Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_17053g0010 |
Family | CBM57 |
Protein Properties | Length: 911 Molecular Weight: 100197 Isoelectric Point: 6.3032 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 31 | 160 | 1.6e-26 |
SDTGYFMDSSKPSYIATNQSQITKTLDSELYKTARLSPSSLRYYGLGLENGPYTVNLQFAEIQIENTNGWKSLGRRIFDVYVQEQKVLTDFDIRKEAGGS NIAVVKSFNKINVTSNFLEIHFFWAGKGTC |
Full Sequence |
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Protein Sequence Length: 911 Download |
MTYGGDVFEQ ENETLNAASF YVSNTQKWGV SDTGYFMDSS KPSYIATNQS QITKTLDSEL 60 YKTARLSPSS LRYYGLGLEN GPYTVNLQFA EIQIENTNGW KSLGRRIFDV YVQEQKVLTD 120 FDIRKEAGGS NIAVVKSFNK INVTSNFLEI HFFWAGKGTC CIPIQGAYGP LVSAIRVTPE 180 FNTKKSKTGI VIGIAIGIAS ALICIILVFF LWRRRVRKLA GTDVKEDEAI NDIRSKLKIF 240 TYAEMKTATK DFSRENKLGE GGYGAVYKGT LSDGEMVAVK QLSSESRQGK REFINEVAVI 300 SAVQHRNLVK LNGCCLETDD PLLVYEYFAN SSLDKALLDS GFAINCGGPR KTFGPGDVFE 360 QENETLNAAS FYVNKAQKWG VSNTGSFLDS RNPTYTASKF NSTVDGAKSK TGIVIGITIG 420 IAAAFICIIF VFLLWKRRVQ KLAGTDVEED EAINVIRSKL KIFSYADMKT ATGDFDNENK 480 LGEGGYGAVY KAILSDGKMV AVKQLSSDSR QGKREFINEV AVISAVQHRN LVKLHGCCLE 540 ADHRLLVYEY LENNSLAKAL FGNKKSHLQL DWHTRYNICI GTARGLAYLH EESSTRIIHR 600 DIKASNILLD DSLNPKIADF GLARLYDEMK THVSTRVAGT VGYLAPEYAM RGHLTEKADV 660 FSFGVVALEL TWHLQEKERP LDLMDPDIES TCSKEEVLRV IEVALLCTQA LPPMRPSMSR 720 VVAMLTGDIE VNPAASRPGY IKDLQYNNAI AGGTGTGSTP VAATTSMDNS AGSLSIVNTD 780 SLTLSSADEN TWHLYEQGRP LELMDSYIES TCSKEEVLSV IEVALLCTQA VPTMRPSMSR 840 VVAMLTSDVE VIPVASRPGY IKDLEYNNVI AGATSTGSTT PMHNSTEGSP ILNYDRLALC 900 SAETKCNSIK D |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
cd00180 | PKc | 2.0e-13 | 258 | 333 | 78 | + 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 | 1.0e-51 | 478 | 725 | 270 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
cd00180 | PKc | 8.0e-53 | 481 | 680 | 213 | + 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 | 7.0e-56 | 19 | 175 | 159 | + 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. |
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 | CAN73906.1 | 0 | 23 | 341 | 157 | 436 | hypothetical protein [Vitis vinifera] |
EMBL | CAN73906.1 | 0 | 463 | 784 | 335 | 675 | hypothetical protein [Vitis vinifera] |
EMBL | CAN73906.1 | 0.000000000000003 | 789 | 869 | 560 | 639 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529290.1 | 0 | 449 | 743 | 231 | 543 | 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 | 446 | 728 | 3 | 309 | A Chain A, Crystal Structure Analysis Of Syd |
PDB | 3ulz_A | 2e-20 | 236 | 337 | 16 | 118 | A Chain A, Crystal Structure Analysis Of Syd |
PDB | 3ulz_A | 0.00008 | 803 | 848 | 264 | 309 | A Chain A, Crystal Structure Analysis Of Syd |
PDB | 3uim_A | 0 | 446 | 728 | 3 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3uim_A | 2e-20 | 236 | 337 | 16 | 118 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |