MAG: hypothetical protein H6866_09090 [Rhodospirillales bacterium]
SH3 domain-containing protein( domain architecture ID 11467360)
Src Homology 3 (SH3) domain-containing protein plays versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others; similar to Bacillus cereus antisigma factor
List of domain hits
Name | Accession | Description | Interval | E-value | |||
SH3 | COG3807 | SH3-like domain [Function unknown]; |
30-173 | 1.48e-67 | |||
SH3-like domain [Function unknown]; : Pssm-ID: 443020 [Multi-domain] Cd Length: 150 Bit Score: 202.44 E-value: 1.48e-67
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Name | Accession | Description | Interval | E-value | |||
SH3 | COG3807 | SH3-like domain [Function unknown]; |
30-173 | 1.48e-67 | |||
SH3-like domain [Function unknown]; Pssm-ID: 443020 [Multi-domain] Cd Length: 150 Bit Score: 202.44 E-value: 1.48e-67
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SH3_4 | pfam06347 | Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ... |
51-106 | 4.22e-12 | |||
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues. They are found in a great variety of intracellular or membrane-associated proteins, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteriztic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes. This family consists of several hypothetical bacterial proteins of unknown function, but that contain an SH-3 region. Family members include probable invasion-associated protein p60 that are conceptually translated from iap genes. The iap gene, which is regarded as a virulence-associated gene in L. monocytogenes, codes for a gene product that has murein-lytic activity and is involved in cell division. Pssm-ID: 428898 [Multi-domain] Cd Length: 56 Bit Score: 58.13 E-value: 4.22e-12
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SH3_and_anchor | TIGR04211 | SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
51-105 | 1.49e-04 | |||
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region. Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 40.38 E-value: 1.49e-04
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Name | Accession | Description | Interval | E-value | |||
SH3 | COG3807 | SH3-like domain [Function unknown]; |
30-173 | 1.48e-67 | |||
SH3-like domain [Function unknown]; Pssm-ID: 443020 [Multi-domain] Cd Length: 150 Bit Score: 202.44 E-value: 1.48e-67
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YgiM | COG3103 | Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family ... |
51-161 | 5.78e-15 | |||
Uncharacterized conserved protein YgiM, contains N-terminal SH3 domain, DUF1202 family [General function prediction only]; Pssm-ID: 442337 [Multi-domain] Cd Length: 119 Bit Score: 67.46 E-value: 5.78e-15
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SH3_4 | pfam06347 | Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ... |
51-106 | 4.22e-12 | |||
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues. They are found in a great variety of intracellular or membrane-associated proteins, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteriztic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes. This family consists of several hypothetical bacterial proteins of unknown function, but that contain an SH-3 region. Family members include probable invasion-associated protein p60 that are conceptually translated from iap genes. The iap gene, which is regarded as a virulence-associated gene in L. monocytogenes, codes for a gene product that has murein-lytic activity and is involved in cell division. Pssm-ID: 428898 [Multi-domain] Cd Length: 56 Bit Score: 58.13 E-value: 4.22e-12
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SH3_4 | pfam06347 | Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing ... |
115-168 | 3.00e-07 | |||
Bacterial SH3 domain; SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues. They are found in a great variety of intracellular or membrane-associated proteins, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteriztic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes. This family consists of several hypothetical bacterial proteins of unknown function, but that contain an SH-3 region. Family members include probable invasion-associated protein p60 that are conceptually translated from iap genes. The iap gene, which is regarded as a virulence-associated gene in L. monocytogenes, codes for a gene product that has murein-lytic activity and is involved in cell division. Pssm-ID: 428898 [Multi-domain] Cd Length: 56 Bit Score: 45.41 E-value: 3.00e-07
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SH3_3 | pfam08239 | Bacterial SH3 domain; |
54-105 | 2.15e-06 | |||
Bacterial SH3 domain; Pssm-ID: 462405 [Multi-domain] Cd Length: 54 Bit Score: 43.01 E-value: 2.15e-06
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SH3_and_anchor | TIGR04211 | SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
51-105 | 1.49e-04 | |||
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region. Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 40.38 E-value: 1.49e-04
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YraI | COG4991 | Uncharacterized conserved protein YraI [Function unknown]; |
116-161 | 1.92e-03 | |||
Uncharacterized conserved protein YraI [Function unknown]; Pssm-ID: 444015 [Multi-domain] Cd Length: 92 Bit Score: 35.81 E-value: 1.92e-03
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Blast search parameters | ||||
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