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Conserved domains on  [gi|2462591955|ref|XP_054203532|]
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Golgi reassembly-stacking protein 1 isoform X4 [Homo sapiens]

Protein Classification

Golgi reassembly-stacking protein( domain architecture ID 20384073)

Golgi reassembly-stacking protein (GORASP) plays an important role in stacking of Golgi cisternae

CATH:  2.30.42.10
Gene Ontology:  GO:0007283|GO:0007030|GO:0005515
PubMed:  30712672|32573693|11158544|11283303

Graphical summary

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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 ...
 74-194 2.71e-68

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: 209.43  E-value: 2.71e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  74 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSD-QILQESE 152
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462591955 153 DFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGS 194
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGA 122
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 26-105 2.58e-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: 79.62  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  26 QVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 105
Cdd:pfam04495  49 DVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGL 127
 
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 ...
 74-194 2.71e-68

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: 209.43  E-value: 2.71e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  74 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSD-QILQESE 152
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462591955 153 DFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGS 194
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGA 122
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 26-105 2.58e-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: 79.62  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  26 QVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 105
Cdd:pfam04495  49 DVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGL 127
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
100-193 1.22e-13

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 70.93  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955 100 LLGASVRFCSFRRASEQVWHVLDVE-PSSPAALAGLRPYTDYVVGSD--QILQESE-DFFTLIESHEGKPLKLMVYNSKS 175
Cdd:COG5233   170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSSdgQPLEIGElDLEDVNESPVNLPLSLYYYNPID 249

                          90
                  ....*....|....*...
gi 2462591955 176 DSCREVTVTPNAAWGGEG 193
Cdd:COG5233   250 DQERAKTERDGVHKGIVG 267
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 26-85 7.54e-05

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: 7.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591955  26 QVQENSPAQQAGLEPyFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF---NMKTMRVR 85
Cdd:cd10838    39 QVLPNSPAARAGLRR-GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLrgdRRQTLAVK 100
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 26-121 7.95e-05

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 43.92  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  26 QVQENSPAQQAGLEPYfDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVfnmktMR---VREVEVVP-SNMWGGQGLL 101
Cdd:COG0750   134 EVVPGSPAAKAGLQPG-DRIVAINGQPVTSWDD-LVDIIRASPGKPLTLTV-----ERdgeELTLTVTPrLVEEDGVGRI 206

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462591955 102 GASVRFC----------SFRRASEQVWHVL 121
Cdd:COG0750   207 GVSPSGEvvtvrygpleALGAGVKETWDMI 236
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 123-185 8.26e-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: 37.56  E-value: 8.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591955 123 VEPSSPAALAGLRPyTDYVV-GSDQILQESEDFFTLIESHEGKPLKLMVynSKSDSCREVTVTP 185
Cdd:cd23081     6 VVANSPAAEAGLKP-GDRILkIDGQKVRTWEDIVRIVRENPGKPLTLKI--ERDGKILTVTVTP 66
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 16-136 9.59e-04

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: 40.67  E-value: 9.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  16 GMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF-NMKTMRVR-------E 86
Cdd:TIGR02037 252 GLEKQRGALvAQVLPGSPAEKAGLKAG-DVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILrKGKEKTITvtlgaspE 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462591955  87 VEVVPSNMWggQGLLGASVRFCSFRRASEQVWH----VLDVEPSSPAALAGLRP 136
Cdd:TIGR02037 331 EQASSSNPF--LGLTVANLSPEIRKELRLKGDVkgvvVTKVVSGSPAARAGLQP 382
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 12-76 4.51e-03

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 35.82  E-value: 4.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591955   12 SVDSGMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEV 76
Cdd:smart00228  17 SLVGGKDEGGGVVvSSVVPGSPAAKAGLRVG-DVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTV 81
 
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 ...
 74-194 2.71e-68

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: 209.43  E-value: 2.71e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  74 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSD-QILQESE 152
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462591955 153 DFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGS 194
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGA 122
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 26-105 2.58e-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: 79.62  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  26 QVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 105
Cdd:pfam04495  49 DVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGL 127
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
100-193 1.22e-13

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 70.93  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955 100 LLGASVRFCSFRRASEQVWHVLDVE-PSSPAALAGLRPYTDYVVGSD--QILQESE-DFFTLIESHEGKPLKLMVYNSKS 175
Cdd:COG5233   170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSSdgQPLEIGElDLEDVNESPVNLPLSLYYYNPID 249

                          90
                  ....*....|....*...
gi 2462591955 176 DSCREVTVTPNAAWGGEG 193
Cdd:COG5233   250 DQERAKTERDGVHKGIVG 267
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
11-148 2.57e-05

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 45.51  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  11 ASVDSGMHparSVFQQVQEnSPAQQAGLEPYFDFIITIGHSRLNKENDT-LKALLKANVEKPVKLEVFNMKTMRVREVEV 89
Cdd:COG5233   182 DVVCSDSH---ILNVSIQD-KPPAYALLSPDEDYIDGSSDGQPLEIGELdLEDVNESPVNLPLSLYYYNPIDDQERAKTE 257

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462591955  90 VPSNMWGGQGLLGasvrfcsfrrasEQVWHvlDVEPSSPAALAGLRPYTDYVVGSDQIL 148
Cdd:COG5233   258 RDGVHKGIVGILG------------CQVGH--GFLHRLPLAGVGQKPQLQKLGTTKRTE 302
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 26-85 7.54e-05

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: 7.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462591955  26 QVQENSPAQQAGLEPyFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF---NMKTMRVR 85
Cdd:cd10838    39 QVLPNSPAARAGLRR-GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLrgdRRQTLAVK 100
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 26-121 7.95e-05

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 43.92  E-value: 7.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  26 QVQENSPAQQAGLEPYfDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVfnmktMR---VREVEVVP-SNMWGGQGLL 101
Cdd:COG0750   134 EVVPGSPAAKAGLQPG-DRIVAINGQPVTSWDD-LVDIIRASPGKPLTLTV-----ERdgeELTLTVTPrLVEEDGVGRI 206

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462591955 102 GASVRFC----------SFRRASEQVWHVL 121
Cdd:COG0750   207 GVSPSGEvvtvrygpleALGAGVKETWDMI 236
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
19-91 6.18e-04

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 41.35  E-value: 6.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591955  19 PARSVFQQVQENSPAQQAGLEPYfDFIITIGHSRLNKENdtLKALLK-ANVEKPVKLEVFNMKtmRVREVEVVP 91
Cdd:COG3975   493 GGGLVVTSVLWGSPAYKAGLSAG-DELLAIDGLRVTADN--LDDALAaYKPGDPIELLVFRRD--ELRTVTVTL 561
PDZ_2 pfam13180
PDZ domain;
17-77 7.54e-04

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 37.64  E-value: 7.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462591955  17 MHPARSVFQQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF 77
Cdd:pfam13180   3 DLEGGVVVVSVKSSGPAAKAGLKAG-DVILSIDGRKINDLTDLESALYGHKPGDTVTLQVY 62
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 123-185 8.26e-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: 37.56  E-value: 8.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462591955 123 VEPSSPAALAGLRPyTDYVV-GSDQILQESEDFFTLIESHEGKPLKLMVynSKSDSCREVTVTP 185
Cdd:cd23081     6 VVANSPAAEAGLKP-GDRILkIDGQKVRTWEDIVRIVRENPGKPLTLKI--ERDGKILTVTVTP 66
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 16-136 9.59e-04

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: 40.67  E-value: 9.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  16 GMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF-NMKTMRVR-------E 86
Cdd:TIGR02037 252 GLEKQRGALvAQVLPGSPAEKAGLKAG-DVITSVNGKPISSFADLRRAIGTLKPGKKVTLGILrKGKEKTITvtlgaspE 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462591955  87 VEVVPSNMWggQGLLGASVRFCSFRRASEQVWH----VLDVEPSSPAALAGLRP 136
Cdd:TIGR02037 331 EQASSSNPF--LGLTVANLSPEIRKELRLKGDVkgvvVTKVVSGSPAARAGLQP 382
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 26-102 9.67e-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: 37.56  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  26 QVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKAlLKANVEKPVKLEVfnmktMR---VREVEVVPSNM---WGGQG 99
Cdd:cd23081     5 EVVANSPAAEAGLKPG-DRILKIDGQKVRTWEDIVRI-VRENPGKPLTLKI-----ERdgkILTVTVTPELVeveGKGVG 77


                  ...
gi 2462591955 100 LLG 102
Cdd:cd23081    78 RIG 80
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 120-187 1.55e-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: 39.68  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591955 120 VLDVEPSSPAALAGLRPytdyvvGsDQIL-------QESEDFFTLIESHEGKPLKLMVY-NSKSdscREVTVTPNA 187
Cdd:COG0750   132 VGEVVPGSPAAKAGLQP------G-DRIVaingqpvTSWDDLVDIIRASPGKPLTLTVErDGEE---LTLTVTPRL 197
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 25-91 2.96e-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: 38.59  E-value: 2.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  25 QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVfnmktMR---VREVEVVP 91
Cdd:COG0265   206 ARVEPGSPAAKAGLRPG-DVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV-----LRggkELTVTVTL 269
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 120-185 2.98e-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: 38.59  E-value: 2.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462591955 120 VLDVEPSSPAALAGLRPYtdyvvgsDQILQ-------ESEDFFTLIESHE-GKPLKLMVY-NSKSdscREVTVTP 185
Cdd:COG0265   205 VARVEPGSPAAKAGLRPG-------DVILAvdgkpvtSARDLQRLLASLKpGDTVTLTVLrGGKE---LTVTVTL 269
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 23-76 3.49e-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: 35.20  E-value: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462591955  23 VFQQVQENSPAQQAGLEPYfDFIITI-GHSRLNKENdtLKALLKANVEKPVKLEV 76
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVG-DVILAVnGKPVRSLED--VARLLQGSAGESVTLTV 52
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 12-76 4.51e-03

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 35.82  E-value: 4.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462591955   12 SVDSGMHPARSVF-QQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEV 76
Cdd:smart00228  17 SLVGGKDEGGGVVvSSVVPGSPAAKAGLRVG-DVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTV 81
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 23-76 6.96e-03

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. 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 BsHtrA-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: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 35.30  E-value: 6.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462591955  23 VFQQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEV 76
Cdd:cd06781    33 YVAQVQSNSPAEKAGLKKG-DVITKLDGKKVESSSDLRQILYSHKVGDTVKVTI 85
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 85-184 7.25e-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: 37.54  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  85 REVEVVPSNMWGGQGLLGASVRFcsfrraSEQVWHVLDVEPSSPAALAGLRPYtDYVV---GSDQILQESEDFFTLIESH 161
Cdd:COG0793    46 EEYEDFQESTSGEFGGLGAELGE------EDGKVVVVSVIPGSPAEKAGIKPG-DIILaidGKSVAGLTLDDAVKLLRGK 118

                          90       100
                  ....*....|....*....|...
gi 2462591955 162 EGKPLKLMVYNSKSDSCREVTVT 184
Cdd:COG0793   119 AGTKVTLTIKRPGEGEPITVTLT 141
Peptidase_M50 pfam02163
Peptidase family M50;
19-102 8.59e-03

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 37.47  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462591955  19 PARSVFQQVQENSPAQQAGLEPYfDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKtmRVREVEVVPsNMWGGQ 98
Cdd:pfam02163  92 PAPPVIGGVAPGSPAAKAGLKPG-DVILSINGKKITSWQD-LVEALAKSPGKPITLTVERGG--QTLTVTITP-KSSEES 166


                  ....
gi 2462591955  99 GLLG 102
Cdd:pfam02163 167 KFIG 170
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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