISLLSNLNQL KISDINSPSQ DFPMLRNMTG MTILVLRNCH ITGELPSYFW 300 SMKNLNMLDV SFNKLVGEIP VIDVPVGHLR FLFLTGNMLS GNLPESLLKD GSSLDLSYNN 360 FTWQGPDQPA CRDYLNLNLN LFRSFSGTKL RGLLPCSKIS NCPAYSHCFH VNCGGKNVKV 420 MENDENIQYV GDDGALGSSA AKYFIDYENH WGFSSTGDFL DDGDYLNSRY IRSLPSSNLP 480 ELYKTARVAP ISLTYFRYCM ENGKYTVKLH FAEIQFSNDN TYSSLGRRLF DIYVQGALFR 540 KDFNIEGETH VAQKPYILSL YNVNVTDNIL EIQFYWAGKG TTRIPVSGVY GPLISAFSIV 600 SDSKPCTDQK NVRHKIIVGV GFGVTALCLV IIIVGIFWWK GYFKGIIRKI KDTERRDCLT 660 GTFTLKQIRD ATEDFSPDNK IGEGGFGPVY KGQLSDGTLV AVKQLSSRSR QGNGEFLNEI 720 GMISCLQHPN LVKLHGFCIE GDQLILVYEY MENNSLAHAL FSSKDQLKLD WATRLRICIG 780 IAKGLAFLHE ESRLKIVHRD IKATNVLLDG NLNPKISDFG LARLDEEKTH VTTRIAGTIG 840 YMAPEYALWG YLSYKADVYS YGVVVFEVVS GKNYKNFMPS DNCVCLLDKA FHLQRAENLI 900 EMVDERLRSE VNPTEAITLM KVALLCTSVS PSHRPTMSEV VNMLEGRISI PNAIQQPTDF 960 SEDLRFKAMR DIHQQRENHS LSTS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00221 | STYKc | 2.0e-43 | 678 | 944 | 280 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
pfam07714 | Pkinase_Tyr | 1.0e-43 | 680 | 944 | 280 | + Protein tyrosine kinase. | ||
smart00219 | TyrKc | 9.0e-44 | 678 | 944 | 280 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 1.0e-45 | 681 | 944 | 268 | + 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. | ||
pfam11721 | Malectin | 4.0e-49 | 407 | 597 | 192 | + Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan. |
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 |
GenBank | ACM89466.1 | 0 | 421 | 984 | 1 | 564 | ATP-binding/protein serine/threonine kinase [Glycine max] |
RefSeq | NP_174268.7 | 0 | 8 | 980 | 22 | 988 | 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 | 35 | 982 | 5 | 975 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305711.1 | 0 | 36 | 984 | 1 | 912 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522277.1 | 0 | 46 | 975 | 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 | 663 | 946 | 20 | 308 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3uim_A | 0 | 663 | 946 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 663 | 946 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 663 | 946 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 663 | 946 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |