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Search results 2401 to 2500 out of 2733 for C6

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Type Details Score
Protein Domain
Type: Domain
Description: Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].The potyviridae are a family of positive strand RNA viruses, members of which include Zucchini yellow mosaic virus, and Turnip mosaic virus (strain Japanese) which cause considerable losses of crops worldwide.This entry represents a C-terminal region from various plant potyvirus P1 proteins (found at the N terminus of the polyprotein). The C terminus of P1 is a serine peptidase belonging to MEROPS peptidase family S30 (clan PA(S)). It is the protease responsible for autocatalytic cleavage between P1 and the helper component protease, which is a cysteine peptidase belonging to MEROPS peptidase family C6 [, ]. The P1 protein may be involved in virus-host interactions [], and evasion of immune responses [].
Protein Domain
Type: Homologous_superfamily
Description: Potyviruses form one of the most numerous groups of plant viruses and are a major cause of crop loss worldwide. The helper-component proteinase (HC-Pro) is an indispensable, multifunctional protein of members of the genus Potyvirus and other viruses of the family Potyviridae. It is directly involved in diverse steps of viral infection, such as aphid plant-to-plant transmission, polyprotein processing, and suppression of host antiviral RNA silencing. HC-Pro is generally divided into three functional domains: a N-terminal domain, a central region, and a cysteine protease domain (CPD) in the C-terminal region. The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. Cysteine and histidine residues form the catalytic dyad at the active site. The HC-Pro CPD domain constitutes the peptidase family C6 of the CA clan [].The HC-Pro CPD domain adopts a compact oval-shaped alpha/beta fold. The secondary structure elements include four α-helices (alpha1-alpha4) and two short β-strands (beta1 and beta2) arranged in the order alpha1-alpha2-alpha3-beta1-beta2-alpha4. In addition, two 3(10) helices are located between alpha3 and beta1 and downstream of alpha4. The four helices form a helix bundle packed against one face of a short β-hairpin formed by strands beta1 and beta2. The catalytic residue Cys is located at the N terminus of helix alpha1, and the other catalytic residue His is located on strand beta2. The substrate binding cleft is lined by the loop connecting helices alpha2 and alpha3 and the N-terminal region of helix alpha1 on one side and by strand beta2 on the other side [].This superfamily represents the CPD domain of the HC-Pro protein.
Protein Domain
Type: Domain
Description: This entry represents the CPD domain of the HC-Pro protein. Potyviruses form one of the most numerous groups of plant viruses and are a major cause of crop loss worldwide. The helper-component proteinase (HC-Pro) is an indispensable, multifunctional protein of members of the genus Potyvirus and other viruses of the family Potyviridae. It is directly involved in diverse steps of viral infection, such as aphid plant-to-plant transmission, polyprotein processing, and suppression of host antiviral RNA silencing. HC-Pro is generally divided into three functional domains: a N-terminal domain, a central region, and a cysteine protease domain (CPD) in the C-terminal region. The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. Cysteine and histidine residues form the catalytic dyad at the active site. The HC-Pro CPD domain constitutes the peptidase family C6 of the CA clan [].The HC-Pro CPD domain adopts a compact oval-shaped alpha/beta fold. The secondary structure elements include four α-helices (alpha1-alpha4) and two short β-strands (beta1 and beta2) arranged in the order alpha1-alpha2-alpha3-beta1-beta2-alpha4. In addition, two 3(10) helices are located between alpha3 and beta1 and downstream of alpha4. The four helices form a helix bundle packed against one face of a short β-hairpin formed by strands beta1 and beta2. The catalytic residue Cys is located at the N terminus of helix alpha1, and the other catalytic residue His is located on strand beta2. The substrate binding cleft is lined by the loop connecting helices alpha2 and alpha3 and the N-terminal region of helix alpha1 on one side and by strand beta2 on the other side [].
Protein
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
Publication
First Author: Xue F
Year: 1993
Journal: Cell
Title: kelch encodes a component of intercellular bridges in Drosophila egg chambers.
Volume: 72
Issue: 5
Pages: 681-93
Publication
First Author: Way M
Year: 1995
Journal: J Cell Biol
Title: Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm.
Volume: 128
Issue: 1-2
Pages: 51-60
Publication
First Author: Ito N
Year: 1994
Journal: J Mol Biol
Title: Crystal structure of a free radical enzyme, galactose oxidase.
Volume: 238
Issue: 5
Pages: 794-814
Publication
First Author: Ito N
Year: 1991
Journal: Nature
Title: Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.
Volume: 350
Issue: 6313
Pages: 87-90
Publication
First Author: Schughart K
Year: 1988
Journal: Proc Natl Acad Sci U S A
Title: Structure and expression of Hox-2.2, a murine homeobox-containing gene.
Volume: 85
Issue: 15
Pages: 5582-6
Publication
First Author: Gulati GS
Year: 2019
Journal: Proc Natl Acad Sci U S A
Title: Neogenin-1 distinguishes between myeloid-biased and balanced Hoxb5 + mouse long-term hematopoietic stem cells.
Volume: 116
Issue: 50
Pages: 25115-25125
Publication
First Author: Ura K
Year: 1991
Journal: Nucleic Acids Res
Title: Possible role of DNA topoisomerase II on transcription of the homeobox gene Hox-2.1 in F9 embryonal carcinoma cells.
Volume: 19
Issue: 22
Pages: 6087-92
Publication
First Author: Münke M
Year: 1986
Journal: Cytogenet Cell Genet
Title: The murine Hox-2 cluster of homeo box containing genes maps distal on chromosome 11 near the tail-short (Ts) locus.
Volume: 42
Issue: 4
Pages: 236-40
Publication
First Author: Utset MF
Year: 1987
Journal: Science
Title: Region-specific expression of two mouse homeo box genes.
Volume: 235
Issue: 4794
Pages: 1379-82
Publication
First Author: Safaei R
Year: 1997
Journal: Brain Res Dev Brain Res
Title: A target of the HoxB5 gene from the mouse nervous system.
Volume: 100
Issue: 1
Pages: 5-12
Publication
First Author: Hershko AY
Year: 2003
Journal: Gene
Title: Methylation of HoxA5 and HoxB5 and its relevance to expression during mouse development.
Volume: 302
Issue: 1-2
Pages: 65-72
Publication
First Author: Holland PW
Year: 1988
Journal: Development
Title: Spatially restricted patterns of expression of the homeobox-containing gene Hox 2.1. during mouse embryogenesis.
Volume: 102
Issue: 1
Pages: 159-74
Publication
First Author: Munton RP
Year: 2007
Journal: Mol Cell Proteomics
Title: Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.
Volume: 6
Issue: 2
Pages: 283-93
Publication
First Author: Boj SF
Year: 2012
Journal: Cell
Title: Diabetes risk gene and Wnt effector Tcf7l2/TCF4 controls hepatic response to perinatal and adult metabolic demand.
Volume: 151
Issue: 7
Pages: 1595-607
Publication
First Author: Larsen BM
Year: 2015
Journal: Development
Title: Mesenchymal Hox6 function is required for mouse pancreatic endocrine cell differentiation.
Volume: 142
Issue: 22
Pages: 3859-68
Publication    
First Author: Catela C
Year: 2022
Journal: Elife
Title: Control of spinal motor neuron terminal differentiation through sustained Hoxc8 gene activity.
Volume: 11
Publication
First Author: Hanley O
Year: 2016
Journal: Neuron
Title: Parallel Pbx-Dependent Pathways Govern the Coalescence and Fate of Motor Columns.
Volume: 91
Issue: 5
Pages: 1005-1020
Publication
First Author: Lammert F
Year: 2001
Journal: Gastroenterology
Title: Chromosomal organization of candidate genes involved in cholesterol gallstone formation: a murine gallstone map.
Volume: 120
Issue: 1
Pages: 221-38
Protein
Organism: Mus musculus/domesticus
Length: 571  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 568  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 735  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 554  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 613  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 554  
Fragment?: false
Publication
First Author: Pósfai J
Year: 1988
Journal: Gene
Title: Sequence motifs specific for cytosine methyltransferases.
Volume: 74
Issue: 1
Pages: 261-5
Publication
First Author: Lauster R
Year: 1989
Journal: J Mol Biol
Title: Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains.
Volume: 206
Issue: 2
Pages: 305-12
Publication
First Author: Hauser CA
Year: 1985
Journal: Cell
Title: Expression of homologous homeo-box-containing genes in differentiated human teratocarcinoma cells and mouse embryos.
Volume: 43
Issue: 1
Pages: 19-28
Publication
First Author: Frohman MA
Year: 1990
Journal: Development
Title: Isolation of the mouse Hox-2.9 gene; analysis of embryonic expression suggests that positional information along the anterior-posterior axis is specified by mesoderm.
Volume: 110
Issue: 2
Pages: 589-607
Publication
First Author: Yamauchi Y
Year: 1999
Journal: Dev Biol
Title: A novel transgenic technique that allows specific marking of the neural crest cell lineage in mice.
Volume: 212
Issue: 1
Pages: 191-203
Publication
First Author: Wu Y
Year: 2003
Journal: Mol Cell Biol
Title: HoxB5 is an upstream transcriptional switch for differentiation of the vascular endothelium from precursor cells.
Volume: 23
Issue: 16
Pages: 5680-91
Publication
First Author: Volpe MV
Year: 1997
Journal: Histochem Cell Biol
Title: Hoxb-5 expression in the developing mouse lung suggests a role in branching morphogenesis and epithelial cell fate.
Volume: 108
Issue: 6
Pages: 495-504
Publication
First Author: Chinoy MR
Year: 2002
Journal: J Surg Res
Title: Mesenchymal nuclear transcription factors in nitrofen-induced hypoplastic lung.
Volume: 108
Issue: 2
Pages: 203-11
Protein
Organism: Mus musculus/domesticus
Length: 766  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 751  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 633  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 875  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 493  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 752  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 711  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 493  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 469  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 302  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 751  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 393  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 818  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 441  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 844  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 758  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 814  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 709  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 588  
Fragment?: false
Publication
First Author: Choi MY
Year: 2006
Journal: Development
Title: A dynamic expression survey identifies transcription factors relevant in mouse digestive tract development.
Volume: 133
Issue: 20
Pages: 4119-29
Publication
First Author: Kondrashov N
Year: 2011
Journal: Cell
Title: Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning.
Volume: 145
Issue: 3
Pages: 383-397
Publication
First Author: Thut CJ
Year: 2001
Journal: Dev Biol
Title: A large-scale in situ screen provides molecular evidence for the induction of eye anterior segment structures by the developing lens.
Volume: 231
Issue: 1
Pages: 63-76
Protein
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 604  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
Publication
First Author: Lussier M
Year: 1990
Journal: Gene
Title: The mouse keratin 19-encoding gene: sequence, structure and chromosomal assignment.
Volume: 95
Issue: 2
Pages: 203-13
Publication  
First Author: Kam MK
Year: 2014
Journal: Int J Biochem Cell Biol
Title: Homeobox b5 (Hoxb5) regulates the expression of Forkhead box D3 gene (Foxd3) in neural crest.
Volume: 55
Pages: 144-52
Publication
First Author: Mock B
Year: 1987
Journal: Nucleic Acids Res
Title: A TaqI restriction fragment length polymorphism at the Hox-2.1 locus cosegregates with the Dlb-1 locus on mouse chromosome 11.
Volume: 15
Issue: 5
Pages: 2397
Publication
First Author: Sharpe J
Year: 1998
Journal: EMBO J
Title: Selectivity, sharing and competitive interactions in the regulation of Hoxb genes.
Volume: 17
Issue: 6
Pages: 1788-98
Protein
Organism: Mus musculus/domesticus
Length: 686  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 529  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 486  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 584  
Fragment?: false