| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01037993001 |
| Family | CBM57 |
| Protein Properties | Length: 2283 Molecular Weight: 251775 Isoelectric Point: 6.1127 |
| Chromosome | Chromosome/Scaffold: 10 Start: 12136607 End: 12204378 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 1703 | 1868 | 2.9e-30 |
| SIKCGGPEWRTPDGTVYEADNSITTGTASTSYYVSRLENWGVSNVGLYSDRIAYKTEVSGTNHPELFKTSRISPGSLRYYGLGLQNGHYTVSLQFAEMEL KDQSAQTWESIGRRVFDIYIQGTLQLKDFDITKEAGGVERAIERKFNAVVSQNYLEIHLFWAGKGT | |||
| CBM57 | 434 | 602 | 3.3e-32 |
| SVNCGGQEMRIADGTVYEVDNSSLGAASYYVTNTEKWAVSNVGLFSDSSNPAYLENNLKQVADTSTPELFQTSRVSPGSLRYYGLGLENGNYTVSLEFAE TKFASRSTETWESLGRRVFDIYIQGSLQLKDFDISKEAGGVDKALEKKFNATVSENYLEIHLFWAGKGT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 2283 Download |
| MNVTVKRASA SPSLPRCPSI IILFFLLWLF LLFQESTAEN ATLDPSEAEA LNSIFQQWDT 60 QSVALWNISG EPCTGSAING TAFESDDNNP AIKCDCSYDS GTTCHITQLR VYALNKKGVI 120 PEELATLTYL TFLKIDQNYF TGPLPSFIGN LSKLSLLSIA HNAFSGTIPK ELGNLTELEV 180 LSLGSNNFSG NLPPELGNLS KLRELYINSC GAGGEIPSTF AELLNLQVME GSDSPFTGKI 240 PNFIGNFTRL TSLRFQGNSF EGPIPSSFSK LISLSSLRIS DLYNVSSSLD FIRDLKNLTD 300 LNLRNALISG SIPSFTGEFQ KLQRLDLSFN NLTGEVPSSL FNSSALTDLF LGNNSLSGSL 360 PAQKSEELKN IDLSYNQLSG SFPSWVTSAS GLQLNLVANN FIFGSSNSSF FQGLNCLQRN 420 FPCNRNTPLY ANFSVNCGGQ EMRIADGTVY EVDNSSLGAA SYYVTNTEKW AVSNVGLFSD 480 SSNPAYLENN LKQVADTSTP ELFQTSRVSP GSLRYYGLGL ENGNYTVSLE FAETKFASRS 540 TETWESLGRR VFDIYIQGSL QLKDFDISKE AGGVDKALEK KFNATVSENY LEIHLFWAGK 600 GTCCIPVQGY YGPSISALSV VSDFTPSVSG IPSIPPSKKN NTGLIVGVVV AVGSVSFILI 660 CAVFYMKMRA SNINEDEELL GIGPRPNTFT YAELRTATED FNPTNKLGEG GFGPVYKGKL 720 NDERAVAVKQ LSVASHQGKS QFITEIATIS AVQHRNLVKL YGCCIEGDKR LLVYEYLENK 780 SLDQALFGKN DLHLDWATRF NVCMGTARGL AYLHEESRPR IVHRDVKASN ILLDAELCPK 840 ISDFGLAKLY DDKKTHISTR VAGTIGYLAP EYAMRGHLTE KADVFGFGVV ALEILSGRPN 900 SDNSLETEKI YLLEWAWTLH ESNRGLELVD PTLTAFDEDE ANRIIGVALL CTQSSPLLRP 960 TMSRAVAMLA GDIEISAVTV KPSYLTDWDF KDITSELLDE GDTQISVASK NGSAHDHGQY 1020 YNDDASKLAP SPINFTEPTL HETSETKFNF FIPRLPIFSL WRFLHECFYF HALINFILEI 1080 RALLSQSSIP VFPTAQFHPA TFSLSSYHHT THLTHSFIIS ITSYPRTYIR HTSPCLYSHT 1140 PSHPYIHDRD PTSISSSYPT PHLWSRHRIQ MCWREPLVLA AGLQRFALFT IRDCSIVVVS 1200 RYNMAMEILW DAIGARHAAL LTSNSQLHVD SLDDNMCGTT VITVLIRGRA IYVANSGDPR 1260 AVTVERKGKE IVAVDLSNDR YHPCRLLKST AQNATLHPSE GTCPSSISFS LSLSPSFLIH 1320 SLNSLFQKWD IEAVPLWNIS GEPCSGSAIN GTEFESEANS PAIKCDCSYD SNTTCHITQL 1380 RVHALNKRGV IVEEFKAFTY LMVLKLDKNY FTGPLPSFIG NLSQLTYLSV SHNALSGTIP 1440 KELGNLKELL MLSIGSNNFS GTLPPEIGNL VKLQQIYIDS SGVSGEIPST FAKLQDMVVM 1500 FATDVPITGK IPDFIGNWTK LESLRFQGNS LEGPIPSSFS KLTSLTTLRI SDLSNVSSSL 1560 DFIKEMKNLT DLVLRNSLIS GSIPFYIGEF QSLKTLDLSF NNLTGEIPDA LFNLSSLTSL 1620 FLGTNRLSGT FPAQKSEQLQ TIDLSYNELS GSFPSWLKSG LQLNLVANNL TFDSTNRSIF 1680 EGLECLQRNF PCNRDPPPYT NVSIKCGGPE WRTPDGTVYE ADNSITTGTA STSYYVSRLE 1740 NWGVSNVGLY SDRIAYKTEV SGTNHPELFK TSRISPGSLR YYGLGLQNGH YTVSLQFAEM 1800 ELKDQSAQTW ESIGRRVFDI YIQGTLQLKD FDITKEAGGV ERAIERKFNA VVSQNYLEIH 1860 LFWAGKGTCC IPFEGYYGPS ISALSVVSDL KRVPTTTPPK KGYTGLIAGI VAAIGILSFI 1920 LIICAVFYVK WKASNLNKDI VLLGVGPRPN TFRYAELRTA TENFSATNKL GEGGFGSVYK 1980 GTLPDGRVVA VKELTVASQH GKSQFITEIA TISAVQHRNL VKLYGFCIKG NRRLLVYEYL 2040 ENRSLDHSLF GKNNLHLDWP TRFNVCLATA RALAYLHEES RPRIVHRDVK ASNILLDEDL 2100 CPKISDFGLA KLYDDKKTHI STRIAGTIGY LAPEYAMRGH LTEKADVFSF GVVALEILSG 2160 RPNTDNSLDA KMIYLLEWAW ALHENNRSLD LIDPRLTAFD ENEAIRVVGV ALLCTQASPV 2220 LRPTMSRVVA MLAGDIEVST VASKPSYLTD WDFNDATSSF LSEDTQTSSA FNKSAIIQRL 2280 PL* 2340 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00180 | PKc | 2.0e-46 | 707 | 894 | 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 | 2.0e-48 | 706 | 896 | 197 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00180 | PKc | 3.0e-49 | 1970 | 2187 | 222 | + 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 | 1.0e-57 | 432 | 618 | 190 | + 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. | ||
| pfam11721 | Malectin | 2.0e-58 | 1700 | 1884 | 187 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI39030.1 | 0 | 1 | 2282 | 1 | 2282 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002272816.1 | 0 | 49 | 1041 | 6 | 1001 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002272816.1 | 0 | 1319 | 2275 | 5 | 961 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002273016.1 | 0 | 1 | 1042 | 1 | 1042 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002273016.1 | 0 | 1288 | 2270 | 35 | 1008 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 1952 | 2235 | 20 | 309 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3ulz_A | 0 | 689 | 972 | 20 | 309 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3uim_A | 0 | 1952 | 2235 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3uim_A | 0 | 689 | 972 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 1952 | 2235 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
