Golgi reassembly-stacking protein 1 isoform X1 [Arvicanthis niloticus]
Protein Classification
Golgi reassembly-stacking protein( domain architecture ID 20384073)
Golgi reassembly-stacking protein (GORASP) plays an important role in stacking of Golgi cisternae
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| GRASP55_65 | pfam04495 | GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ... |
68-204 | 3.14e-85 | |||
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain. : Pssm-ID: 427981 [Multi-domain] Cd Length: 138 Bit Score: 256.81 E-value: 3.14e-85
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| PDZ_canonical super family | cl49608 | canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
14-99 | 3.06e-18 | |||
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 pfam04495: Pssm-ID: 483948 [Multi-domain] Cd Length: 138 Bit Score: 80.77 E-value: 3.06e-18
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| Name | Accession | Description | Interval | E-value | ||||
| GRASP55_65 | pfam04495 | GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ... |
68-204 | 3.14e-85 | ||||
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain. Pssm-ID: 427981 [Multi-domain] Cd Length: 138 Bit Score: 256.81 E-value: 3.14e-85
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| GRH1 | COG5233 | Peripheral Golgi membrane protein [Intracellular trafficking and secretion]; |
94-246 | 7.52e-24 | ||||
Peripheral Golgi membrane protein [Intracellular trafficking and secretion]; Pssm-ID: 227558 [Multi-domain] Cd Length: 417 Bit Score: 102.90 E-value: 7.52e-24
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| GRASP55_65 | pfam04495 | GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ... |
14-99 | 3.06e-18 | ||||
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain. Pssm-ID: 427981 [Multi-domain] Cd Length: 138 Bit Score: 80.77 E-value: 3.06e-18
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| cpPDZ_HhoA-like | cd10838 | circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ... |
14-70 | 1.26e-04 | ||||
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus. Pssm-ID: 467629 [Multi-domain] Cd Length: 104 Bit Score: 41.15 E-value: 1.26e-04
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| cpPDZ_EcRseP-like | cd23081 | circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ... |
117-179 | 4.08e-04 | ||||
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus. Pssm-ID: 467638 [Multi-domain] Cd Length: 83 Bit Score: 39.10 E-value: 4.08e-04
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| RseP | COG0750 | Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
20-106 | 1.33e-03 | ||||
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription]; Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 40.84 E-value: 1.33e-03
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| degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
20-165 | 9.00e-03 | ||||
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273938 [Multi-domain] Cd Length: 428 Bit Score: 38.36 E-value: 9.00e-03
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| Name | Accession | Description | Interval | E-value | ||||
| GRASP55_65 | pfam04495 | GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ... |
68-204 | 3.14e-85 | ||||
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain. Pssm-ID: 427981 [Multi-domain] Cd Length: 138 Bit Score: 256.81 E-value: 3.14e-85
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| GRH1 | COG5233 | Peripheral Golgi membrane protein [Intracellular trafficking and secretion]; |
94-246 | 7.52e-24 | ||||
Peripheral Golgi membrane protein [Intracellular trafficking and secretion]; Pssm-ID: 227558 [Multi-domain] Cd Length: 417 Bit Score: 102.90 E-value: 7.52e-24
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| GRASP55_65 | pfam04495 | GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ... |
14-99 | 3.06e-18 | ||||
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. This region appears to be related to the PDZ domain. Pssm-ID: 427981 [Multi-domain] Cd Length: 138 Bit Score: 80.77 E-value: 3.06e-18
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| cpPDZ_HhoA-like | cd10838 | circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ... |
14-70 | 1.26e-04 | ||||
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus. Pssm-ID: 467629 [Multi-domain] Cd Length: 104 Bit Score: 41.15 E-value: 1.26e-04
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| RseP | COG0750 | Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
114-190 | 2.53e-04 | ||||
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription]; Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 42.77 E-value: 2.53e-04
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| cpPDZ_EcRseP-like | cd23081 | circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ... |
117-179 | 4.08e-04 | ||||
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus. Pssm-ID: 467638 [Multi-domain] Cd Length: 83 Bit Score: 39.10 E-value: 4.08e-04
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| cpPDZ_EcRseP-like | cd23081 | circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ... |
20-96 | 1.14e-03 | ||||
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus. Pssm-ID: 467638 [Multi-domain] Cd Length: 83 Bit Score: 37.56 E-value: 1.14e-03
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| RseP | COG0750 | Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
20-106 | 1.33e-03 | ||||
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription]; Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 40.84 E-value: 1.33e-03
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| DegQ | COG0265 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ... |
20-85 | 2.89e-03 | ||||
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440035 [Multi-domain] Cd Length: 274 Bit Score: 39.36 E-value: 2.89e-03
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| GRH1 | COG5233 | Peripheral Golgi membrane protein [Intracellular trafficking and secretion]; |
23-99 | 3.72e-03 | ||||
Peripheral Golgi membrane protein [Intracellular trafficking and secretion]; Pssm-ID: 227558 [Multi-domain] Cd Length: 417 Bit Score: 39.35 E-value: 3.72e-03
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| CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
79-178 | 4.71e-03 | ||||
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440556 [Multi-domain] Cd Length: 341 Bit Score: 39.08 E-value: 4.71e-03
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| PDZ_2 | pfam13180 | PDZ domain; |
21-83 | 4.88e-03 | ||||
PDZ domain; Pssm-ID: 433015 [Multi-domain] Cd Length: 74 Bit Score: 35.71 E-value: 4.88e-03
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| PDZ_6 | pfam17820 | PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
113-162 | 6.85e-03 | ||||
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 34.81 E-value: 6.85e-03
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| DegQ | COG0265 | Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ... |
114-179 | 7.18e-03 | ||||
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440035 [Multi-domain] Cd Length: 274 Bit Score: 38.21 E-value: 7.18e-03
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| Peptidase_M50 | pfam02163 | Peptidase family M50; |
114-180 | 7.26e-03 | ||||
Peptidase family M50; Pssm-ID: 426630 [Multi-domain] Cd Length: 291 Bit Score: 38.24 E-value: 7.26e-03
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| COG3975 | COG3975 | Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only]; |
21-71 | 8.33e-03 | ||||
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only]; Pssm-ID: 443174 [Multi-domain] Cd Length: 591 Bit Score: 38.65 E-value: 8.33e-03
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| degP_htrA_DO | TIGR02037 | periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ... |
20-165 | 9.00e-03 | ||||
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273938 [Multi-domain] Cd Length: 428 Bit Score: 38.36 E-value: 9.00e-03
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| Blast search parameters | ||||
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