EH domain-containing protein 4 isoform X1 [Gallus gallus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| EHD | cd09913 | Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
64-304 | 1.76e-159 | |||||
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling. : Pssm-ID: 206740 Cd Length: 241 Bit Score: 453.65 E-value: 1.76e-159
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| DUF5600 | pfam18150 | Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ... |
293-398 | 3.99e-61 | |||||
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain. : Pssm-ID: 465667 Cd Length: 107 Bit Score: 196.68 E-value: 3.99e-61
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| EH | smart00027 | Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
442-535 | 4.45e-33 | |||||
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences. : Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 121.23 E-value: 4.45e-33
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| EHD_N | pfam16880 | N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ... |
28-60 | 3.82e-13 | |||||
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins. : Pssm-ID: 465295 [Multi-domain] Cd Length: 33 Bit Score: 63.19 E-value: 3.82e-13
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| Name | Accession | Description | Interval | E-value | |||||
| EHD | cd09913 | Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
64-304 | 1.76e-159 | |||||
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling. Pssm-ID: 206740 Cd Length: 241 Bit Score: 453.65 E-value: 1.76e-159
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| DUF5600 | pfam18150 | Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ... |
293-398 | 3.99e-61 | |||||
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain. Pssm-ID: 465667 Cd Length: 107 Bit Score: 196.68 E-value: 3.99e-61
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| EH | smart00027 | Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
442-535 | 4.45e-33 | |||||
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences. Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 121.23 E-value: 4.45e-33
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| EH | cd00052 | Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
452-516 | 8.99e-22 | |||||
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs. Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 88.82 E-value: 8.99e-22
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| Dynamin_N | pfam00350 | Dynamin family; |
65-225 | 1.43e-21 | |||||
Dynamin family; Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 91.52 E-value: 1.43e-21
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| EF-hand_4 | pfam12763 | Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
441-533 | 1.32e-17 | |||||
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species. Pssm-ID: 289529 Cd Length: 104 Bit Score: 78.18 E-value: 1.32e-17
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| EHD_N | pfam16880 | N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ... |
28-60 | 3.82e-13 | |||||
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins. Pssm-ID: 465295 [Multi-domain] Cd Length: 33 Bit Score: 63.19 E-value: 3.82e-13
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| Name | Accession | Description | Interval | E-value | |||||
| EHD | cd09913 | Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ... |
64-304 | 1.76e-159 | |||||
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling. Pssm-ID: 206740 Cd Length: 241 Bit Score: 453.65 E-value: 1.76e-159
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| DUF5600 | pfam18150 | Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ... |
293-398 | 3.99e-61 | |||||
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain. Pssm-ID: 465667 Cd Length: 107 Bit Score: 196.68 E-value: 3.99e-61
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| EH | smart00027 | Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ... |
442-535 | 4.45e-33 | |||||
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences. Pssm-ID: 197477 [Multi-domain] Cd Length: 96 Bit Score: 121.23 E-value: 4.45e-33
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| EH | cd00052 | Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
452-516 | 8.99e-22 | |||||
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs. Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 88.82 E-value: 8.99e-22
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| Dynamin_N | pfam00350 | Dynamin family; |
65-225 | 1.43e-21 | |||||
Dynamin family; Pssm-ID: 459775 [Multi-domain] Cd Length: 168 Bit Score: 91.52 E-value: 1.43e-21
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| EF-hand_4 | pfam12763 | Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ... |
441-533 | 1.32e-17 | |||||
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species. Pssm-ID: 289529 Cd Length: 104 Bit Score: 78.18 E-value: 1.32e-17
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| EHD_N | pfam16880 | N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ... |
28-60 | 3.82e-13 | |||||
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins. Pssm-ID: 465295 [Multi-domain] Cd Length: 33 Bit Score: 63.19 E-value: 3.82e-13
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
66-248 | 3.74e-11 | |||||
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions. Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 61.70 E-value: 3.74e-11
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| DLP_2 | cd09912 | Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
65-233 | 4.13e-06 | |||||
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner. Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 47.16 E-value: 4.13e-06
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| MMR_HSR1 | pfam01926 | 50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
65-224 | 5.30e-06 | |||||
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide. Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 45.30 E-value: 5.30e-06
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
150-232 | 6.53e-04 | |||||
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 40.69 E-value: 6.53e-04
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| YfjP | cd11383 | YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
150-228 | 3.96e-03 | |||||
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 37.70 E-value: 3.96e-03
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