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Conserved domains on  [gi|149018254|gb|EDL76895|]
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rCG25352, isoform CRA_b [Rattus norvegicus]

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 ...
 68-204 3.62e-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: 3.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254   68 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSD-QILQESE 146
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 149018254  147 DFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQ 204
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPVV 138
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 14-99 6.67e-19

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: 82.70  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254   14 EGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQG 93
Cdd:pfam04495  43 NVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEG 121


                  ....*.
gi 149018254   94 LLGASV 99
Cdd:pfam04495 122 ALGCGL 127
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 210-419 4.91e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  210 KKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPghgtadyggcl 289
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----------- 2932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  290 hsMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSSNTSVCPSLSSS--SLLTPTAVSALGPEDIGSSSSSHERGGEATWSGS 367
Cdd:PHA03247 2933 --PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVprFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 149018254  368 -EFEISFPDSPGSQAQVDHLP-RLTLPDGLTSAASPEEGLSAELLEAQTEEPAD 419
Cdd:PHA03247 3011 lALHEETDPPPVSLKQTLWPPdDTEDSDADSLFDSDSERSDLEALDPLPPEPHD 3064
 
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 3.62e-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: 3.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254   68 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSD-QILQESE 146
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 149018254  147 DFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQ 204
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPVV 138
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
94-303 6.36e-24

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 103.29  E-value: 6.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  94 LLGASVRFCSFRRASEHVWHVLDVE-PSSPAALAGLRPYTDYIVGSD--QILQESE-DFFTLIESHEGKPLKLMVYNSES 169
Cdd:COG5233  170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSSdgQPLEIGElDLEDVNESPVNLPLSLYYYNPID 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254 170 DSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQykkPPSASSPGTPAKTPQPNAFPLGAP----PPWPIPQdSS 245
Cdd:COG5233  250 DQERAKTERDGVHKGIVGILGCQVGHGFLHRLPLAGVGQ---KPQLQKLGTTKRTEDPESHQVEQRgveeNFLPIPK-PD 325

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149018254 246 GPELGSRQSDYMEALPQVPGG----------------FMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQ 303
Cdd:COG5233  326 THRSEFAAKNFLSSLPLSFYGkksehksgtqravttsYHEENGECPLCFKHEEKDRSSESSGEYTPLAPPPSLS 399
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 14-99 6.67e-19

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: 82.70  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254   14 EGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQG 93
Cdd:pfam04495  43 NVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEG 121


                  ....*.
gi 149018254   94 LLGASV 99
Cdd:pfam04495 122 ALGCGL 127
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 14-79 1.07e-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: 1.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149018254  14 EGFHLHGVQENSPAQQAGLEPyFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF---NMKTMRVR 79
Cdd:cd10838   33 DGVLIMQVLPNSPAARAGLRR-GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLrgdRRQTLAVK 100
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 117-179 5.21e-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: 38.71  E-value: 5.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149018254 117 VEPSSPAALAGLRPyTDYIV-GSDQILQESEDFFTLIESHEGKPLKLMVynsESD-SCREVTVTP 179
Cdd:cd23081    6 VVANSPAAEAGLKP-GDRILkIDGQKVRTWEDIVRIVRENPGKPLTLKI---ERDgKILTVTVTP 66
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 20-106 6.77e-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: 41.61  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  20 GVQENSPAQQAGLEPYfDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVfnmktMR---VREVEVVP-SNMWGGQGLL 95
Cdd:COG0750  134 EVVPGSPAAKAGLQPG-DRIVAINGQPVTSWDD-LVDIIRASPGKPLTLTV-----ERdgeELTLTVTPrLVEEDGVGRI 206

                         90
                 ....*....|.
gi 149018254  96 GASVRFCSFRR 106
Cdd:COG0750  207 GVSPSGEVVTV 217
PHA03247 PHA03247
large tegument protein UL36; Provisional
 210-419 4.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  210 KKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPghgtadyggcl 289
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----------- 2932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  290 hsMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSSNTSVCPSLSSS--SLLTPTAVSALGPEDIGSSSSSHERGGEATWSGS 367
Cdd:PHA03247 2933 --PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVprFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 149018254  368 -EFEISFPDSPGSQAQVDHLP-RLTLPDGLTSAASPEEGLSAELLEAQTEEPAD 419
Cdd:PHA03247 3011 lALHEETDPPPVSLKQTLWPPdDTEDSDADSLFDSDSERSDLEALDPLPPEPHD 3064
 
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 3.62e-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: 3.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254   68 LEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSD-QILQESE 146
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 149018254  147 DFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQ 204
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPVV 138
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
94-303 6.36e-24

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 103.29  E-value: 6.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  94 LLGASVRFCSFRRASEHVWHVLDVE-PSSPAALAGLRPYTDYIVGSD--QILQESE-DFFTLIESHEGKPLKLMVYNSES 169
Cdd:COG5233  170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSSdgQPLEIGElDLEDVNESPVNLPLSLYYYNPID 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254 170 DSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQykkPPSASSPGTPAKTPQPNAFPLGAP----PPWPIPQdSS 245
Cdd:COG5233  250 DQERAKTERDGVHKGIVGILGCQVGHGFLHRLPLAGVGQ---KPQLQKLGTTKRTEDPESHQVEQRgveeNFLPIPK-PD 325

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149018254 246 GPELGSRQSDYMEALPQVPGG----------------FMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQ 303
Cdd:COG5233  326 THRSEFAAKNFLSSLPLSFYGkksehksgtqravttsYHEENGECPLCFKHEEKDRSSESSGEYTPLAPPPSLS 399
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 14-99 6.67e-19

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: 82.70  E-value: 6.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254   14 EGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQG 93
Cdd:pfam04495  43 NVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLLKGEDD-LYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEG 121


                  ....*.
gi 149018254   94 LLGASV 99
Cdd:pfam04495 122 ALGCGL 127
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 14-79 1.07e-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: 1.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149018254  14 EGFHLHGVQENSPAQQAGLEPyFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF---NMKTMRVR 79
Cdd:cd10838   33 DGVLIMQVLPNSPAARAGLRR-GDVIQAVDGQPVTTADDVQRIVEQAGVGEELELTVLrgdRRQTLAVK 100
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 114-190 2.57e-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: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254 114 VLDVEPSSPAALAGLRPyTDYIVGSD-QILQESEDFFTLIESHEGKPLKLMVY-NSESdscREVTVTPNA-AWGGEGSLG 190
Cdd:COG0750  132 VGEVVPGSPAAKAGLQP-GDRIVAINgQPVTSWDDLVDIIRASPGKPLTLTVErDGEE---LTLTVTPRLvEEDGVGRIG 207
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 117-179 5.21e-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: 38.71  E-value: 5.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149018254 117 VEPSSPAALAGLRPyTDYIV-GSDQILQESEDFFTLIESHEGKPLKLMVynsESD-SCREVTVTP 179
Cdd:cd23081    6 VVANSPAAEAGLKP-GDRILkIDGQKVRTWEDIVRIVRENPGKPLTLKI---ERDgKILTVTVTP 66
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 20-106 6.77e-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: 41.61  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  20 GVQENSPAQQAGLEPYfDFIITIGHSRLNKENDtLKALLKANVEKPVKLEVfnmktMR---VREVEVVP-SNMWGGQGLL 95
Cdd:COG0750  134 EVVPGSPAAKAGLQPG-DRIVAINGQPVTSWDD-LVDIIRASPGKPLTLTV-----ERdgeELTLTVTPrLVEEDGVGRI 206

                         90
                 ....*....|.
gi 149018254  96 GASVRFCSFRR 106
Cdd:COG0750  207 GVSPSGEVVTV 217
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
23-99 1.07e-03

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 41.27  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149018254  23 ENSPAQQAGLEPYFDFIITIGHSRLNKENDT-LKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASV 99
Cdd:COG5233  196 QDKPPAYALLSPDEDYIDGSSDGQPLEIGELdLEDVNESPVNLPLSLYYYNPIDDQERAKTERDGVHKGIVGILGCQV 273
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 20-96 2.03e-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: 37.17  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  20 GVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKAlLKANVEKPVKLEVfnmktMR---VREVEVVPSNM---WGGQG 93
Cdd:cd23081    5 EVVANSPAAEAGLKPG-DRILKIDGQKVRTWEDIVRI-VRENPGKPLTLKI-----ERdgkILTVTVTPELVeveGKGVG 77


                 ...
gi 149018254  94 LLG 96
Cdd:cd23081   78 RIG 80
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
21-85 2.74e-03

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 40.19  E-value: 2.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149018254  21 VQENSPAQQAGLEPYfDFIITIGHSRLNKENdtLKALLK-ANVEKPVKLEVFNMKtmRVREVEVVP 85
Cdd:COG3975  501 VLWGSPAYKAGLSAG-DELLAIDGLRVTADN--LDDALAaYKPGDPIELLVFRRD--ELRTVTVTL 561
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 79-178 4.78e-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: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  79 REVEVVPSNMWGGQGLLGASVRFcsfrraSEHVWHVLDVEPSSPAALAGLRPYtDYIV---GSDQILQESEDFFTLIESH 155
Cdd:COG0793   46 EEYEDFQESTSGEFGGLGAELGE------EDGKVVVVSVIPGSPAEKAGIKPG-DIILaidGKSVAGLTLDDAVKLLRGK 118

                         90       100
                 ....*....|....*....|...
gi 149018254 156 EGKPLKLMVYNSESDSCREVTVT 178
Cdd:COG0793  119 AGTKVTLTIKRPGEGEPITVTLT 141
PHA03247 PHA03247
large tegument protein UL36; Provisional
 210-419 4.91e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  210 KKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPghgtadyggcl 289
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----------- 2932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018254  290 hsMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSSNTSVCPSLSSS--SLLTPTAVSALGPEDIGSSSSSHERGGEATWSGS 367
Cdd:PHA03247 2933 --PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVprFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASS 3010

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 149018254  368 -EFEISFPDSPGSQAQVDHLP-RLTLPDGLTSAASPEEGLSAELLEAQTEEPAD 419
Cdd:PHA03247 3011 lALHEETDPPPVSLKQTLWPPdDTEDSDADSLFDSDSERSDLEALDPLPPEPHD 3064
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 20-85 4.96e-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: 4.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149018254  20 GVQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVfnmktMR---VREVEVVP 85
Cdd:COG0265  207 RVEPGSPAAKAGLRPG-DVILAVDGKPVTSARDLQRLLASLKPGDTVTLTV-----LRggkELTVTVTL 269
PDZ_2 pfam13180
PDZ domain;
21-71 6.24e-03

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 35.33  E-value: 6.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 149018254   21 VQENSPAQQAGLEPYfDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVF 71
Cdd:pfam13180  13 VKSSGPAAKAGLKAG-DVILSIDGRKINDLTDLESALYGHKPGDTVTLQVY 62
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 113-162 6.39e-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: 6.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 149018254  113 HVLDVEPSSPAALAGLRPyTDYIVGSD-QILQESEDFFTLIESHEGKPLKL 162
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRV-GDVILAVNgKPVRSLEDVARLLQGSAGESVTL 50
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 114-179 6.77e-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: 6.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149018254 114 VLDVEPSSPAALAGLRPYtDYIVGSD-QILQESEDFFTLIESHE-GKPLKLMVY-NSESdscREVTVTP 179
Cdd:COG0265  205 VARVEPGSPAAKAGLRPG-DVILAVDgKPVTSARDLQRLLASLKpGDTVTLTVLrGGKE---LTVTVTL 269
Peptidase_M50 pfam02163
Peptidase family M50;
114-180 7.35e-03

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 38.24  E-value: 7.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149018254  114 VLDVEPSSPAALAGLRPyTDYIVGSD-QILQESEDFFTLIESHEGKPLKLMVYNSESDscREVTVTPN 180
Cdd:pfam02163  97 IGGVAPGSPAAKAGLKP-GDVILSINgKKITSWQDLVEALAKSPGKPITLTVERGGQT--LTVTITPK 161
 
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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