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Conserved domains on  [gi|224967109|ref|NP_081628|]
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Golgi reassembly-stacking protein 2 [Mus musculus]

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 ...
 69-204 8.07e-81

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: 246.02  E-value: 8.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   69 MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGAD-TVMNESE 147
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224967109  148 DLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT 204
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPV 137
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 14-100 9.82e-20

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: 85.01  E-value: 9.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   14 TEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLnKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQ 93
Cdd:pfam04495  42 ENVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLL-KGEDDLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGE 120


                  ....*..
gi 224967109   94 GLLGVSI 100
Cdd:pfam04495 121 GALGCGL 127
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 248-422 6.89e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  248 GTTGVEQSLSGLSISSAPPAVSNVLST-GVPTVPLLPPQVNQSLASMPPMNPATTLPSLMPLSAGLPSLPNLPSLSNFNL 326
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  327 PAPHIMPGVGLPELGSPGLPPLPSLPPRNLPGIAPLPMLSDFLPSfPLVPEGSSAasAGEPLSSLPAMGPPSDPVMTTAK 406
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-SLPLGGSVA--PGGDVRRRPPSRSPAAKPAAPAR 2880

                         170
                  ....*....|....*.
gi 224967109  407 ADASSLTVDVTSPASK 422
Cdd:PHA03247 2881 PPVRRLARPAVSRSTE 2896
 
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 ...
 69-204 8.07e-81

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: 246.02  E-value: 8.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   69 MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGAD-TVMNESE 147
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224967109  148 DLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT 204
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPV 137
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 14-100 9.82e-20

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: 85.01  E-value: 9.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   14 TEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLnKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQ 93
Cdd:pfam04495  42 ENVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLL-KGEDDLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGE 120


                  ....*..
gi 224967109   94 GLLGVSI 100
Cdd:pfam04495 121 GALGCGL 127
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
95-223 3.76e-18

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 85.95  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  95 LLGVSIRFCSFDGANENVWHVLEVE-SNSPAALAGLRPHSDYIIGA-DTVMNES--EDLFSLIETHEAKPLKLYVYNTDT 170
Cdd:COG5233  170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSsDGQPLEIgeLDLEDVNESPVNLPLSLYYYNPID 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 224967109 171 DNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT---RPFEEGKKISLPGQMTGTP 223
Cdd:COG5233  250 DQERAKTERDGVHKGIVGILGCQVGHGFLHRLPLagvGQKPQLQKLGTTKRTEDPE 305
PHA03247 PHA03247
large tegument protein UL36; Provisional
 248-422 6.89e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  248 GTTGVEQSLSGLSISSAPPAVSNVLST-GVPTVPLLPPQVNQSLASMPPMNPATTLPSLMPLSAGLPSLPNLPSLSNFNL 326
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  327 PAPHIMPGVGLPELGSPGLPPLPSLPPRNLPGIAPLPMLSDFLPSfPLVPEGSSAasAGEPLSSLPAMGPPSDPVMTTAK 406
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-SLPLGGSVA--PGGDVRRRPPSRSPAAKPAAPAR 2880

                         170
                  ....*....|....*.
gi 224967109  407 ADASSLTVDVTSPASK 422
Cdd:PHA03247 2881 PPVRRLARPAVSRSTE 2896
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 19-99 7.92e-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: 44.69  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  19 VLRVQENSPGHRAGLEPfFDFIVSINGSRLNkDNDTLKDLLKANVEKPVKMLIY-SSKTLELreaSVTP-SNLWGGQGLL 96
Cdd:COG0750  132 VGEVVPGSPAAKAGLQP-GDRIVAINGQPVT-SWDDLVDIIRASPGKPLTLTVErDGEELTL---TVTPrLVEEDGVGRI 206


                 ...
gi 224967109  97 GVS 99
Cdd:COG0750  207 GVS 209
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 14-53 3.59e-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: 39.61  E-value: 3.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 224967109  14 TEGYHVLRVQENSPGHRAGLEPfFDFIVSINGSRLNKDND 53
Cdd:cd10838   32 VDGVLIMQVLPNSPAARAGLRR-GDVIQAVDGQPVTTADD 70
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 19-75 4.66e-04

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: 38.90  E-value: 4.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 224967109    19 VLRVQENSPGHRAGLEPfFDFIVSINGSRL-NKDNDTLKDLLKANVEKpVKMLIYSSK 75
Cdd:smart00228  30 VSSVVPGSPAAKAGLRV-GDVILEVNGTSVeGLTHLEAVDLLKKAGGK-VTLTVLRGG 85
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 14-140 8.34e-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: 41.44  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   14 TEGYHVLRVQENSPGHRAGLEPFfDFIVSINGSRLNKDND------TLK-------DLLKANVEKPVKMLIYSSKTLELR 80
Cdd:TIGR02037 256 QRGALVAQVLPGSPAEKAGLKAG-DVITSVNGKPISSFADlrraigTLKpgkkvtlGILRKGKEKTITVTLGASPEEQAS 334

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967109   81 EASVTPsnlwggqGLLGVSIRFCSFDGANENVWH----VLEVESNSPAALAGLRPhSDYIIGAD 140
Cdd:TIGR02037 335 SSNPFL-------GLTVANLSPEIRKELRLKGDVkgvvVTKVVSGSPAARAGLQP-GDVILSVN 390
 
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 ...
 69-204 8.07e-81

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: 246.02  E-value: 8.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   69 MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGAD-TVMNESE 147
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 224967109  148 DLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT 204
Cdd:pfam04495  81 DLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGEGALGCGLGYGLLHRIPV 137
GRASP55_65 pfam04495
GRASP55/65 PDZ-like domain; GRASP55 (Golgi re-assembly stacking protein of 55 kDa) and GRASP65 ...
 14-100 9.82e-20

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: 85.01  E-value: 9.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   14 TEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLnKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQ 93
Cdd:pfam04495  42 ENVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLL-KGEDDLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGE 120


                  ....*..
gi 224967109   94 GLLGVSI 100
Cdd:pfam04495 121 GALGCGL 127
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
95-223 3.76e-18

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 85.95  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  95 LLGVSIRFCSFDGANENVWHVLEVE-SNSPAALAGLRPHSDYIIGA-DTVMNES--EDLFSLIETHEAKPLKLYVYNTDT 170
Cdd:COG5233  170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSsDGQPLEIgeLDLEDVNESPVNLPLSLYYYNPID 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 224967109 171 DNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT---RPFEEGKKISLPGQMTGTP 223
Cdd:COG5233  250 DQERAKTERDGVHKGIVGILGCQVGHGFLHRLPLagvGQKPQLQKLGTTKRTEDPE 305
PHA03247 PHA03247
large tegument protein UL36; Provisional
 248-422 6.89e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  248 GTTGVEQSLSGLSISSAPPAVSNVLST-GVPTVPLLPPQVNQSLASMPPMNPATTLPSLMPLSAGLPSLPNLPSLSNFNL 326
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  327 PAPHIMPGVGLPELGSPGLPPLPSLPPRNLPGIAPLPMLSDFLPSfPLVPEGSSAasAGEPLSSLPAMGPPSDPVMTTAK 406
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-SLPLGGSVA--PGGDVRRRPPSRSPAAKPAAPAR 2880

                         170
                  ....*....|....*.
gi 224967109  407 ADASSLTVDVTSPASK 422
Cdd:PHA03247 2881 PPVRRLARPAVSRSTE 2896
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 18-71 3.98e-05

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 40.97  E-value: 3.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 224967109   18 HVLRVQENSPGHRAGLEPfFDFIVSINGSRLNKDNDtLKDLLKANVEKPVKMLI 71
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRV-GDVILAVNGKPVRSLED-VARLLQGSAGESVTLTV 52
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 19-99 7.92e-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: 44.69  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  19 VLRVQENSPGHRAGLEPfFDFIVSINGSRLNkDNDTLKDLLKANVEKPVKMLIY-SSKTLELreaSVTP-SNLWGGQGLL 96
Cdd:COG0750  132 VGEVVPGSPAAKAGLQP-GDRIVAINGQPVT-SWDDLVDIIRASPGKPLTLTVErDGEELTL---TVTPrLVEEDGVGRI 206


                 ...
gi 224967109  97 GVS 99
Cdd:COG0750  207 GVS 209
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
19-86 2.90e-04

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 43.27  E-value: 2.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224967109  19 VLRVQENSPGHRAGLEPfFDFIVSINGSRLNKDNdtLKDLLK-ANVEKPVKMLIYSSKtlELREASVTP 86
Cdd:COG3975  498 VTSVLWGSPAYKAGLSA-GDELLAIDGLRVTADN--LDDALAaYKPGDPIELLVFRRD--ELRTVTVTL 561
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 14-53 3.59e-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: 39.61  E-value: 3.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 224967109  14 TEGYHVLRVQENSPGHRAGLEPfFDFIVSINGSRLNKDND 53
Cdd:cd10838   32 VDGVLIMQVLPNSPAARAGLRR-GDVIQAVDGQPVTTADD 70
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 5-79 4.52e-04

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: 39.16  E-value: 4.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224967109   5 QSVEIPGGGTEGYHVLRVQENSPGHRAGLEPfFDFIVSINGSRLNKDNDTLKDLLKANVEKPVKMLIY---SSKTLEL 79
Cdd:cd06781   20 QSLKLPSNVNKGVYVAQVQSNSPAEKAGLKK-GDVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYrdgKEKTLNI 96
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 19-75 4.66e-04

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: 38.90  E-value: 4.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 224967109    19 VLRVQENSPGHRAGLEPfFDFIVSINGSRL-NKDNDTLKDLLKANVEKpVKMLIYSSK 75
Cdd:smart00228  30 VSSVVPGSPAAKAGLRV-GDVILEVNGTSVeGLTHLEAVDLLKKAGGK-VTLTVLRGG 85
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 21-85 7.77e-04

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing 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.


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 38.73  E-value: 7.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224967109  21 RVQENSPGHRAGLEPfFDFIVSINGsrlnkdndtlKDLLKANVEKPVKMLIYSSKTLELREASVT 85
Cdd:cd06746   48 SVDPGGVADKAGLKK-GDFLLEING----------EDVVKASHEQVVNLIRQSGNTLVLKVVTVT 101
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 14-140 8.34e-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: 41.44  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109   14 TEGYHVLRVQENSPGHRAGLEPFfDFIVSINGSRLNKDND------TLK-------DLLKANVEKPVKMLIYSSKTLELR 80
Cdd:TIGR02037 256 QRGALVAQVLPGSPAEKAGLKAG-DVITSVNGKPISSFADlrraigTLKpgkkvtlGILRKGKEKTITVTLGASPEEQAS 334

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224967109   81 EASVTPsnlwggqGLLGVSIRFCSFDGANENVWH----VLEVESNSPAALAGLRPhSDYIIGAD 140
Cdd:TIGR02037 335 SSNPFL-------GLTVANLSPEIRKELRLKGDVkgvvVTKVVSGSPAARAGLQP-GDVILSVN 390
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 19-46 1.64e-03

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 37.60  E-value: 1.64e-03
                         10        20
                 ....*....|....*....|....*...
gi 224967109  19 VLRVQENSPGHRAGLEPfFDFIVSINGS 46
Cdd:cd06713   39 VCRVHEDSPAYLAGLTA-GDVILSVNGV 65
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 22-99 1.88e-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: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  22 VQENSPGHRAGLEPfFDFIVSINGSRLNKDNDtLKDLLKANVEKPVKMLI-YSSKTLELreaSVTPSN---LWGGQGLLG 97
Cdd:cd23081    6 VVANSPAAEAGLKP-GDRILKIDGQKVRTWED-IVRIVRENPGKPLTLKIeRDGKILTV---TVTPELvevEGKGVGRIG 80


                 ..
gi 224967109  98 VS 99
Cdd:cd23081   81 VQ 82
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 13-45 2.43e-03

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini 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 Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 36.89  E-value: 2.43e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 224967109  13 GTEGYHVLRVQENSPGHRAGLEPfFDFIVSING 45
Cdd:cd06779   23 VNRGVLVAEVIPGSPAAKAGLKE-GDVILSVNG 54
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
17-131 4.18e-03

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 39.35  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  17 YHVLRVQ-ENSPGHRAGLEPFFDFIVSINGSRLNKDNDT-LKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQG 94
Cdd:COG5233  188 SHILNVSiQDKPPAYALLSPDEDYIDGSSDGQPLEIGELdLEDVNESPVNLPLSLYYYNPIDDQERAKTERDGVHKGIVG 267

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 224967109  95 LLGvsirfcsfdganENVWHVleVESNSPAALAGLRP 131
Cdd:COG5233  268 ILG------------CQVGHG--FLHRLPLAGVGQKP 290
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 19-89 5.26e-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: 5.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224967109  19 VLRVQENSPGHRAGLEPfFDFIVSINGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKtlELREASVTPSNL 89
Cdd:COG0265  205 VARVEPGSPAAKAGLRP-GDVILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGG--KELTVTVTLGER 272
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 91-179 7.08e-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: 38.31  E-value: 7.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224967109  91 GGQGLLGVSIRFcsfdgaNENVWHVLEVESNSPAALAGLRPHsDYII---GADTVMNESEDLFSLIETHEAKPLKLYVYN 167
Cdd:COG0793   57 GEFGGLGAELGE------EDGKVVVVSVIPGSPAEKAGIKPG-DIILaidGKSVAGLTLDDAVKLLRGKAGTKVTLTIKR 129

                         90
                 ....*....|..
gi 224967109 168 TDTDNCREVIIT 179
Cdd:COG0793  130 PGEGEPITVTLT 141
 
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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