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Conserved domains on  [gi|1808736465]
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Chain A, Sequestosome-1

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 4-102 6.65e-41

The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


:

Pssm-ID: 99723  Cd Length: 87  Bit Score: 130.53  E-value: 6.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808736465   4 LTVKAYLLGKeDAAREIRRFSFCCSPEPEaeaeaaagpgpCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd06402     1 LTVKAYLLGK-DANAEIRRFAIDEDVSTS-----------YEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEEL 68

                          90
                  ....*....|....*....
gi 1808736465  84 TMAMSYVKDDIFRIYIKEK 102
Cdd:cd06402    69 VMALGSLNDDTFRIYIKEK 87
 
Name Accession Description Interval E-value
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 4-102 6.65e-41

The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99723  Cd Length: 87  Bit Score: 130.53  E-value: 6.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808736465   4 LTVKAYLLGKeDAAREIRRFSFCCSPEPEaeaeaaagpgpCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd06402     1 LTVKAYLLGK-DANAEIRRFAIDEDVSTS-----------YEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEEL 68

                          90
                  ....*....|....*....
gi 1808736465  84 TMAMSYVKDDIFRIYIKEK 102
Cdd:cd06402    69 VMALGSLNDDTFRIYIKEK 87
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 3-99 2.64e-12

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 57.60  E-value: 2.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808736465    3 SLTVKAYLLGkedaarEIRRFSFCCSPEpeaeaeaaagpgpCERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEE 82
Cdd:smart00666   1 TVDVKLRYGG------ETRRLSVPRDIS-------------FEDLRSKVAKRFG-LDNQSFTLKYQDEDGDLVSLTSDED 60

                           90       100
                   ....*....|....*....|
gi 1808736465   83 LTMAMSYVK---DDIFRIYI 99
Cdd:smart00666  61 LEEAIEEYDslgSKKLRLHV 80
PB1 pfam00564
PB1 domain;
44-102 1.17e-10

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 53.45  E-value: 1.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1808736465  44 CERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVK---DDIFRIYIKEK 102
Cdd:pfam00564  24 FEELRALVEQRFG-LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARslgSKSLRLHVFPT 84
 
Name Accession Description Interval E-value
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 4-102 6.65e-41

The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) involved in cell signaling, receptor internalization, and protein turnover. The PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99723  Cd Length: 87  Bit Score: 130.53  E-value: 6.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808736465   4 LTVKAYLLGKeDAAREIRRFSFCCSPEPEaeaeaaagpgpCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd06402     1 LTVKAYLLGK-DANAEIRRFAIDEDVSTS-----------YEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEEL 68

                          90
                  ....*....|....*....
gi 1808736465  84 TMAMSYVKDDIFRIYIKEK 102
Cdd:cd06402    69 VMALGSLNDDTFRIYIKEK 87
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 3-99 2.64e-12

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 57.60  E-value: 2.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808736465    3 SLTVKAYLLGkedaarEIRRFSFCCSPEpeaeaeaaagpgpCERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEE 82
Cdd:smart00666   1 TVDVKLRYGG------ETRRLSVPRDIS-------------FEDLRSKVAKRFG-LDNQSFTLKYQDEDGDLVSLTSDED 60

                           90       100
                   ....*....|....*....|
gi 1808736465   83 LTMAMSYVK---DDIFRIYI 99
Cdd:smart00666  61 LEEAIEEYDslgSKKLRLHV 80
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 4-100 3.02e-11

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 54.98  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808736465   4 LTVKAYLLGkedaarEIRRFSFCCSPEPeaeaeaaagpgpCERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd05992     1 VRVKVKYGG------EIRRFVVVSRSIS------------FEDLRSKIAEKFG-LDAVSFKLKYPDEDGDLVTISSDEDL 61

                          90       100
                  ....*....|....*....|
gi 1808736465  84 TMAMSYVK---DDIFRIYIK 100
Cdd:cd05992    62 EEAIEEARrsgSKKLRLFVF 81
PB1 pfam00564
PB1 domain;
44-102 1.17e-10

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 53.45  E-value: 1.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1808736465  44 CERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVK---DDIFRIYIKEK 102
Cdd:pfam00564  24 FEELRALVEQRFG-LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARslgSKSLRLHVFPT 84
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
 47-89 2.13e-04

The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with sulfur stress inducible UP9 protein. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99720  Cd Length: 91  Bit Score: 37.39  E-value: 2.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1808736465  47 LLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSY 89
Cdd:cd06398    30 LREKVEELFSLSPDADLSLTYTDEDGDVVTLVDDNDLTDAIQY 72
 
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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