Differentially expressed in FDCP 8 homolog [Caenorhabditis elegans]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
zf-RING_9 | pfam13901 | Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members ... |
259-467 | 8.36e-76 | ||||
Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169 : Pssm-ID: 464030 Cd Length: 205 Bit Score: 236.74 E-value: 8.36e-76
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C1_DEF8 | cd20819 | protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ... |
160-216 | 4.53e-21 | ||||
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. : Pssm-ID: 410369 Cd Length: 62 Bit Score: 86.56 E-value: 4.53e-21
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Name | Accession | Description | Interval | E-value | ||||
zf-RING_9 | pfam13901 | Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members ... |
259-467 | 8.36e-76 | ||||
Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169 Pssm-ID: 464030 Cd Length: 205 Bit Score: 236.74 E-value: 8.36e-76
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C1_DEF8 | cd20819 | protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ... |
160-216 | 4.53e-21 | ||||
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410369 Cd Length: 62 Bit Score: 86.56 E-value: 4.53e-21
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C1 | smart00109 | Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
166-212 | 1.44e-08 | ||||
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains. Pssm-ID: 197519 Cd Length: 50 Bit Score: 50.93 E-value: 1.44e-08
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C1_1 | pfam00130 | Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
176-212 | 9.81e-03 | ||||
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain. Pssm-ID: 395079 Cd Length: 53 Bit Score: 34.34 E-value: 9.81e-03
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Name | Accession | Description | Interval | E-value | ||||
zf-RING_9 | pfam13901 | Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members ... |
259-467 | 8.36e-76 | ||||
Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169 Pssm-ID: 464030 Cd Length: 205 Bit Score: 236.74 E-value: 8.36e-76
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C1_DEF8 | cd20819 | protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ... |
160-216 | 4.53e-21 | ||||
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410369 Cd Length: 62 Bit Score: 86.56 E-value: 4.53e-21
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C1 | smart00109 | Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
166-212 | 1.44e-08 | ||||
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains. Pssm-ID: 197519 Cd Length: 50 Bit Score: 50.93 E-value: 1.44e-08
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C1 | cd00029 | protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
161-212 | 1.46e-06 | ||||
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme. Pssm-ID: 410341 Cd Length: 50 Bit Score: 45.20 E-value: 1.46e-06
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C1_Sbf-like | cd20827 | protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ... |
176-213 | 7.05e-04 | ||||
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410377 Cd Length: 53 Bit Score: 37.78 E-value: 7.05e-04
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C1_CHN | cd20806 | protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ... |
161-212 | 2.05e-03 | ||||
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410356 Cd Length: 53 Bit Score: 36.13 E-value: 2.05e-03
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C1_PKD3_rpt1 | cd20841 | first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ... |
176-219 | 2.43e-03 | ||||
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410391 Cd Length: 75 Bit Score: 36.94 E-value: 2.43e-03
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C1_SpBZZ1-like | cd20824 | protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ... |
176-214 | 3.03e-03 | ||||
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410374 Cd Length: 53 Bit Score: 35.75 E-value: 3.03e-03
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C1_betaCHN | cd20857 | protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ... |
161-212 | 3.85e-03 | ||||
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410407 Cd Length: 61 Bit Score: 35.79 E-value: 3.85e-03
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C1_cPKC_nPKC_rpt2 | cd20793 | second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ... |
176-212 | 4.01e-03 | ||||
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410343 Cd Length: 50 Bit Score: 35.33 E-value: 4.01e-03
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C1_MTMR-like | cd20828 | protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ... |
176-212 | 4.95e-03 | ||||
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites. Pssm-ID: 410378 Cd Length: 57 Bit Score: 35.50 E-value: 4.95e-03
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C1_1 | pfam00130 | Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
176-212 | 9.81e-03 | ||||
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain. Pssm-ID: 395079 Cd Length: 53 Bit Score: 34.34 E-value: 9.81e-03
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Blast search parameters | ||||
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