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NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform WWP2-FL [Homo sapiens]
C2_E3_ubiquitin_ligase and HECTc domain-containing protein( domain architecture ID 10134116)
protein containing domains C2_E3_ubiquitin_ligase, PHA03247, WW, and HECTc
List of domain hits
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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: 529.83 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 | 3.93e-54 | ||||||
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: 183.25 E-value: 3.93e-54
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 | 1.72e-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: 62.14 E-value: 1.72e-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 | 3.75e-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: 60.98 E-value: 3.75e-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 | 2.40e-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: 58.67 E-value: 2.40e-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 | 1.26e-08 | ||||||
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: 50.99 E-value: 1.26e-08
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PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
164-343 | 3.58e-05 | ||||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 3.58e-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: 529.83 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 | 5.83e-178 | |||||||||
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: 516.02 E-value: 5.83e-178
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HUL4 | COG5021 | Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
331-870 | 3.16e-175 | |||||||||
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 528.95 E-value: 3.16e-175
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HECT | pfam00632 | HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
565-868 | 3.65e-128 | |||||||||
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus. Pssm-ID: 459880 Cd Length: 304 Bit Score: 386.97 E-value: 3.65e-128
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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 | 3.93e-54 | |||||||||
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: 183.25 E-value: 3.93e-54
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 | 1.72e-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: 62.14 E-value: 1.72e-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 | 3.75e-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: 60.98 E-value: 3.75e-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 | 5.88e-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: 60.69 E-value: 5.88e-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 | 1.26e-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: 59.46 E-value: 1.26e-11
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 | 2.40e-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: 58.67 E-value: 2.40e-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 | 4.19e-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: 58.00 E-value: 4.19e-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 | 7.82e-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: 57.54 E-value: 7.82e-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 | 9.80e-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: 57.23 E-value: 9.80e-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 | 1.14e-10 | |||||||||
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: 56.77 E-value: 1.14e-10
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C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
19-115 | 4.57e-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: 4.57e-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 | 1.26e-08 | |||||||||
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: 50.99 E-value: 1.26e-08
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
446-475 | 8.42e-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: 48.66 E-value: 8.42e-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 | 1.61e-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: 47.98 E-value: 1.61e-07
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
164-343 | 3.58e-05 | |||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 3.58e-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: 529.83 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 | 5.83e-178 | |||||||||
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: 516.02 E-value: 5.83e-178
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HUL4 | COG5021 | Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; |
331-870 | 3.16e-175 | |||||||||
Ubiquitin-protein ligase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227354 [Multi-domain] Cd Length: 872 Bit Score: 528.95 E-value: 3.16e-175
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HECT | pfam00632 | HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl ... |
565-868 | 3.65e-128 | |||||||||
HECT-domain (ubiquitin-transferase); The name HECT comes from Homologous to the E6-AP Carboxyl Terminus. Pssm-ID: 459880 Cd Length: 304 Bit Score: 386.97 E-value: 3.65e-128
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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 | 3.93e-54 | |||||||||
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: 183.25 E-value: 3.93e-54
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
332-361 | 1.72e-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: 62.14 E-value: 1.72e-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 | 3.75e-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: 60.98 E-value: 3.75e-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 | 5.88e-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: 60.69 E-value: 5.88e-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 | 1.26e-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: 59.46 E-value: 1.26e-11
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
302-331 | 2.40e-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: 58.67 E-value: 2.40e-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 | 4.19e-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: 58.00 E-value: 4.19e-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 | 7.82e-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: 57.54 E-value: 7.82e-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 | 9.80e-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: 57.23 E-value: 9.80e-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 | 1.14e-10 | |||||||||
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: 56.77 E-value: 1.14e-10
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C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
19-115 | 4.57e-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: 4.57e-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 | 1.26e-08 | |||||||||
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: 50.99 E-value: 1.26e-08
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PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
297-381 | 8.26e-08 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 55.86 E-value: 8.26e-08
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WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
446-475 | 8.42e-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: 48.66 E-value: 8.42e-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 | 1.61e-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: 47.98 E-value: 1.61e-07
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
164-343 | 3.58e-05 | |||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.01 E-value: 3.58e-05
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
135-345 | 9.71e-05 | |||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 9.71e-05
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PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
172-299 | 1.22e-04 | |||||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.00 E-value: 1.22e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
149-319 | 3.04e-04 | |||||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.59 E-value: 3.04e-04
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PRK10905 | PRK10905 | cell division protein DamX; Validated |
198-301 | 5.61e-04 | |||||||||
cell division protein DamX; Validated Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 43.00 E-value: 5.61e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
163-305 | 6.54e-04 | |||||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 6.54e-04
|
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
151-300 | 6.71e-04 | |||||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 6.71e-04
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PRK10118 | PRK10118 | flagellar hook length control protein FliK; |
199-308 | 9.17e-04 | |||||||||
flagellar hook length control protein FliK; Pssm-ID: 236652 [Multi-domain] Cd Length: 408 Bit Score: 42.55 E-value: 9.17e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
142-308 | 1.34e-03 | |||||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 1.34e-03
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PHA03291 | PHA03291 | envelope glycoprotein I; Provisional |
239-304 | 1.60e-03 | |||||||||
envelope glycoprotein I; Provisional Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 41.86 E-value: 1.60e-03
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Blast search parameters | ||||
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