unnamed protein product [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| RocCOR | cd09914 | Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ... |
173-346 | 5.13e-76 | ||||
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease. : Pssm-ID: 206741 [Multi-domain] Cd Length: 161 Bit Score: 237.23 E-value: 5.13e-76
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
12-140 | 1.55e-21 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; : Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 96.93 E-value: 1.55e-21
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| COR super family | cl24610 | C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ... |
366-543 | 1.01e-19 | ||||
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity. The actual alignment was detected with superfamily member pfam16095: Pssm-ID: 406489 Cd Length: 196 Bit Score: 87.30 E-value: 1.01e-19
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| Name | Accession | Description | Interval | E-value | ||||
| RocCOR | cd09914 | Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ... |
173-346 | 5.13e-76 | ||||
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease. Pssm-ID: 206741 [Multi-domain] Cd Length: 161 Bit Score: 237.23 E-value: 5.13e-76
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| Roc | pfam08477 | Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ... |
175-294 | 1.12e-38 | ||||
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis. Pssm-ID: 462490 [Multi-domain] Cd Length: 114 Bit Score: 137.25 E-value: 1.12e-38
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
12-140 | 1.55e-21 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 96.93 E-value: 1.55e-21
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| Gem1 | COG1100 | GTPase SAR1 family domain [General function prediction only]; |
171-343 | 7.21e-20 | ||||
GTPase SAR1 family domain [General function prediction only]; Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 86.96 E-value: 7.21e-20
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| COR | pfam16095 | C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ... |
366-543 | 1.01e-19 | ||||
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity. Pssm-ID: 406489 Cd Length: 196 Bit Score: 87.30 E-value: 1.01e-19
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| RAB | smart00175 | Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking. |
174-300 | 3.07e-14 | ||||
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking. Pssm-ID: 197555 [Multi-domain] Cd Length: 164 Bit Score: 70.61 E-value: 3.07e-14
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| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
173-321 | 1.00e-12 | ||||
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General] Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 66.24 E-value: 1.00e-12
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| PLN03118 | PLN03118 | Rab family protein; Provisional |
175-299 | 5.82e-08 | ||||
Rab family protein; Provisional Pssm-ID: 215587 [Multi-domain] Cd Length: 211 Bit Score: 53.52 E-value: 5.82e-08
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| PLN00113 | PLN00113 | leucine-rich repeat receptor-like protein kinase; Provisional |
12-138 | 1.12e-07 | ||||
leucine-rich repeat receptor-like protein kinase; Provisional Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 54.85 E-value: 1.12e-07
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| PPP1R42 | cd21340 | protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
2-140 | 6.61e-06 | ||||
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation. Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 47.47 E-value: 6.61e-06
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| LRR_8 | pfam13855 | Leucine rich repeat; |
60-118 | 3.64e-05 | ||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.74 E-value: 3.64e-05
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| Name | Accession | Description | Interval | E-value | ||||
| RocCOR | cd09914 | Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ... |
173-346 | 5.13e-76 | ||||
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease. Pssm-ID: 206741 [Multi-domain] Cd Length: 161 Bit Score: 237.23 E-value: 5.13e-76
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| Roc | pfam08477 | Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ... |
175-294 | 1.12e-38 | ||||
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis. Pssm-ID: 462490 [Multi-domain] Cd Length: 114 Bit Score: 137.25 E-value: 1.12e-38
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
12-140 | 1.55e-21 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 96.93 E-value: 1.55e-21
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
12-140 | 1.70e-21 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 96.93 E-value: 1.70e-21
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| Gem1 | COG1100 | GTPase SAR1 family domain [General function prediction only]; |
171-343 | 7.21e-20 | ||||
GTPase SAR1 family domain [General function prediction only]; Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 86.96 E-value: 7.21e-20
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| COR | pfam16095 | C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ... |
366-543 | 1.01e-19 | ||||
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity. Pssm-ID: 406489 Cd Length: 196 Bit Score: 87.30 E-value: 1.01e-19
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
12-140 | 4.37e-16 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 80.36 E-value: 4.37e-16
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| Rab30 | cd04114 | Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ... |
175-339 | 3.70e-15 | ||||
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 133314 [Multi-domain] Cd Length: 169 Bit Score: 73.39 E-value: 3.70e-15
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| Ras_like_GTPase | cd00882 | Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
178-345 | 2.03e-14 | ||||
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: 70.95 E-value: 2.03e-14
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| RAB | smart00175 | Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking. |
174-300 | 3.07e-14 | ||||
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking. Pssm-ID: 197555 [Multi-domain] Cd Length: 164 Bit Score: 70.61 E-value: 3.07e-14
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| Rab | cd00154 | Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ... |
174-300 | 4.50e-14 | ||||
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible. Pssm-ID: 206640 [Multi-domain] Cd Length: 159 Bit Score: 69.79 E-value: 4.50e-14
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| Rab26 | cd04112 | Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ... |
175-302 | 2.44e-13 | ||||
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Pssm-ID: 206695 [Multi-domain] Cd Length: 191 Bit Score: 68.74 E-value: 2.44e-13
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| small_GTP | TIGR00231 | small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
173-321 | 1.00e-12 | ||||
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General] Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 66.24 E-value: 1.00e-12
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
14-136 | 1.32e-12 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 69.58 E-value: 1.32e-12
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| Ras | pfam00071 | Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ... |
175-300 | 1.58e-12 | ||||
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices. Pssm-ID: 425451 [Multi-domain] Cd Length: 162 Bit Score: 65.61 E-value: 1.58e-12
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| Rab12 | cd04120 | Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ... |
174-300 | 6.37e-11 | ||||
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Pssm-ID: 206699 [Multi-domain] Cd Length: 202 Bit Score: 61.95 E-value: 6.37e-11
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| Rab19 | cd01864 | Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ... |
175-304 | 2.75e-10 | ||||
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet characterized. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 133267 [Multi-domain] Cd Length: 165 Bit Score: 59.37 E-value: 2.75e-10
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| Rab27A | cd04127 | Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ... |
174-321 | 5.91e-10 | ||||
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated insulin secretion, making it a potential target for diabetes therapy. When bound to JFC1 in prostate cells, Rab27a is believed to regulate the exocytosis of prostate- specific markers. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206700 [Multi-domain] Cd Length: 180 Bit Score: 58.67 E-value: 5.91e-10
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| Rab35 | cd04110 | Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ... |
175-307 | 8.30e-10 | ||||
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Pssm-ID: 133310 [Multi-domain] Cd Length: 199 Bit Score: 58.71 E-value: 8.30e-10
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| Rab39 | cd04111 | Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ... |
175-300 | 1.26e-08 | ||||
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Pssm-ID: 133311 [Multi-domain] Cd Length: 211 Bit Score: 55.15 E-value: 1.26e-08
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| Rab23_like | cd04106 | Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ... |
174-316 | 2.43e-08 | ||||
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 133306 [Multi-domain] Cd Length: 162 Bit Score: 53.60 E-value: 2.43e-08
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| Rab3 | cd01865 | Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ... |
175-299 | 3.20e-08 | ||||
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206657 [Multi-domain] Cd Length: 165 Bit Score: 53.38 E-value: 3.20e-08
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| Rab8_Rab10_Rab13_like | cd01867 | Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ... |
174-300 | 3.21e-08 | ||||
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206659 [Multi-domain] Cd Length: 167 Bit Score: 53.04 E-value: 3.21e-08
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| PLN03118 | PLN03118 | Rab family protein; Provisional |
175-299 | 5.82e-08 | ||||
Rab family protein; Provisional Pssm-ID: 215587 [Multi-domain] Cd Length: 211 Bit Score: 53.52 E-value: 5.82e-08
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| PLN00113 | PLN00113 | leucine-rich repeat receptor-like protein kinase; Provisional |
12-138 | 1.12e-07 | ||||
leucine-rich repeat receptor-like protein kinase; Provisional Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 54.85 E-value: 1.12e-07
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| Rnd | cd04131 | Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ... |
173-319 | 1.25e-07 | ||||
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206703 [Multi-domain] Cd Length: 176 Bit Score: 51.67 E-value: 1.25e-07
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
12-120 | 1.28e-07 | ||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 54.17 E-value: 1.28e-07
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| PLN03108 | PLN03108 | Rab family protein; Provisional |
175-299 | 1.71e-07 | ||||
Rab family protein; Provisional Pssm-ID: 178655 [Multi-domain] Cd Length: 210 Bit Score: 51.87 E-value: 1.71e-07
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| Rab14 | cd04122 | Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ... |
175-300 | 2.75e-07 | ||||
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 133322 [Multi-domain] Cd Length: 166 Bit Score: 50.61 E-value: 2.75e-07
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| PRK15370 | PRK15370 | type III secretion system effector E3 ubiquitin transferase SlrP; |
2-121 | 5.61e-07 | ||||
type III secretion system effector E3 ubiquitin transferase SlrP; Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 52.39 E-value: 5.61e-07
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| Rab7 | cd01862 | Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ... |
174-307 | 9.23e-07 | ||||
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206655 [Multi-domain] Cd Length: 172 Bit Score: 49.20 E-value: 9.23e-07
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| PRK15370 | PRK15370 | type III secretion system effector E3 ubiquitin transferase SlrP; |
2-127 | 9.81e-07 | ||||
type III secretion system effector E3 ubiquitin transferase SlrP; Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 51.62 E-value: 9.81e-07
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| Rab18 | cd01863 | Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ... |
175-294 | 1.01e-06 | ||||
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206656 [Multi-domain] Cd Length: 161 Bit Score: 48.85 E-value: 1.01e-06
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| Spg1 | cd04128 | Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ... |
174-294 | 2.00e-06 | ||||
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Pssm-ID: 206701 [Multi-domain] Cd Length: 182 Bit Score: 48.16 E-value: 2.00e-06
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| Rop_like | cd04133 | Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ... |
229-300 | 2.71e-06 | ||||
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Rop1, Rop3, and Rop5 are all involved in pollen-tube growth; Rop2 plays a role in response to low-oxygen environments, cell-morphology, and root-hair development; root-hair development is also regulated by Rop4 and Rop6; Rop6 is also responsible for ABA response, and ABA response is also regulated by Rop10. Plants retain some of the regulatory mechanisms that are shared by other members of the Rho family, but have also developed a number of unique modes for regulating Rops. Unique RhoGEFs have been identified that are exclusively active toward Rop proteins, such as those containing the domain PRONE (plant-specific Rop nucleotide exchanger). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206705 [Multi-domain] Cd Length: 173 Bit Score: 47.92 E-value: 2.71e-06
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| PPP1R42 | cd21340 | protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
2-140 | 6.61e-06 | ||||
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation. Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 47.47 E-value: 6.61e-06
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| Rnd1_Rho6 | cd04174 | Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ... |
173-300 | 7.79e-06 | ||||
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206737 [Multi-domain] Cd Length: 232 Bit Score: 47.36 E-value: 7.79e-06
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| PRK15387 | PRK15387 | type III secretion system effector E3 ubiquitin transferase SspH2; |
2-140 | 7.89e-06 | ||||
type III secretion system effector E3 ubiquitin transferase SspH2; Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 48.62 E-value: 7.89e-06
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| RAN | smart00176 | Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ... |
179-350 | 1.05e-05 | ||||
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the active transport of proteins through nuclear pores. Pssm-ID: 128473 [Multi-domain] Cd Length: 200 Bit Score: 46.54 E-value: 1.05e-05
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| PLN00113 | PLN00113 | leucine-rich repeat receptor-like protein kinase; Provisional |
12-124 | 1.34e-05 | ||||
leucine-rich repeat receptor-like protein kinase; Provisional Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 48.31 E-value: 1.34e-05
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| Rnd2_Rho7 | cd04173 | Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ... |
173-295 | 1.55e-05 | ||||
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Pssm-ID: 206736 [Multi-domain] Cd Length: 221 Bit Score: 46.17 E-value: 1.55e-05
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| Ran | cd00877 | Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ... |
175-309 | 1.62e-05 | ||||
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is bound to chromatin and confined to the nucleus. Ran itself is mobile and is actively imported into the nucleus by a mechanism involving NTF-2. Together with the compartmentalization of its regulators, this is thought to produce a relatively high concentration of RanGTP in the nucleus. Pssm-ID: 206643 [Multi-domain] Cd Length: 166 Bit Score: 45.37 E-value: 1.62e-05
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| PLN03150 | PLN03150 | hypothetical protein; Provisional |
80-140 | 2.45e-05 | ||||
hypothetical protein; Provisional Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 47.12 E-value: 2.45e-05
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| Rho4_like | cd04132 | Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ... |
174-301 | 2.62e-05 | ||||
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Pssm-ID: 206704 [Multi-domain] Cd Length: 197 Bit Score: 45.41 E-value: 2.62e-05
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| LRR_8 | pfam13855 | Leucine rich repeat; |
60-118 | 3.64e-05 | ||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.74 E-value: 3.64e-05
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| PLN03071 | PLN03071 | GTP-binding nuclear protein Ran; Provisional |
169-303 | 3.73e-05 | ||||
GTP-binding nuclear protein Ran; Provisional Pssm-ID: 178620 [Multi-domain] Cd Length: 219 Bit Score: 45.13 E-value: 3.73e-05
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| PLN00113 | PLN00113 | leucine-rich repeat receptor-like protein kinase; Provisional |
12-117 | 4.73e-05 | ||||
leucine-rich repeat receptor-like protein kinase; Provisional Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 46.38 E-value: 4.73e-05
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| PRK15387 | PRK15387 | type III secretion system effector E3 ubiquitin transferase SspH2; |
2-134 | 6.37e-05 | ||||
type III secretion system effector E3 ubiquitin transferase SspH2; Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 45.92 E-value: 6.37e-05
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| PLN00113 | PLN00113 | leucine-rich repeat receptor-like protein kinase; Provisional |
2-133 | 6.44e-05 | ||||
leucine-rich repeat receptor-like protein kinase; Provisional Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 45.99 E-value: 6.44e-05
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| PLN00113 | PLN00113 | leucine-rich repeat receptor-like protein kinase; Provisional |
10-117 | 6.89e-05 | ||||
leucine-rich repeat receptor-like protein kinase; Provisional Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 45.99 E-value: 6.89e-05
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| PTZ00132 | PTZ00132 | GTP-binding nuclear protein Ran; Provisional |
175-305 | 1.04e-04 | ||||
GTP-binding nuclear protein Ran; Provisional Pssm-ID: 240284 [Multi-domain] Cd Length: 215 Bit Score: 43.53 E-value: 1.04e-04
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| PLN00023 | PLN00023 | GTP-binding protein; Provisional |
170-262 | 1.13e-04 | ||||
GTP-binding protein; Provisional Pssm-ID: 177661 Cd Length: 334 Bit Score: 44.47 E-value: 1.13e-04
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| Rab15 | cd04117 | Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ... |
175-300 | 1.16e-04 | ||||
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206698 [Multi-domain] Cd Length: 164 Bit Score: 42.66 E-value: 1.16e-04
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| LRR_8 | pfam13855 | Leucine rich repeat; |
12-47 | 1.21e-04 | ||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 40.20 E-value: 1.21e-04
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| PTZ00099 | PTZ00099 | rab6; Provisional |
206-300 | 1.58e-04 | ||||
rab6; Provisional Pssm-ID: 185444 [Multi-domain] Cd Length: 176 Bit Score: 42.81 E-value: 1.58e-04
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| LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
85-125 | 2.17e-04 | ||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 38.77 E-value: 2.17e-04
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| Rap2 | cd04176 | Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ... |
175-300 | 2.98e-04 | ||||
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, including the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 133376 [Multi-domain] Cd Length: 163 Bit Score: 41.75 E-value: 2.98e-04
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| Rac1_like | cd01871 | Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ... |
174-300 | 3.02e-04 | ||||
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3; The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206663 [Multi-domain] Cd Length: 174 Bit Score: 41.72 E-value: 3.02e-04
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| LRR_8 | pfam13855 | Leucine rich repeat; |
12-71 | 3.07e-04 | ||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.04 E-value: 3.07e-04
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| Rap_like | cd04136 | Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ... |
175-299 | 3.32e-04 | ||||
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap2 is involved in multiple functions, including activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton and activation of the Wnt/beta-catenin signaling pathway in embryonic Xenopus. A number of effector proteins for Rap2 have been identified, including isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK), and the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. RSR1 is the fungal homolog of Rap1 and Rap2. In budding yeasts, it is involved in selecting a site for bud growth, which directs the establishment of cell polarization. The Rho family GTPase Cdc42 and its GEF, Cdc24, then establish an axis of polarized growth. It is believed that Cdc42 interacts directly with RSR1 in vivo. In filamentous fungi such as Ashbya gossypii, RSR1 is a key regulator of polar growth in the hypha. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206708 [Multi-domain] Cd Length: 164 Bit Score: 41.39 E-value: 3.32e-04
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| RJL | cd04119 | Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ... |
175-294 | 6.15e-04 | ||||
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Pssm-ID: 133319 [Multi-domain] Cd Length: 168 Bit Score: 40.80 E-value: 6.15e-04
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| RabL3 | cd04102 | Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins ... |
174-301 | 6.35e-04 | ||||
Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown. Pssm-ID: 206689 Cd Length: 204 Bit Score: 41.04 E-value: 6.35e-04
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| Wrch_1 | cd04130 | Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ... |
174-298 | 6.52e-04 | ||||
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 133330 [Multi-domain] Cd Length: 173 Bit Score: 40.85 E-value: 6.52e-04
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| ABC_cobalt_CbiO_domain1 | cd03225 | First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
175-223 | 8.53e-04 | ||||
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems. Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 40.91 E-value: 8.53e-04
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| Era_like | cd00880 | E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
178-345 | 1.13e-03 | ||||
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: 39.92 E-value: 1.13e-03
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| PTZ00369 | PTZ00369 | Ras-like protein; Provisional |
172-300 | 1.15e-03 | ||||
Ras-like protein; Provisional Pssm-ID: 240385 [Multi-domain] Cd Length: 189 Bit Score: 40.23 E-value: 1.15e-03
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| ABC_ATPase | cd00267 | ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
176-229 | 1.19e-03 | ||||
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.54 E-value: 1.19e-03
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| RabL2 | cd04124 | Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab ... |
174-294 | 1.29e-03 | ||||
Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share > 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Pssm-ID: 133324 [Multi-domain] Cd Length: 161 Bit Score: 39.84 E-value: 1.29e-03
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| RHO | smart00174 | Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ... |
176-300 | 1.36e-03 | ||||
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms. Pssm-ID: 197554 [Multi-domain] Cd Length: 174 Bit Score: 39.90 E-value: 1.36e-03
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| ABCC_bacteriocin_exporters | cd03245 | ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
175-246 | 1.48e-03 | ||||
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane. Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 40.27 E-value: 1.48e-03
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| RabL4 | cd04101 | Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ... |
174-300 | 1.65e-03 | ||||
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown. Pssm-ID: 206688 [Multi-domain] Cd Length: 167 Bit Score: 39.43 E-value: 1.65e-03
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| PRK11784 | PRK11784 | tRNA 2-selenouridine synthase; Provisional |
159-205 | 1.72e-03 | ||||
tRNA 2-selenouridine synthase; Provisional Pssm-ID: 236982 [Multi-domain] Cd Length: 345 Bit Score: 40.58 E-value: 1.72e-03
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| Arf_Arl | cd00878 | ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ... |
175-240 | 1.77e-03 | ||||
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions. Pssm-ID: 206644 [Multi-domain] Cd Length: 158 Bit Score: 39.10 E-value: 1.77e-03
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| ABCC_MRP_Like | cd03228 | ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
175-216 | 1.80e-03 | ||||
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 39.29 E-value: 1.80e-03
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| Rab5_related | cd01860 | Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ... |
175-300 | 1.96e-03 | ||||
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Pssm-ID: 206653 [Multi-domain] Cd Length: 163 Bit Score: 39.07 E-value: 1.96e-03
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| RNA1 | COG5238 | Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
11-167 | 2.44e-03 | ||||
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis]; Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 40.54 E-value: 2.44e-03
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| LRR_8 | pfam13855 | Leucine rich repeat; |
84-143 | 2.84e-03 | ||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 36.35 E-value: 2.84e-03
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| VirB11 | COG0630 | Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
172-200 | 3.16e-03 | ||||
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 40.06 E-value: 3.16e-03
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| Rab28 | cd04109 | Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ... |
174-304 | 3.33e-03 | ||||
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Pssm-ID: 206694 [Multi-domain] Cd Length: 213 Bit Score: 39.01 E-value: 3.33e-03
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| LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
35-79 | 3.77e-03 | ||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 35.30 E-value: 3.77e-03
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| GsiA | COG1123 | ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
176-223 | 5.37e-03 | ||||
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 39.50 E-value: 5.37e-03
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| ABCC_Glucan_exporter_like | cd03254 | ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
174-217 | 6.01e-03 | ||||
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 38.36 E-value: 6.01e-03
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| AAA_7 | pfam12775 | P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ... |
158-200 | 8.24e-03 | ||||
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs). Pssm-ID: 463698 [Multi-domain] Cd Length: 179 Bit Score: 37.37 E-value: 8.24e-03
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| ABC_NikE_OppD_transporters | cd03257 | ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
178-227 | 9.06e-03 | ||||
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF. Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 37.87 E-value: 9.06e-03
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