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Conserved domains on  [gi|5901572|gb|AAD55350|]
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golgi stacking protein homolog GRASP55 [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 ...
 69-204 6.23e-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: 246.41  E-value: 6.23e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572     69 MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGAD-TVMNESE 147
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5901572    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 2.24e-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: 84.24  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572     14 TEGYHVLRVQENSPGHRAGLEPFFDFIVSISGSRLnKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQ 93
Cdd:pfam04495  42 ENVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLL-KGEDDLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGE 120


                  ....*..
gi 5901572     94 GLLGVSI 100
Cdd:pfam04495 121 GALGCGL 127
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 248-422 9.91e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    248 GTAGVEQSLSGLSISSAPPAVSNVLST-GVPTVPLLPPQVNQSLASVPPMNPAATLPSLMPLSAGLPNLPNLPSLSNFNL 326
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    327 PAPHIMPGVGLPELGKPGLPPLPSLPPRNVPGIAPLPMPSDFLPSfPLVPEGSSAasAGEPLSSLPAMGPPSDPVMTTAK 406
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-SLPLGGSVA--PGGDVRRRPPSRSPAAKPAAPAR 2880

                         170
                  ....*....|....*.
gi 5901572    407 ADTSSLTVDVMSPASK 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 6.23e-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: 246.41  E-value: 6.23e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572     69 MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGAD-TVMNESE 147
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5901572    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 2.24e-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: 84.24  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572     14 TEGYHVLRVQENSPGHRAGLEPFFDFIVSISGSRLnKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQ 93
Cdd:pfam04495  42 ENVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLL-KGEDDLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGE 120


                  ....*..
gi 5901572     94 GLLGVSI 100
Cdd:pfam04495 121 GALGCGL 127
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
95-223 2.13e-18

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 86.73  E-value: 2.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572   95 LLGVSIRFCSFDGANENVWHVLEVE-SNSPAALAGLRPHSDYIIGA-DTVMNES--EDLFSLIETHEAKPLKLYVYNTDT 170
Cdd:COG5233 170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSsDGQPLEIgeLDLEDVNESPVNLPLSLYYYNPID 249

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5901572  171 DNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT---RPFEEGKKISLPGQMTGTP 223
Cdd:COG5233 250 DQERAKTERDGVHKGIVGILGCQVGHGFLHRLPLagvGQKPQLQKLGTTKRTEDPE 305
PHA03247 PHA03247
large tegument protein UL36; Provisional
 248-422 9.91e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    248 GTAGVEQSLSGLSISSAPPAVSNVLST-GVPTVPLLPPQVNQSLASVPPMNPAATLPSLMPLSAGLPNLPNLPSLSNFNL 326
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    327 PAPHIMPGVGLPELGKPGLPPLPSLPPRNVPGIAPLPMPSDFLPSfPLVPEGSSAasAGEPLSSLPAMGPPSDPVMTTAK 406
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-SLPLGGSVA--PGGDVRRRPPSRSPAAKPAAPAR 2880

                         170
                  ....*....|....*.
gi 5901572    407 ADTSSLTVDVMSPASK 422
Cdd:PHA03247 2881 PPVRRLARPAVSRSTE 2896
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 19-99 2.00e-03

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 40.07  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572   19 VLRVQENSPGHRAGLEPfFDFIVSISGSRLNkDNDTLKDLLKANVEKPVKMLIY-SSKTLELreaSVTP-SNLWGGQGLL 96
Cdd:COG0750 132 VGEVVPGSPAAKAGLQP-GDRIVAINGQPVT-SWDDLVDIIRASPGKPLTLTVErDGEELTL---TVTPrLVEEDGVGRI 206


                ...
gi 5901572   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 2.02e-03

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: 37.68  E-value: 2.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 5901572   14 TEGYHVLRVQENSPGHRAGLEPfFDFIVSISGSRLNKDND 53
Cdd:cd10838  32 VDGVLIMQVLPNSPAARAGLRR-GDVIQAVDGQPVTTADD 70
 
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 6.23e-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: 246.41  E-value: 6.23e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572     69 MLIYSSKTLELREASVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGAD-TVMNESE 147
Cdd:pfam04495   1 LTVYNAKGQKIRDVYIVPSNTWGGQGLLGLSLRWCSFAKALENVWHVLDVHENSPAAKAGLQPYSDYIIGTPkGLLKGED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5901572    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 2.24e-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: 84.24  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572     14 TEGYHVLRVQENSPGHRAGLEPFFDFIVSISGSRLnKDNDTLKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQ 93
Cdd:pfam04495  42 ENVWHVLDVHENSPAAKAGLQPYSDYIIGTPKGLL-KGEDDLYTLVEDHEDRPLRLYVYNSETDTVREVTITPNRNWGGE 120


                  ....*..
gi 5901572     94 GLLGVSI 100
Cdd:pfam04495 121 GALGCGL 127
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
95-223 2.13e-18

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 86.73  E-value: 2.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572   95 LLGVSIRFCSFDGANENVWHVLEVE-SNSPAALAGLRPHSDYIIGA-DTVMNES--EDLFSLIETHEAKPLKLYVYNTDT 170
Cdd:COG5233 170 LRGKDIQWSRLKDVVCSDSHILNVSiQDKPPAYALLSPDEDYIDGSsDGQPLEIgeLDLEDVNESPVNLPLSLYYYNPID 249

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5901572  171 DNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPT---RPFEEGKKISLPGQMTGTP 223
Cdd:COG5233 250 DQERAKTERDGVHKGIVGILGCQVGHGFLHRLPLagvGQKPQLQKLGTTKRTEDPE 305
PHA03247 PHA03247
large tegument protein UL36; Provisional
 248-422 9.91e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    248 GTAGVEQSLSGLSISSAPPAVSNVLST-GVPTVPLLPPQVNQSLASVPPMNPAATLPSLMPLSAGLPNLPNLPSLSNFNL 326
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAVPAGPATpGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    327 PAPHIMPGVGLPELGKPGLPPLPSLPPRNVPGIAPLPMPSDFLPSfPLVPEGSSAasAGEPLSSLPAMGPPSDPVMTTAK 406
Cdd:PHA03247 2804 PADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP-SLPLGGSVA--PGGDVRRRPPSRSPAAKPAAPAR 2880

                         170
                  ....*....|....*.
gi 5901572    407 ADTSSLTVDVMSPASK 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 9.24e-04

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 37.12  E-value: 9.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 5901572     18 HVLRVQENSPGHRAGLEPfFDFIVSISGSRLNKDNDtLKDLLKANVEKPVKMLI 71
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRV-GDVILAVNGKPVRSLED-VARLLQGSAGESVTLTV 52
GRH1 COG5233
Peripheral Golgi membrane protein [Intracellular trafficking and secretion];
17-131 1.19e-03

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];


Pssm-ID: 227558 [Multi-domain]  Cd Length: 417  Bit Score: 41.27  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572   17 YHVLRVQ-ENSPGHRAGLEPFFDFIVSISGSRLNKDNDT-LKDLLKANVEKPVKMLIYSSKTLELREASVTPSNLWGGQG 94
Cdd:COG5233 188 SHILNVSiQDKPPAYALLSPDEDYIDGSSDGQPLEIGELdLEDVNESPVNLPLSLYYYNPIDDQERAKTERDGVHKGIVG 267

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5901572   95 LLGvsirfcsfdganENVWHVleVESNSPAALAGLRP 131
Cdd:COG5233 268 ILG------------CQVGHG--FLHRLPLAGVGQKP 290
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 19-99 2.00e-03

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 40.07  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572   19 VLRVQENSPGHRAGLEPfFDFIVSISGSRLNkDNDTLKDLLKANVEKPVKMLIY-SSKTLELreaSVTP-SNLWGGQGLL 96
Cdd:COG0750 132 VGEVVPGSPAAKAGLQP-GDRIVAINGQPVT-SWDDLVDIIRASPGKPLTLTVErDGEELTL---TVTPrLVEEDGVGRI 206


                ...
gi 5901572   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 2.02e-03

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: 37.68  E-value: 2.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 5901572   14 TEGYHVLRVQENSPGHRAGLEPfFDFIVSISGSRLNKDND 53
Cdd:cd10838  32 VDGVLIMQVLPNSPAARAGLRR-GDVIQAVDGQPVTTADD 70
PHA03247 PHA03247
large tegument protein UL36; Provisional
 277-452 3.83e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    277 PTVPLLPPQVNqSLASV--PPMNPAATLPSLMPLSAGLPnLPNLPSLSNFNLPAPHIMPGVGLPELGKPGLPPLPSLPPR 354
Cdd:PHA03247 2683 PRRRAARPTVG-SLTSLadPPPPPPTPEPAPHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572    355 NVPGIAPLPMPSDFLPSFP----LVPEGSSAASAgepLSSLPAMGPPSDPVMTTAKADTSSLTVDVMSPASKVPTTVEDR 430
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPprrlTRPAVASLSES---RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT 2837

                         170       180
                  ....*....|....*....|..
gi 5901572    431 VSDCTPAMEKPVSAVTDANASG 452
Cdd:PHA03247 2838 APPPPPGPPPPSLPLGGSVAPG 2859
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 5-79 4.16e-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: 36.46  E-value: 4.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5901572    5 QSVEIPGGGTEGYHVLRVQENSPGHRAGLEPfFDFIVSISGSRLNKDNDTLKDLLKANVEKPVKMLIY---SSKTLEL 79
Cdd:cd06781  20 QSLKLPSNVNKGVYVAQVQSNSPAEKAGLKK-GDVITKLDGKKVESSSDLRQILYSHKVGDTVKVTIYrdgKEKTLNI 96
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
19-86 6.92e-03

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


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 38.65  E-value: 6.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5901572   19 VLRVQENSPGHRAGLEPfFDFIVSISGSRLNKDNdtLKDLLK-ANVEKPVKMLIYSSKtlELREASVTP 86
Cdd:COG3975 498 VTSVLWGSPAYKAGLSA-GDELLAIDGLRVTADN--LDDALAaYKPGDPIELLVFRRD--ELRTVTVTL 561
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 91-179 7.15e-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: 7.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5901572   91 GGQGLLGVSIRFcsfdgaNENVWHVLEVESNSPAALAGLRPHsDYII---GADTVMNESEDLFSLIETHEAKPLKLYVYN 167
Cdd:COG0793  57 GEFGGLGAELGE------EDGKVVVVSVIPGSPAEKAGIKPG-DIILaidGKSVAGLTLDDAVKLLRGKAGTKVTLTIKR 129

                        90
                ....*....|..
gi 5901572  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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