IQ motif and SEC7 domain-containing protein 3 isoform X4 [Homo sapiens]
Protein Classification
IQ motif and SEC7 domain-containing protein( domain architecture ID 11116401)
IQ motif and SEC7 domain-containing protein (IQSEC) contains an IQ domain that may bind calmodulin, a PH domain that may mediate membrane localization by binding of phosphoinositides, and a SEC7 domain that functions as a guanine-nucleotide-exchange factor (GEF) for members of the ARF class of small GTPases
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Sec7 | pfam01369 | Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ... |
348-536 | 7.75e-92 | ||||
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family. : Pssm-ID: 460178 Cd Length: 183 Bit Score: 287.43 E-value: 7.75e-92
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| IQ_SEC7_PH | pfam16453 | PH domain; This PH domain is found in IQ motif and SEC7 domain-containing proteins. |
558-687 | 3.35e-73 | ||||
PH domain; This PH domain is found in IQ motif and SEC7 domain-containing proteins. : Pssm-ID: 465120 Cd Length: 127 Bit Score: 235.64 E-value: 3.35e-73
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| LGT super family | cl00478 | Prolipoprotein diacylglyceryl transferase; |
141-250 | 1.70e-04 | ||||
Prolipoprotein diacylglyceryl transferase; The actual alignment was detected with superfamily member PRK13108: Pssm-ID: 469786 [Multi-domain] Cd Length: 460 Bit Score: 44.97 E-value: 1.70e-04
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| Name | Accession | Description | Interval | E-value | ||||
| Sec7 | pfam01369 | Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ... |
348-536 | 7.75e-92 | ||||
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family. Pssm-ID: 460178 Cd Length: 183 Bit Score: 287.43 E-value: 7.75e-92
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| Sec7 | cd00171 | Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ... |
348-536 | 2.81e-81 | ||||
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity. Pssm-ID: 238100 Cd Length: 185 Bit Score: 259.46 E-value: 2.81e-81
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| Sec7 | smart00222 | Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ... |
348-536 | 8.13e-74 | ||||
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors). Pssm-ID: 214569 [Multi-domain] Cd Length: 189 Bit Score: 239.88 E-value: 8.13e-74
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| IQ_SEC7_PH | pfam16453 | PH domain; This PH domain is found in IQ motif and SEC7 domain-containing proteins. |
558-687 | 3.35e-73 | ||||
PH domain; This PH domain is found in IQ motif and SEC7 domain-containing proteins. Pssm-ID: 465120 Cd Length: 127 Bit Score: 235.64 E-value: 3.35e-73
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| PH_IQSEC | cd13318 | IQ motif and SEC7 domain-containing protein family Pleckstrin homology domain; The IQSEC (also ... |
563-693 | 5.14e-69 | ||||
IQ motif and SEC7 domain-containing protein family Pleckstrin homology domain; The IQSEC (also called BRAG/Brefeldin A-resistant Arf-gunanine nucleotide exchange factor) family are a subset of Arf GEFs that have been shown to activate Arf6, which acts in the endocytic pathway to control the trafficking of a subset of cargo proteins including integrins and have key roles in the function and organization of distinct excitatory and inhibitory synapses in the retina. The family consists of 3 members: IQSEC1 (also called BRAG2/GEP100), IQSEC2 (also called BRAG1), and IQSEC3 (also called SynArfGEF, BRAG3, or KIAA1110). IQSEC1 interacts with clathrin and modulates cell adhesion by regulating integrin surface expression and in addition to Arf6, it also activates the class II Arfs, Arf4 and Arf5. Mutations in IQSEC2 cause non-syndromic X-linked intellectual disability as well as reduced activation of Arf substrates (Arf1, Arf6). IQSEC3 regulates Arf6 at inhibitory synapses and associates with the dystrophin-associated glycoprotein complex and S-SCAM. These members contains a IQ domain that may bind calmodulin, a PH domain that is thought to mediate membrane localization by binding of phosphoinositides, and a SEC7 domain that can promote GEF activity on ARF. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270128 Cd Length: 128 Bit Score: 224.50 E-value: 5.14e-69
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| PLN03076 | PLN03076 | ARF guanine nucleotide exchange factor (ARF-GEF); Provisional |
348-566 | 6.59e-51 | ||||
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional Pssm-ID: 215560 [Multi-domain] Cd Length: 1780 Bit Score: 195.04 E-value: 6.59e-51
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| PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
588-676 | 1.70e-05 | ||||
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 44.46 E-value: 1.70e-05
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| PRK13108 | PRK13108 | prolipoprotein diacylglyceryl transferase; Reviewed |
141-250 | 1.70e-04 | ||||
prolipoprotein diacylglyceryl transferase; Reviewed Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.97 E-value: 1.70e-04
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| Name | Accession | Description | Interval | E-value | ||||
| Sec7 | pfam01369 | Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ... |
348-536 | 7.75e-92 | ||||
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family. Pssm-ID: 460178 Cd Length: 183 Bit Score: 287.43 E-value: 7.75e-92
|
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| Sec7 | cd00171 | Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ... |
348-536 | 2.81e-81 | ||||
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity. Pssm-ID: 238100 Cd Length: 185 Bit Score: 259.46 E-value: 2.81e-81
|
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| Sec7 | smart00222 | Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ... |
348-536 | 8.13e-74 | ||||
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors). Pssm-ID: 214569 [Multi-domain] Cd Length: 189 Bit Score: 239.88 E-value: 8.13e-74
|
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| IQ_SEC7_PH | pfam16453 | PH domain; This PH domain is found in IQ motif and SEC7 domain-containing proteins. |
558-687 | 3.35e-73 | ||||
PH domain; This PH domain is found in IQ motif and SEC7 domain-containing proteins. Pssm-ID: 465120 Cd Length: 127 Bit Score: 235.64 E-value: 3.35e-73
|
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| PH_IQSEC | cd13318 | IQ motif and SEC7 domain-containing protein family Pleckstrin homology domain; The IQSEC (also ... |
563-693 | 5.14e-69 | ||||
IQ motif and SEC7 domain-containing protein family Pleckstrin homology domain; The IQSEC (also called BRAG/Brefeldin A-resistant Arf-gunanine nucleotide exchange factor) family are a subset of Arf GEFs that have been shown to activate Arf6, which acts in the endocytic pathway to control the trafficking of a subset of cargo proteins including integrins and have key roles in the function and organization of distinct excitatory and inhibitory synapses in the retina. The family consists of 3 members: IQSEC1 (also called BRAG2/GEP100), IQSEC2 (also called BRAG1), and IQSEC3 (also called SynArfGEF, BRAG3, or KIAA1110). IQSEC1 interacts with clathrin and modulates cell adhesion by regulating integrin surface expression and in addition to Arf6, it also activates the class II Arfs, Arf4 and Arf5. Mutations in IQSEC2 cause non-syndromic X-linked intellectual disability as well as reduced activation of Arf substrates (Arf1, Arf6). IQSEC3 regulates Arf6 at inhibitory synapses and associates with the dystrophin-associated glycoprotein complex and S-SCAM. These members contains a IQ domain that may bind calmodulin, a PH domain that is thought to mediate membrane localization by binding of phosphoinositides, and a SEC7 domain that can promote GEF activity on ARF. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270128 Cd Length: 128 Bit Score: 224.50 E-value: 5.14e-69
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| PLN03076 | PLN03076 | ARF guanine nucleotide exchange factor (ARF-GEF); Provisional |
348-566 | 6.59e-51 | ||||
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional Pssm-ID: 215560 [Multi-domain] Cd Length: 1780 Bit Score: 195.04 E-value: 6.59e-51
|
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| PH | smart00233 | Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
588-676 | 1.70e-05 | ||||
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 44.46 E-value: 1.70e-05
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| PRK13108 | PRK13108 | prolipoprotein diacylglyceryl transferase; Reviewed |
141-250 | 1.70e-04 | ||||
prolipoprotein diacylglyceryl transferase; Reviewed Pssm-ID: 237284 [Multi-domain] Cd Length: 460 Bit Score: 44.97 E-value: 1.70e-04
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| PH | cd00821 | Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
588-671 | 4.89e-03 | ||||
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 37.14 E-value: 4.89e-03
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| PH1_FGD5_FGD6 | cd13389 | FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ... |
581-677 | 7.90e-03 | ||||
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal Pleckstrin Homology (PH) domain; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 275424 Cd Length: 124 Bit Score: 37.25 E-value: 7.90e-03
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| Blast search parameters | ||||
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