mKIAA1849 protein, partial [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| Myo5p-like_CBD_Rasip1 | cd15472 | cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
437-804 | 0e+00 | ||||||
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain. : Pssm-ID: 271256 Cd Length: 366 Bit Score: 675.14 E-value: 0e+00
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| RA_Radil_like | cd17116 | Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ... |
76-187 | 7.99e-67 | ||||||
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein (Radil) and similar proteins; Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation.This family also includes Ras-interacting protein 1 (Rain, also termed Rasip1), which is a novel Ras-interacting protein with a unique subcellular localization. It interacts with Ras in a GTP-dependent manner, and may serve as an effector for endomembrane-associated Ras. Radil contains RA, DIL, and PDZ domains. In contrast, Rain contains a myosin5-like cargo binding domain, a RA domain and a PDZ domain. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. : Pssm-ID: 340636 Cd Length: 121 Bit Score: 219.89 E-value: 7.99e-67
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| FHA super family | cl00062 | forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
270-384 | 8.39e-50 | ||||||
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function. The actual alignment was detected with superfamily member cd22733: Pssm-ID: 469597 Cd Length: 113 Bit Score: 171.52 E-value: 8.39e-50
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| PDZ_canonical super family | cl49608 | canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
993-1019 | 1.86e-07 | ||||||
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. The actual alignment was detected with superfamily member cd06690: Pssm-ID: 483948 [Multi-domain] Cd Length: 88 Bit Score: 49.60 E-value: 1.86e-07
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| Name | Accession | Description | Interval | E-value | ||||||
| Myo5p-like_CBD_Rasip1 | cd15472 | cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
437-804 | 0e+00 | ||||||
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain. Pssm-ID: 271256 Cd Length: 366 Bit Score: 675.14 E-value: 0e+00
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| RA_Radil_like | cd17116 | Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ... |
76-187 | 7.99e-67 | ||||||
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein (Radil) and similar proteins; Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation.This family also includes Ras-interacting protein 1 (Rain, also termed Rasip1), which is a novel Ras-interacting protein with a unique subcellular localization. It interacts with Ras in a GTP-dependent manner, and may serve as an effector for endomembrane-associated Ras. Radil contains RA, DIL, and PDZ domains. In contrast, Rain contains a myosin5-like cargo binding domain, a RA domain and a PDZ domain. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Pssm-ID: 340636 Cd Length: 121 Bit Score: 219.89 E-value: 7.99e-67
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| FHA_RADIL | cd22733 | forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
270-384 | 8.39e-50 | ||||||
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438785 Cd Length: 113 Bit Score: 171.52 E-value: 8.39e-50
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| DIL | pfam01843 | DIL domain; The DIL domain has no known function. |
660-767 | 4.21e-27 | ||||||
DIL domain; The DIL domain has no known function. Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 106.14 E-value: 4.21e-27
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| RA | pfam00788 | Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ... |
87-190 | 5.29e-20 | ||||||
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Pssm-ID: 425871 Cd Length: 93 Bit Score: 85.46 E-value: 5.29e-20
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| RA | smart00314 | Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ... |
87-189 | 2.43e-13 | ||||||
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.) Pssm-ID: 214612 Cd Length: 90 Bit Score: 66.55 E-value: 2.43e-13
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| PDZ_Radil-like | cd06690 | PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ... |
993-1019 | 1.86e-07 | ||||||
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Radil-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467177 [Multi-domain] Cd Length: 88 Bit Score: 49.60 E-value: 1.86e-07
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| FHA | pfam00498 | FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
299-369 | 5.70e-04 | ||||||
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 39.10 E-value: 5.70e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| Myo5p-like_CBD_Rasip1 | cd15472 | cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
437-804 | 0e+00 | ||||||
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain. Pssm-ID: 271256 Cd Length: 366 Bit Score: 675.14 E-value: 0e+00
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| Myo5-like_CBD | cd14945 | Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
439-794 | 6.08e-83 | ||||||
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo. Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 271.19 E-value: 6.08e-83
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| RA_Radil_like | cd17116 | Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein ... |
76-187 | 7.99e-67 | ||||||
Ras-associating (RA) domain found in ras-associating and dilute domain-containing protein (Radil) and similar proteins; Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation.This family also includes Ras-interacting protein 1 (Rain, also termed Rasip1), which is a novel Ras-interacting protein with a unique subcellular localization. It interacts with Ras in a GTP-dependent manner, and may serve as an effector for endomembrane-associated Ras. Radil contains RA, DIL, and PDZ domains. In contrast, Rain contains a myosin5-like cargo binding domain, a RA domain and a PDZ domain. RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Pssm-ID: 340636 Cd Length: 121 Bit Score: 219.89 E-value: 7.99e-67
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| FHA_RADIL | cd22733 | forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
270-384 | 8.39e-50 | ||||||
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438785 Cd Length: 113 Bit Score: 171.52 E-value: 8.39e-50
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| FHA_RADIL-like | cd22712 | forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
272-384 | 1.38e-31 | ||||||
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438764 [Multi-domain] Cd Length: 120 Bit Score: 119.71 E-value: 1.38e-31
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| DIL | pfam01843 | DIL domain; The DIL domain has no known function. |
660-767 | 4.21e-27 | ||||||
DIL domain; The DIL domain has no known function. Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 106.14 E-value: 4.21e-27
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| RA | pfam00788 | Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ... |
87-190 | 5.29e-20 | ||||||
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Pssm-ID: 425871 Cd Length: 93 Bit Score: 85.46 E-value: 5.29e-20
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| Myo5p-like_CBD_afadin | cd15471 | cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
437-766 | 1.56e-17 | ||||||
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain. Pssm-ID: 271255 Cd Length: 322 Bit Score: 85.06 E-value: 1.56e-17
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| FHA_RAIN | cd22734 | forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called ... |
275-384 | 1.69e-16 | ||||||
forkhead associated (FHA) domain found in Ras-interacting protein 1 (Rain); Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438786 Cd Length: 119 Bit Score: 76.74 E-value: 1.69e-16
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| RA | cd17043 | Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ... |
90-187 | 5.10e-16 | ||||||
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon. Pssm-ID: 340563 Cd Length: 87 Bit Score: 74.28 E-value: 5.10e-16
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| RA | smart00314 | Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ... |
87-189 | 2.43e-13 | ||||||
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.) Pssm-ID: 214612 Cd Length: 90 Bit Score: 66.55 E-value: 2.43e-13
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| RA2_Afadin | cd01781 | Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ... |
89-188 | 6.31e-12 | ||||||
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin. Pssm-ID: 340479 Cd Length: 102 Bit Score: 63.06 E-value: 6.31e-12
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| Myo5p-like_CBD_DIL_ANK | cd15473 | cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
432-763 | 3.65e-09 | ||||||
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown. Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 59.49 E-value: 3.65e-09
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| FHA_KIF14 | cd22707 | forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ... |
275-369 | 2.10e-08 | ||||||
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438759 [Multi-domain] Cd Length: 108 Bit Score: 53.04 E-value: 2.10e-08
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| RA_Myosin-IX | cd01779 | Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ... |
90-188 | 1.17e-07 | ||||||
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system. Pssm-ID: 340477 Cd Length: 97 Bit Score: 50.78 E-value: 1.17e-07
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| PDZ_Radil-like | cd06690 | PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; ... |
993-1019 | 1.86e-07 | ||||||
PDZ domain of Ras-associating and dilute domain-containing protein (Radil) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Radil (also known as protein KIAA1849) and related domains. Radil is required for cell adhesion and migration of neural crest precursors during development. Radil is a component of a Rasip1-Radil-ARHGAP29 complex at endothelial cell-cell junctions. Rap1, via its effectors Radil and Rasip1 and their binding partner ArhGAP29, controls the endothelial barrier by decreasing Rho-mediated radial tension on cell-cell junctions. ArhGAP29 binds the Radil PDZ domain. The Radil PDZ domain also binds kinesin family protein 14 (KIF14); KIF14 negatively regulates Rap1-mediated inside-out integrin activation by tethering Radil on microtubules. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Radil-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. Pssm-ID: 467177 [Multi-domain] Cd Length: 88 Bit Score: 49.60 E-value: 1.86e-07
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| RA2_DAGK-theta | cd01783 | Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ... |
89-188 | 1.12e-05 | ||||||
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta. Pssm-ID: 340481 Cd Length: 95 Bit Score: 44.91 E-value: 1.12e-05
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| Myo5p-like_CBD_fungal | cd15474 | cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
518-772 | 3.06e-05 | ||||||
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site. Pssm-ID: 271258 Cd Length: 352 Bit Score: 47.41 E-value: 3.06e-05
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| RA_PLC-epsilon | cd17114 | Ras-associating (RA) domain found in Phosphatidylinositide-specific phospholipase C (PLC) ... |
91-188 | 7.94e-05 | ||||||
Ras-associating (RA) domain found in Phosphatidylinositide-specific phospholipase C (PLC)-epsilon; PLC is a signaling enzyme that hydrolyzes membrane phospholipids to generate inositol triphosphate. PLC-epsilon represents a novel forth class of PLC that has a PLC catalytic core domain, a CDC25 guanine nucleotide exchange factor domain and two RA (Ras-association) domains. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Although PLC RA1 and RA2 have homologous ubiquitin-like folds only RA2 can bind Ras and activate it. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. Pssm-ID: 340634 Cd Length: 97 Bit Score: 42.71 E-value: 7.94e-05
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| FHA_KIF13 | cd22706 | forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ... |
290-369 | 1.32e-04 | ||||||
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438758 [Multi-domain] Cd Length: 101 Bit Score: 41.90 E-value: 1.32e-04
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| FHA_KIF28P | cd22709 | forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
275-369 | 3.39e-04 | ||||||
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438761 [Multi-domain] Cd Length: 102 Bit Score: 41.05 E-value: 3.39e-04
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| FHA_KIF1A | cd22726 | forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
275-388 | 3.57e-04 | ||||||
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438778 [Multi-domain] Cd Length: 115 Bit Score: 41.45 E-value: 3.57e-04
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| FHA_KIF1 | cd22705 | forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
274-369 | 4.74e-04 | ||||||
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438757 [Multi-domain] Cd Length: 101 Bit Score: 40.68 E-value: 4.74e-04
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| FHA | pfam00498 | FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
299-369 | 5.70e-04 | ||||||
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 39.10 E-value: 5.70e-04
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| FHA_KIF1B | cd22727 | forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ... |
275-386 | 6.66e-04 | ||||||
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438779 [Multi-domain] Cd Length: 110 Bit Score: 40.40 E-value: 6.66e-04
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| Myo5_CBD | cd15470 | Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
634-769 | 1.15e-03 | ||||||
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2. Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 42.58 E-value: 1.15e-03
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| FHA_KIF1C | cd22728 | forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
275-369 | 4.52e-03 | ||||||
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 37.93 E-value: 4.52e-03
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| Myo5a_CBD | cd15478 | Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
439-711 | 4.65e-03 | ||||||
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease. Pssm-ID: 271262 Cd Length: 375 Bit Score: 40.78 E-value: 4.65e-03
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| RA_PDZ-GEF1 | cd01785 | Ras-associating (RA) domain found in PDZ domain-containing guanine nucleotide exchange factor ... |
89-151 | 5.37e-03 | ||||||
Ras-associating (RA) domain found in PDZ domain-containing guanine nucleotide exchange factor 1 (PDZ-GEF1) and similar proteins; PDZ-GEF1, also termed Rap guanine nucleotide exchange factor 2, or cyclic nucleotide ras GEF (CNrasGEF), or neural RAP guanine nucleotide exchange protein (nRap GEP), or Ras/Rap1-associating GEF-1 (RA-GEF-1), is a Rap-specific guanine nucleotide exchange factor (GEF) that has a PSD-95/DlgA/ZO-1 (PDZ) domain, a RA domain and a region related to a cyclic nucleotide binding domain (RCBD). The RA domain of PDZ-GEF interacts with Rap1 and also contributes to the membrane localization of PDZ-GEF. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and involve in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Pssm-ID: 340483 Cd Length: 85 Bit Score: 36.90 E-value: 5.37e-03
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| FHA | cd00060 | forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
276-369 | 5.70e-03 | ||||||
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function. Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 37.25 E-value: 5.70e-03
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| FHA_KIF16 | cd22708 | forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ... |
272-369 | 8.33e-03 | ||||||
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438760 [Multi-domain] Cd Length: 109 Bit Score: 37.25 E-value: 8.33e-03
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| FHA_AFDN | cd22711 | forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
302-369 | 9.00e-03 | ||||||
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine. Pssm-ID: 438763 [Multi-domain] Cd Length: 106 Bit Score: 36.92 E-value: 9.00e-03
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