NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform X1 [Mus musculus]
Protein Classification
WW domain-containing protein( domain architecture ID 10134116)
WW domain-containing protein; the WW domain mediates protein-protein interaction via proline-rich motifs, such as PPxY; similar to mammalian Yes-associated protein 1 (YAP1) which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| HECTc | cd00078 | HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
516-868 | 0e+00 | ||||||
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. : Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 529.44 E-value: 0e+00
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| C2_E3_ubiquitin_ligase | cd04021 | C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
17-142 | 2.08e-53 | ||||||
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. : Pssm-ID: 175988 [Multi-domain] Cd Length: 125 Bit Score: 181.32 E-value: 2.08e-53
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 | 1.21e-12 | ||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. : Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.52 E-value: 1.21e-12
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
407-435 | 2.64e-12 | ||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. : Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 61.37 E-value: 2.64e-12
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 | 1.76e-11 | ||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. : Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 59.06 E-value: 1.76e-11
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
447-477 | 9.31e-09 | ||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. : Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 51.37 E-value: 9.31e-09
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| Treacle super family | cl25490 | Treacher Collins syndrome protein Treacle; |
155-304 | 7.69e-05 | ||||||
Treacher Collins syndrome protein Treacle; The actual alignment was detected with superfamily member pfam03546: Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 46.22 E-value: 7.69e-05
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| Name | Accession | Description | Interval | E-value | |||||||||
| HECTc | cd00078 | HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
516-868 | 0e+00 | |||||||||
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 529.44 E-value: 0e+00
|
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| HECTc | smart00119 | Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
539-867 | 9.84e-177 | |||||||||
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes. Pssm-ID: 214523 Cd Length: 328 Bit Score: 512.93 E-value: 9.84e-177
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| HUL4 | COG5021 | Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
331-870 | 1.06e-173 | |||||||||
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 525.10 E-value: 1.06e-173
|
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| HECT | pfam00632 | HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
565-868 | 8.06e-129 | |||||||||
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus. Pssm-ID: 459880 Cd Length: 304 Bit Score: 388.51 E-value: 8.06e-129
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| C2_E3_ubiquitin_ligase | cd04021 | C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
17-142 | 2.08e-53 | |||||||||
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175988 [Multi-domain] Cd Length: 125 Bit Score: 181.32 E-value: 2.08e-53
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 | 1.21e-12 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.52 E-value: 1.21e-12
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
407-435 | 2.64e-12 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 61.37 E-value: 2.64e-12
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
406-436 | 3.98e-12 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 61.08 E-value: 3.98e-12
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
408-436 | 8.68e-12 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 60.23 E-value: 8.68e-12
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 | 1.76e-11 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 59.06 E-value: 1.76e-11
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
331-362 | 2.89e-11 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 58.77 E-value: 2.89e-11
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
333-362 | 5.50e-11 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.92 E-value: 5.50e-11
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
302-331 | 6.83e-11 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 57.61 E-value: 6.83e-11
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
303-331 | 8.29e-11 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.15 E-value: 8.29e-11
|
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
19-115 | 4.44e-09 | |||||||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 54.42 E-value: 4.44e-09
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
447-477 | 9.31e-09 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 51.37 E-value: 9.31e-09
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
446-475 | 6.53e-08 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 6.53e-08
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
446-477 | 1.21e-07 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 48.37 E-value: 1.21e-07
|
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| Treacle | pfam03546 | Treacher Collins syndrome protein Treacle; |
155-304 | 7.69e-05 | |||||||||
Treacher Collins syndrome protein Treacle; Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 46.22 E-value: 7.69e-05
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| PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
149-299 | 2.18e-04 | |||||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 2.18e-04
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| Name | Accession | Description | Interval | E-value | |||||||||
| HECTc | cd00078 | HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It ... |
516-868 | 0e+00 | |||||||||
HECT domain; C-terminal catalytic domain of a subclass of Ubiquitin-protein ligase (E3). It binds specific ubiquitin-conjugating enzymes (E2), accepts ubiquitin from E2, transfers ubiquitin to substrate lysine side chains, and transfers additional ubiquitin molecules to the end of growing ubiquitin chains. Pssm-ID: 238033 [Multi-domain] Cd Length: 352 Bit Score: 529.44 E-value: 0e+00
|
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| HECTc | smart00119 | Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to ... |
539-867 | 9.84e-177 | |||||||||
Domain Homologous to E6-AP Carboxyl Terminus with; E3 ubiquitin-protein ligases. Can bind to E2 enzymes. Pssm-ID: 214523 Cd Length: 328 Bit Score: 512.93 E-value: 9.84e-177
|
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| HUL4 | COG5021 | Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
331-870 | 1.06e-173 | |||||||||
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 525.10 E-value: 1.06e-173
|
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| HECT | pfam00632 | HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
565-868 | 8.06e-129 | |||||||||
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus. Pssm-ID: 459880 Cd Length: 304 Bit Score: 388.51 E-value: 8.06e-129
|
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| C2_E3_ubiquitin_ligase | cd04021 | C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation ... |
17-142 | 2.08e-53 | |||||||||
C2 domain present in E3 ubiquitin ligase; E3 ubiquitin ligase is part of the ubiquitylation mechanism responsible for controlling surface expression of membrane proteins. The sequential action of several enzymes are involved: ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin-protein ligase E3 which is responsible for substrate recognition and promoting the transfer of ubiquitin to the target protein. E3 ubiquitin ligase is composed of an N-terminal C2 domain, 4 WW domains, and a HECTc domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175988 [Multi-domain] Cd Length: 125 Bit Score: 181.32 E-value: 2.08e-53
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 | 1.21e-12 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 62.52 E-value: 1.21e-12
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
407-435 | 2.64e-12 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 61.37 E-value: 2.64e-12
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
406-436 | 3.98e-12 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 61.08 E-value: 3.98e-12
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
408-436 | 8.68e-12 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 60.23 E-value: 8.68e-12
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 | 1.76e-11 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 59.06 E-value: 1.76e-11
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
331-362 | 2.89e-11 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 58.77 E-value: 2.89e-11
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
333-362 | 5.50e-11 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.92 E-value: 5.50e-11
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
302-331 | 6.83e-11 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 57.61 E-value: 6.83e-11
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
303-331 | 8.29e-11 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 57.15 E-value: 8.29e-11
|
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
19-115 | 4.44e-09 | |||||||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 54.42 E-value: 4.44e-09
|
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| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
447-477 | 9.31e-09 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 51.37 E-value: 9.31e-09
|
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| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
446-475 | 6.53e-08 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.04 E-value: 6.53e-08
|
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| PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
297-381 | 1.07e-07 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 55.47 E-value: 1.07e-07
|
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| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
446-477 | 1.21e-07 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 48.37 E-value: 1.21e-07
|
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| Treacle | pfam03546 | Treacher Collins syndrome protein Treacle; |
155-304 | 7.69e-05 | |||||||||
Treacher Collins syndrome protein Treacle; Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 46.22 E-value: 7.69e-05
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| PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
149-299 | 2.18e-04 | |||||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 2.18e-04
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| PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
156-301 | 7.24e-04 | |||||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 43.30 E-value: 7.24e-04
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| C2_SRC2_like | cd04051 | C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production ... |
20-131 | 3.61e-03 | |||||||||
C2 domain present in Soybean genes Regulated by Cold 2 (SRC2)-like proteins; SRC2 production is a response to pathogen infiltration. The initial response of increased Ca2+ concentrations are coupled to downstream signal transduction pathways via calcium binding proteins. SRC2 contains a single C2 domain which localizes to the plasma membrane and is involved in Ca2+ dependent protein binding. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 176016 [Multi-domain] Cd Length: 125 Bit Score: 38.37 E-value: 3.61e-03
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