excalibur calcium-binding domain-containing protein, partial [Bacillus thuringiensis]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Excalibur | pfam05901 | Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ... |
219-254 | 6.07e-19 | |||
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognized and the evolution of EF-hand-like domains is probably more complex than previously appreciated. : Pssm-ID: 428664 Cd Length: 36 Bit Score: 77.12 E-value: 6.07e-19
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MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
151-194 | 1.74e-07 | |||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. : Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.27 E-value: 1.74e-07
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tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
91-194 | 1.97e-05 | |||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] : Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 1.97e-05
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COG4652 super family | cl47356 | Uncharacterized conserved protein, DUF1430 domain [Function unknown]; |
1-115 | 8.79e-05 | |||
Uncharacterized conserved protein, DUF1430 domain [Function unknown]; The actual alignment was detected with superfamily member COG4652: Pssm-ID: 443690 [Multi-domain] Cd Length: 583 Bit Score: 43.16 E-value: 8.79e-05
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Name | Accession | Description | Interval | E-value | |||
Excalibur | pfam05901 | Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ... |
219-254 | 6.07e-19 | |||
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognized and the evolution of EF-hand-like domains is probably more complex than previously appreciated. Pssm-ID: 428664 Cd Length: 36 Bit Score: 77.12 E-value: 6.07e-19
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Excalibur | smart00894 | Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ... |
218-254 | 4.01e-18 | |||
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated. Pssm-ID: 214891 [Multi-domain] Cd Length: 37 Bit Score: 75.00 E-value: 4.01e-18
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MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
151-194 | 1.74e-07 | |||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.27 E-value: 1.74e-07
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
151-191 | 1.29e-06 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.29e-06
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tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
91-194 | 1.97e-05 | |||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 1.97e-05
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
91-192 | 3.36e-05 | |||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 3.36e-05
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COG4652 | COG4652 | Uncharacterized conserved protein, DUF1430 domain [Function unknown]; |
1-115 | 8.79e-05 | |||
Uncharacterized conserved protein, DUF1430 domain [Function unknown]; Pssm-ID: 443690 [Multi-domain] Cd Length: 583 Bit Score: 43.16 E-value: 8.79e-05
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glyco_rpt_poly | TIGR04370 | oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ... |
2-111 | 3.68e-04 | |||
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 275163 [Multi-domain] Cd Length: 392 Bit Score: 41.38 E-value: 3.68e-04
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MFS_TRI12_like | cd06179 | Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; ... |
8-119 | 9.83e-04 | |||
Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; This family includes Fusarium sporotrichioides trichothecene efflux pump (TRI12), which may play a role in F. sporotrichioides self-protection against trichothecenes. TRI12 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Pssm-ID: 340868 [Multi-domain] Cd Length: 518 Bit Score: 39.92 E-value: 9.83e-04
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ABC2_membrane_3 | pfam12698 | ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
5-112 | 2.72e-03 | |||
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061. Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 38.53 E-value: 2.72e-03
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tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
151-194 | 3.83e-03 | |||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 37.90 E-value: 3.83e-03
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Name | Accession | Description | Interval | E-value | |||
Excalibur | pfam05901 | Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ... |
219-254 | 6.07e-19 | |||
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognized and the evolution of EF-hand-like domains is probably more complex than previously appreciated. Pssm-ID: 428664 Cd Length: 36 Bit Score: 77.12 E-value: 6.07e-19
|
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Excalibur | smart00894 | Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus ... |
218-254 | 4.01e-18 | |||
Excalibur calcium-binding domain; Extracellular Ca2+-dependent nuclease YokF from Bacillus subtilis and several other surface-exposed proteins from diverse bacteria are encoded in the genomes in two paralogous forms that differ by a ~45 amino acid fragment, which comprises a novel conserved domain. Sequence analysis of this domain revealed a conserved DxDxDGxxCE motif, which is strikingly similar to the Ca2+-binding loop of the calmodulin-like EF-hand domains, suggesting an evolutionary relationship between them. Functions of many of the other proteins in which the novel domain, named Excalibur (extracellular calcium-binding region), is found, as well as a structural model of its conserved motif are consistent with the notion that the Excalibur domain binds calcium. This domain is but one more example of the diversity of structural contexts surrounding the EF-hand-like calcium-binding loop in bacteria. This loop is thus more widespread than hitherto recognised and the evolution of EF-hand-like domains is probably more complex than previously appreciated. Pssm-ID: 214891 [Multi-domain] Cd Length: 37 Bit Score: 75.00 E-value: 4.01e-18
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MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
151-194 | 1.74e-07 | |||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.27 E-value: 1.74e-07
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
151-191 | 1.29e-06 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.29e-06
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
116-191 | 2.39e-06 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.39e-06
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MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
152-193 | 6.11e-06 | |||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 45.03 E-value: 6.11e-06
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
151-194 | 1.13e-05 | |||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 1.13e-05
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
111-194 | 1.22e-05 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.22e-05
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
151-191 | 1.24e-05 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.24e-05
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tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
91-194 | 1.97e-05 | |||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 1.97e-05
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DUF4670 | pfam15709 | Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
151-194 | 2.06e-05 | |||
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length. Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 2.06e-05
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
151-194 | 3.02e-05 | |||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 3.02e-05
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tolA | PRK09510 | cell envelope integrity inner membrane protein TolA; Provisional |
91-192 | 3.36e-05 | |||
cell envelope integrity inner membrane protein TolA; Provisional Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 3.36e-05
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tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
67-193 | 4.00e-05 | |||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 4.00e-05
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
114-194 | 5.50e-05 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.50e-05
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
112-194 | 7.14e-05 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.14e-05
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
151-194 | 8.54e-05 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.54e-05
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COG4652 | COG4652 | Uncharacterized conserved protein, DUF1430 domain [Function unknown]; |
1-115 | 8.79e-05 | |||
Uncharacterized conserved protein, DUF1430 domain [Function unknown]; Pssm-ID: 443690 [Multi-domain] Cd Length: 583 Bit Score: 43.16 E-value: 8.79e-05
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
151-191 | 9.17e-05 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.17e-05
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DUF4670 | pfam15709 | Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
151-194 | 1.27e-04 | |||
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length. Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 1.27e-04
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MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
151-192 | 2.18e-04 | |||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 2.18e-04
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glyco_rpt_poly | TIGR04370 | oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ... |
2-111 | 3.68e-04 | |||
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 275163 [Multi-domain] Cd Length: 392 Bit Score: 41.38 E-value: 3.68e-04
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
114-191 | 5.15e-04 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.15e-04
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
114-191 | 6.05e-04 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.05e-04
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MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
151-196 | 7.69e-04 | |||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 7.69e-04
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MFS_TRI12_like | cd06179 | Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; ... |
8-119 | 9.83e-04 | |||
Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; This family includes Fusarium sporotrichioides trichothecene efflux pump (TRI12), which may play a role in F. sporotrichioides self-protection against trichothecenes. TRI12 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Pssm-ID: 340868 [Multi-domain] Cd Length: 518 Bit Score: 39.92 E-value: 9.83e-04
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
151-191 | 1.06e-03 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.06e-03
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
124-191 | 1.24e-03 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.24e-03
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NosY | COG1277 | ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
39-112 | 1.49e-03 | |||
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 38.64 E-value: 1.49e-03
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PLN02316 | PLN02316 | synthase/transferase |
154-194 | 1.55e-03 | |||
synthase/transferase Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 39.47 E-value: 1.55e-03
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matE | TIGR00797 | putative efflux protein, MATE family; The Multi Antimicrobial Extrusion (MATE) Family (TC 2.A. ... |
5-110 | 2.13e-03 | |||
putative efflux protein, MATE family; The Multi Antimicrobial Extrusion (MATE) Family (TC 2.A.66) The MATE family consists of probable efflux proteins including a functionally characterized multi drug efflux system from Vibrio parahaemolyticus, a putative ethionine resistance protein of Saccharomyces cerevisiae, and the functionally uncharacterized DNA damage-inducible protein F (DinF) of E. coli. These proteins have 12 probable TMS. [Transport and binding proteins, Other] Pssm-ID: 273273 [Multi-domain] Cd Length: 342 Bit Score: 38.77 E-value: 2.13e-03
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ABC2_membrane_3 | pfam12698 | ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
5-112 | 2.72e-03 | |||
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061. Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 38.53 E-value: 2.72e-03
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rne | PRK10811 | ribonuclease E; Reviewed |
128-192 | 2.78e-03 | |||
ribonuclease E; Reviewed Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 38.87 E-value: 2.78e-03
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
112-191 | 2.97e-03 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 2.97e-03
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DUF5401 | pfam17380 | Family of unknown function (DUF5401); This is a family of unknown function found in ... |
151-194 | 3.81e-03 | |||
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea. Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.18 E-value: 3.81e-03
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tolA_full | TIGR02794 | TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
151-194 | 3.83e-03 | |||
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis] Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 37.90 E-value: 3.83e-03
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7tmB2_Adhesion | cd15040 | adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ... |
1-110 | 4.08e-03 | |||
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Pssm-ID: 320168 [Multi-domain] Cd Length: 253 Bit Score: 37.55 E-value: 4.08e-03
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DUF4670 | pfam15709 | Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
151-194 | 4.24e-03 | |||
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length. Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 38.01 E-value: 4.24e-03
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DUF5401 | pfam17380 | Family of unknown function (DUF5401); This is a family of unknown function found in ... |
116-194 | 4.64e-03 | |||
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea. Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.18 E-value: 4.64e-03
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DUF4064 | pfam13273 | Protein of unknown function (DUF4064); |
1-104 | 5.75e-03 | |||
Protein of unknown function (DUF4064); Pssm-ID: 433076 Cd Length: 102 Bit Score: 35.36 E-value: 5.75e-03
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DUF4670 | pfam15709 | Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
151-194 | 6.45e-03 | |||
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length. Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 37.62 E-value: 6.45e-03
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PTZ00121 | PTZ00121 | MAEBL; Provisional |
114-191 | 7.75e-03 | |||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.43 E-value: 7.75e-03
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Casc1_N | pfam15927 | Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
156-194 | 8.02e-03 | |||
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important. Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 36.57 E-value: 8.02e-03
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Blast search parameters | ||||
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