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epsin-1 isoform d [Homo sapiens]
ENTH domain-containing protein; epsin; epsin( domain architecture ID 13016790)
ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin family proteins that play an important role as accessory proteins in clathrin-mediated endocytosis; epsin plays an important role as accessory proteins in clathrin-mediated endocytosis; epsin plays an important role as accessory proteins in clathrin-mediated endocytosis
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
ENTH_Epsin | cd16990 | Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ... |
19-142 | 4.74e-99 | ||||
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. : Pssm-ID: 340787 Cd Length: 124 Bit Score: 296.19 E-value: 4.74e-99
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PRK07764 super family | cl35613 | DNA polymerase III subunits gamma and tau; Validated |
265-453 | 3.79e-08 | ||||
DNA polymerase III subunits gamma and tau; Validated The actual alignment was detected with superfamily member PRK07764: Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 3.79e-08
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Name | Accession | Description | Interval | E-value | ||||
ENTH_Epsin | cd16990 | Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ... |
19-142 | 4.74e-99 | ||||
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340787 Cd Length: 124 Bit Score: 296.19 E-value: 4.74e-99
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ENTH | pfam01417 | ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ... |
17-140 | 4.72e-73 | ||||
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown. Pssm-ID: 426255 Cd Length: 124 Bit Score: 228.98 E-value: 4.72e-73
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ENTH | smart00273 | Epsin N-terminal homology (ENTH) domain; |
18-144 | 1.22e-52 | ||||
Epsin N-terminal homology (ENTH) domain; Pssm-ID: 214594 Cd Length: 127 Bit Score: 175.51 E-value: 1.22e-52
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
265-453 | 3.79e-08 | ||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 3.79e-08
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MSCRAMM_ClfB | NF033845 | MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial ... |
294-407 | 4.88e-05 | ||||
MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif. Pssm-ID: 468203 [Multi-domain] Cd Length: 871 Bit Score: 46.48 E-value: 4.88e-05
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FAP | pfam07174 | Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
300-396 | 7.51e-03 | ||||
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix. Pssm-ID: 429334 Cd Length: 301 Bit Score: 38.75 E-value: 7.51e-03
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Name | Accession | Description | Interval | E-value | |||||
ENTH_Epsin | cd16990 | Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ... |
19-142 | 4.74e-99 | |||||
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340787 Cd Length: 124 Bit Score: 296.19 E-value: 4.74e-99
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ENTH | pfam01417 | ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ... |
17-140 | 4.72e-73 | |||||
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown. Pssm-ID: 426255 Cd Length: 124 Bit Score: 228.98 E-value: 4.72e-73
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ENTH_Ent1_Ent2 | cd16991 | Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ... |
17-144 | 2.00e-70 | |||||
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340788 Cd Length: 132 Bit Score: 222.53 E-value: 2.00e-70
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ENTH | cd03571 | Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ... |
20-136 | 2.04e-65 | |||||
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340772 Cd Length: 117 Bit Score: 208.91 E-value: 2.04e-65
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ENTH_EpsinR | cd16989 | Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ... |
20-147 | 2.57e-60 | |||||
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340786 Cd Length: 130 Bit Score: 195.97 E-value: 2.57e-60
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ENTH | smart00273 | Epsin N-terminal homology (ENTH) domain; |
18-144 | 1.22e-52 | |||||
Epsin N-terminal homology (ENTH) domain; Pssm-ID: 214594 Cd Length: 127 Bit Score: 175.51 E-value: 1.22e-52
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ENTH_Ent3 | cd16992 | Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ... |
21-139 | 6.08e-46 | |||||
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340789 Cd Length: 121 Bit Score: 157.61 E-value: 6.08e-46
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VHS_ENTH_ANTH | cd00197 | VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ... |
20-136 | 6.64e-41 | |||||
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH domain-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340764 Cd Length: 115 Bit Score: 143.72 E-value: 6.64e-41
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ENTH_Ent4 | cd16994 | Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ... |
20-138 | 1.28e-21 | |||||
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340791 Cd Length: 126 Bit Score: 90.43 E-value: 1.28e-21
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ENTH_Ent5 | cd16993 | Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ... |
21-145 | 9.52e-09 | |||||
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340790 Cd Length: 158 Bit Score: 54.78 E-value: 9.52e-09
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
265-453 | 3.79e-08 | |||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 3.79e-08
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
267-525 | 6.34e-07 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.63 E-value: 6.34e-07
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
268-526 | 1.76e-06 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.48 E-value: 1.76e-06
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VHS | cd03561 | VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ... |
24-131 | 1.21e-05 | |||||
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking. Pssm-ID: 340765 Cd Length: 131 Bit Score: 44.95 E-value: 1.21e-05
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
261-432 | 2.37e-05 | |||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.18 E-value: 2.37e-05
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MSCRAMM_ClfB | NF033845 | MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial ... |
294-407 | 4.88e-05 | |||||
MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif. Pssm-ID: 468203 [Multi-domain] Cd Length: 871 Bit Score: 46.48 E-value: 4.88e-05
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
266-453 | 1.98e-04 | |||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 1.98e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
266-523 | 3.02e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 3.02e-04
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
265-526 | 6.44e-04 | |||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 6.44e-04
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
265-372 | 7.07e-04 | |||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 7.07e-04
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
265-442 | 7.11e-04 | |||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 7.11e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
266-379 | 7.12e-04 | |||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 7.12e-04
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
261-433 | 9.28e-04 | |||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.17 E-value: 9.28e-04
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kgd | PRK12270 | multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
262-365 | 2.92e-03 | |||||
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit; Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 40.64 E-value: 2.92e-03
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
263-374 | 7.38e-03 | |||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.20 E-value: 7.38e-03
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FAP | pfam07174 | Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
300-396 | 7.51e-03 | |||||
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix. Pssm-ID: 429334 Cd Length: 301 Bit Score: 38.75 E-value: 7.51e-03
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
277-390 | 8.11e-03 | |||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.20 E-value: 8.11e-03
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PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
265-381 | 8.58e-03 | |||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 38.93 E-value: 8.58e-03
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PRK10952 | PRK10952 | proline/glycine betaine ABC transporter permease ProW; |
292-327 | 9.27e-03 | |||||
proline/glycine betaine ABC transporter permease ProW; Pssm-ID: 236805 Cd Length: 355 Bit Score: 38.53 E-value: 9.27e-03
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