lymphocyte inhibitory factor A [Citrobacter rodentium ICC168]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||||||||||||||||||||||
Efa1_rel_toxin super family | cl40410 | LifA/Efa1-related large cytotoxin; Members of this family are large and almost certainly ... |
46-3188 | 0e+00 | ||||||||||||||||||||||||||||||||||||||||||
LifA/Efa1-related large cytotoxin; Members of this family are large and almost certainly multifunctional proteins found in various pathogens from genus Chlamydia, about 3000 amino acids in size and related to lymphostatin (Efa1/LifA) from enteropathogenic Escherichia coli. Roles have been suggested for Efa1 (EHEC factor for adherence) in adhesion, so some members have been annotated as adherence proteins rather than cytotoxins. The actual alignment was detected with superfamily member NF033479: Pssm-ID: 468042 [Multi-domain] Cd Length: 3223 Bit Score: 2826.23 E-value: 0e+00
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Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||||||||||||||||||||||
Efa1_rel_toxin | NF033479 | LifA/Efa1-related large cytotoxin; Members of this family are large and almost certainly ... |
46-3188 | 0e+00 | ||||||||||||||||||||||||||||||||||||||||||
LifA/Efa1-related large cytotoxin; Members of this family are large and almost certainly multifunctional proteins found in various pathogens from genus Chlamydia, about 3000 amino acids in size and related to lymphostatin (Efa1/LifA) from enteropathogenic Escherichia coli. Roles have been suggested for Efa1 (EHEC factor for adherence) in adhesion, so some members have been annotated as adherence proteins rather than cytotoxins. Pssm-ID: 468042 [Multi-domain] Cd Length: 3223 Bit Score: 2826.23 E-value: 0e+00
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DUF3491 | pfam11996 | Protein of unknown function (DUF3491); This family of proteins is functionally uncharacterized. ... |
2167-3093 | 0e+00 | ||||||||||||||||||||||||||||||||||||||||||
Protein of unknown function (DUF3491); This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 286 to 3225 amino acids in length. This protein is found associated with pfam04488. This protein is found associated with pfam04488. Pssm-ID: 314813 Cd Length: 946 Bit Score: 1453.83 E-value: 0e+00
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yopT_cys_prot | TIGR01586 | cysteine protease domain, YopT-type; The model represents a cysteine protease domain found in ... |
1451-1630 | 9.26e-42 | ||||||||||||||||||||||||||||||||||||||||||
cysteine protease domain, YopT-type; The model represents a cysteine protease domain found in proteins of bacteria that include plant pathogens (Pseudomonas syringae), root nodule bacteria, and intracellular pathogens (e.g. Yersinia pestis, Haemophilus ducreyi, Pasteurella multocida, Chlamydia trachomatis) of animal hosts. The domain features a catalytic triad of Cys, His, and Asp. Sequences can be extremely divergent outside of a few well-conserved motifs, and additional members may exist that are detected by this model. YopT, a virulence effector protein of Yersinia pestis, cleaves and releases host cell Rho GTPases from the membrane, thereby disrupting the actin cytoskeleton. Members of the family from pathogenic bacteria are likely to be pathogenesis factors. [Cellular processes, Pathogenesis] Pssm-ID: 273706 Cd Length: 196 Bit Score: 153.03 E-value: 9.26e-42
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C58_PaToxP-like | cd20495 | peptidase C58 domain of Photorhabdus asymbiotica toxin PaTox and LifA/Efa1-related large ... |
1450-1615 | 7.27e-26 | ||||||||||||||||||||||||||||||||||||||||||
peptidase C58 domain of Photorhabdus asymbiotica toxin PaTox and LifA/Efa1-related large cytotoxin, and similar proteins; This subfamily includes the cysteine protease domain of Photorhabdus asymbiotica toxin PaTox, a large virulence-associated multifunctional protein toxin. This domain is similar to AvrPphB protease found in Pseudomonas syringae, a C58 protease. Mutation studies show that this domain enhances cytotoxic effects of the toxin, and therefore is essential for full PaTox activity. Also included in this family is the enteropathogenic Escherichia coli (EPEC) factor for adherence/lymphocyte activation inhibitor (efa1/lifA) gene which is strongly associated with diarrhea. Efa1/LifA proteins are important for A/E lesion formation efficiency in EPEC strains lacking multiple effectors. This domain contains the invariant C/H/D residues conserved in the C58/YopT family. Pssm-ID: 410776 Cd Length: 179 Bit Score: 107.06 E-value: 7.27e-26
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OCH1 | COG3774 | Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis]; |
521-548 | 9.86e-06 | ||||||||||||||||||||||||||||||||||||||||||
Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442988 [Multi-domain] Cd Length: 136 Bit Score: 47.58 E-value: 9.86e-06
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Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||||||||||||||||||||||
Efa1_rel_toxin | NF033479 | LifA/Efa1-related large cytotoxin; Members of this family are large and almost certainly ... |
46-3188 | 0e+00 | ||||||||||||||||||||||||||||||||||||||||||
LifA/Efa1-related large cytotoxin; Members of this family are large and almost certainly multifunctional proteins found in various pathogens from genus Chlamydia, about 3000 amino acids in size and related to lymphostatin (Efa1/LifA) from enteropathogenic Escherichia coli. Roles have been suggested for Efa1 (EHEC factor for adherence) in adhesion, so some members have been annotated as adherence proteins rather than cytotoxins. Pssm-ID: 468042 [Multi-domain] Cd Length: 3223 Bit Score: 2826.23 E-value: 0e+00
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DUF3491 | pfam11996 | Protein of unknown function (DUF3491); This family of proteins is functionally uncharacterized. ... |
2167-3093 | 0e+00 | ||||||||||||||||||||||||||||||||||||||||||
Protein of unknown function (DUF3491); This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 286 to 3225 amino acids in length. This protein is found associated with pfam04488. This protein is found associated with pfam04488. Pssm-ID: 314813 Cd Length: 946 Bit Score: 1453.83 E-value: 0e+00
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TcdA_TcdB | pfam12919 | TcdA/TcdB catalytic glycosyltransferase domain; This domain represents the N-terminal ... |
300-740 | 7.37e-69 | ||||||||||||||||||||||||||||||||||||||||||
TcdA/TcdB catalytic glycosyltransferase domain; This domain represents the N-terminal glycosyltransferase from a set of toxins found in some bacteria. This domain in TcdB glycosylates the host RhoA protein. Pssm-ID: 372382 [Multi-domain] Cd Length: 382 Bit Score: 238.20 E-value: 7.37e-69
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yopT_cys_prot | TIGR01586 | cysteine protease domain, YopT-type; The model represents a cysteine protease domain found in ... |
1451-1630 | 9.26e-42 | ||||||||||||||||||||||||||||||||||||||||||
cysteine protease domain, YopT-type; The model represents a cysteine protease domain found in proteins of bacteria that include plant pathogens (Pseudomonas syringae), root nodule bacteria, and intracellular pathogens (e.g. Yersinia pestis, Haemophilus ducreyi, Pasteurella multocida, Chlamydia trachomatis) of animal hosts. The domain features a catalytic triad of Cys, His, and Asp. Sequences can be extremely divergent outside of a few well-conserved motifs, and additional members may exist that are detected by this model. YopT, a virulence effector protein of Yersinia pestis, cleaves and releases host cell Rho GTPases from the membrane, thereby disrupting the actin cytoskeleton. Members of the family from pathogenic bacteria are likely to be pathogenesis factors. [Cellular processes, Pathogenesis] Pssm-ID: 273706 Cd Length: 196 Bit Score: 153.03 E-value: 9.26e-42
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C58_PaToxP-like | cd20495 | peptidase C58 domain of Photorhabdus asymbiotica toxin PaTox and LifA/Efa1-related large ... |
1450-1615 | 7.27e-26 | ||||||||||||||||||||||||||||||||||||||||||
peptidase C58 domain of Photorhabdus asymbiotica toxin PaTox and LifA/Efa1-related large cytotoxin, and similar proteins; This subfamily includes the cysteine protease domain of Photorhabdus asymbiotica toxin PaTox, a large virulence-associated multifunctional protein toxin. This domain is similar to AvrPphB protease found in Pseudomonas syringae, a C58 protease. Mutation studies show that this domain enhances cytotoxic effects of the toxin, and therefore is essential for full PaTox activity. Also included in this family is the enteropathogenic Escherichia coli (EPEC) factor for adherence/lymphocyte activation inhibitor (efa1/lifA) gene which is strongly associated with diarrhea. Efa1/LifA proteins are important for A/E lesion formation efficiency in EPEC strains lacking multiple effectors. This domain contains the invariant C/H/D residues conserved in the C58/YopT family. Pssm-ID: 410776 Cd Length: 179 Bit Score: 107.06 E-value: 7.27e-26
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TcdB_N | pfam12918 | TcdB toxin N-terminal helical domain; This is a short helical bundle domain found associated ... |
205-266 | 1.16e-15 | ||||||||||||||||||||||||||||||||||||||||||
TcdB toxin N-terminal helical domain; This is a short helical bundle domain found associated with the catalytic domain of the TcdB toxin from C. difficile. The function of this domain is unknown, but it may be involved in substrate recognition. Pssm-ID: 403966 [Multi-domain] Cd Length: 66 Bit Score: 73.56 E-value: 1.16e-15
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Gly_transf_sug | pfam04488 | Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short ... |
458-569 | 4.65e-12 | ||||||||||||||||||||||||||||||||||||||||||
Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short conserved motif found in many families of glycosyltransferases, which add a range of different sugars to other sugars, phosphates and proteins. DXD-containing glycosyltransferases all use nucleoside diphosphate sugars as donors and require divalent cations, usually manganese. The DXD motif is expected to play a carbohydrate binding role in sugar-nucleoside diphosphate and manganese dependent glycosyltransferases. Pssm-ID: 398274 [Multi-domain] Cd Length: 93 Bit Score: 64.28 E-value: 4.65e-12
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235kDa-fam | TIGR01612 | reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
141-483 | 2.30e-07 | ||||||||||||||||||||||||||||||||||||||||||
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii. Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.37 E-value: 2.30e-07
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235kDa-fam | TIGR01612 | reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
16-1127 | 4.33e-06 | ||||||||||||||||||||||||||||||||||||||||||
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii. Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 4.33e-06
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OCH1 | COG3774 | Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis]; |
521-548 | 9.86e-06 | ||||||||||||||||||||||||||||||||||||||||||
Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442988 [Multi-domain] Cd Length: 136 Bit Score: 47.58 E-value: 9.86e-06
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235kDa-fam | TIGR01612 | reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
17-509 | 1.11e-05 | ||||||||||||||||||||||||||||||||||||||||||
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii. Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 1.11e-05
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Blast search parameters | ||||
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