NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148701771|gb|EDL33718|]
View 

sequestosome 1, isoform CRA_b, partial [Mus musculus]

Protein Classification

sequestosome-1; ZZ-type zinc finger protein( domain architecture ID 10157364)

sequestosome-1 (SQSTM) functions as a bridge between polyubiquitinated cargo and autophagosomes| ZZ-type zinc finger protein may function as a molecular serve as scaffold in various cell signaling pathways

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 8-105 6.53e-38

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: 131.69  E-value: 6.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148701771   8 TVKAYLLGKEEAtREIRRFSFCfspepeaeaqaAAGPGPCERLLSRVAVLFPTLRPGGFQAHYRDEDGDLVAFSSDEELT 87
Cdd:cd06402    2 TVKAYLLGKDAN-AEIRRFAID-----------EDVSTSYEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEELV 69

                         90
                 ....*....|....*...
gi 148701771  88 MAMSYVKDDIFRIYIKEK 105
Cdd:cd06402   70 MALGSLNDDTFRIYIKEK 87
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 129-169 6.48e-22

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


:

Pssm-ID: 239080  Cd Length: 43  Bit Score: 87.70  E-value: 6.48e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148701771 129 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHREHSKL 169
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAML 41
 
Name Accession Description Interval E-value
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 8-105 6.53e-38

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: 131.69  E-value: 6.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148701771   8 TVKAYLLGKEEAtREIRRFSFCfspepeaeaqaAAGPGPCERLLSRVAVLFPTLRPGGFQAHYRDEDGDLVAFSSDEELT 87
Cdd:cd06402    2 TVKAYLLGKDAN-AEIRRFAID-----------EDVSTSYEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEELV 69

                         90
                 ....*....|....*...
gi 148701771  88 MAMSYVKDDIFRIYIKEK 105
Cdd:cd06402   70 MALGSLNDDTFRIYIKEK 87
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 129-169 6.48e-22

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 87.70  E-value: 6.48e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148701771 129 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHREHSKL 169
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAML 41
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 125-167 3.63e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.00  E-value: 3.63e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 148701771   125 VHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKG-LHREHS 167
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGsAGGEHS 44
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 6-102 9.72e-13

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: 63.38  E-value: 9.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148701771     6 SFTVKAYLLGkeeatrEIRRFSFCFSPepeaeaqaaagpgPCERLLSRVAVLFPtLRPGGFQAHYRDEDGDLVAFSSDEE 85
Cdd:smart00666   1 TVDVKLRYGG------ETRRLSVPRDI-------------SFEDLRSKVAKRFG-LDNQSFTLKYQDEDGDLVSLTSDED 60

                           90       100
                   ....*....|....*....|
gi 148701771    86 LTMAMSYVK---DDIFRIYI 102
Cdd:smart00666  61 LEEAIEEYDslgSKKLRLHV 80
PB1 pfam00564
PB1 domain;
46-105 8.50e-11

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 57.69  E-value: 8.50e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148701771   46 PCERLLSRVAVLFPtLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVK---DDIFRIYIKEK 105
Cdd:pfam00564  23 SFEELRALVEQRFG-LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARslgSKSLRLHVFPT 84
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 126-166 1.85e-08

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 50.17  E-value: 1.85e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 148701771  126 HPNVICDGC-NGPVVGTRYKCSVCPDYDLCSVCEGKGLHREH 166
Cdd:pfam00569   2 HKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNH 43
 
Name Accession Description Interval E-value
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
 8-105 6.53e-38

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: 131.69  E-value: 6.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148701771   8 TVKAYLLGKEEAtREIRRFSFCfspepeaeaqaAAGPGPCERLLSRVAVLFPTLRPGGFQAHYRDEDGDLVAFSSDEELT 87
Cdd:cd06402    2 TVKAYLLGKDAN-AEIRRFAID-----------EDVSTSYEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEELV 69

                         90
                 ....*....|....*...
gi 148701771  88 MAMSYVKDDIFRIYIKEK 105
Cdd:cd06402   70 MALGSLNDDTFRIYIKEK 87
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 129-169 6.48e-22

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 87.70  E-value: 6.48e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 148701771 129 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHREHSKL 169
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAML 41
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 125-167 3.63e-15

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 69.00  E-value: 3.63e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 148701771   125 VHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKG-LHREHS 167
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGsAGGEHS 44
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 6-102 9.72e-13

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: 63.38  E-value: 9.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148701771     6 SFTVKAYLLGkeeatrEIRRFSFCFSPepeaeaqaaagpgPCERLLSRVAVLFPtLRPGGFQAHYRDEDGDLVAFSSDEE 85
Cdd:smart00666   1 TVDVKLRYGG------ETRRLSVPRDI-------------SFEDLRSKVAKRFG-LDNQSFTLKYQDEDGDLVSLTSDED 60

                           90       100
                   ....*....|....*....|
gi 148701771    86 LTMAMSYVK---DDIFRIYI 102
Cdd:smart00666  61 LEEAIEEYDslgSKKLRLHV 80
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 129-167 1.55e-12

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 61.68  E-value: 1.55e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 148701771 129 VICDGCNGPVVGTRYKCSVCPDYDLCSVC--EGKGLH-REHS 167
Cdd:cd02249    1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCyaKGKKGHpPDHS 42
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 7-103 1.83e-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: 59.60  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148701771   7 FTVKAYLLGkeeatrEIRRFSFCfspepeaeaqaaAGPGPCERLLSRVAVLFPtLRPGGFQAHYRDEDGDLVAFSSDEEL 86
Cdd:cd05992    1 VRVKVKYGG------EIRRFVVV------------SRSISFEDLRSKIAEKFG-LDAVSFKLKYPDEDGDLVTISSDEDL 61

                         90       100
                 ....*....|....*....|
gi 148701771  87 TMAMSYVK---DDIFRIYIK 103
Cdd:cd05992   62 EEAIEEARrsgSKKLRLFVF 81
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 129-166 4.43e-11

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 57.47  E-value: 4.43e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 148701771 129 VICDGCN-GPVVGTRYKCSVCPDYDLCSVCEGKGLHR-EH 166
Cdd:cd02339    1 IICDTCRkQGIIGIRWKCAECPNYDLCTTCYHGDKHDlEH 40
PB1 pfam00564
PB1 domain;
46-105 8.50e-11

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 57.69  E-value: 8.50e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148701771   46 PCERLLSRVAVLFPtLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVK---DDIFRIYIKEK 105
Cdd:pfam00564  23 SFEELRALVEQRFG-LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARslgSKSLRLHVFPT 84
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 126-166 1.85e-08

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 50.17  E-value: 1.85e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 148701771  126 HPNVICDGC-NGPVVGTRYKCSVCPDYDLCSVCEGKGLHREH 166
Cdd:pfam00569   2 HKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNH 43
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 131-169 1.70e-05

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 41.78  E-value: 1.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 148701771 131 CDGCNGpVVGTRYKCSVCPDYDLCSVC-EGKGLHREHSKL 169
Cdd:cd02337    3 CNECKH-HVETRWHCTVCEDYDLCITCyNTKNHPHKMEKL 41
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 129-157 1.81e-05

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 41.56  E-value: 1.81e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 148701771 129 VICDGC-NGPVVGTRYKCSVCPDYDLCSVC 157
Cdd:cd02338    1 VSCDGCgKSNFTGRRYKCLICYDYDLCADC 30
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 131-170 3.22e-05

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239081  Cd Length: 48  Bit Score: 40.88  E-value: 3.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 148701771 131 CDGCN-GPVVGTRYKCSVCP--DYDLCSVC-EGKGLHREHSKLI 170
Cdd:cd02341    3 CDSCGiEPIPGTRYHCSECDdgDFDLCQDCvVKGESHQEDHWLV 46
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
 131-157 5.75e-05

Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239082  Cd Length: 43  Bit Score: 40.26  E-value: 5.75e-05
                         10        20
                 ....*....|....*....|....*...
gi 148701771 131 CDGCN-GPVVGTRYKCSVCPDYDLCSVC 157
Cdd:cd02342    3 CDGCGvLPITGPRYKSKVKEDYDLCTIC 30
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
 129-157 1.24e-04

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239084  Cd Length: 45  Bit Score: 39.10  E-value: 1.24e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 148701771 129 VICDGCNG-PVVGTRYKCSVCPDYDLCSVC 157
Cdd:cd02344    1 VTCDGCQMfPINGPRFKCRNCDDFDFCENC 30
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 131-157 5.59e-04

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 37.66  E-value: 5.59e-04
                         10        20
                 ....*....|....*....|....*...
gi 148701771 131 CDGCNGPVVGT-RYKCSVCPDYDLCSVC 157
Cdd:cd02335    3 CDYCSKDITGTiRIKCAECPDFDLCLEC 30
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
 50-92 2.08e-03

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: 37.00  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 148701771  50 LLSRVAVLFPTLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSY 92
Cdd:cd06398   30 LREKVEELFSLSPDADLSLTYTDEDGDVVTLVDDNDLTDAIQY 72
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 129-168 3.25e-03

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 35.41  E-value: 3.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 148701771 129 VICDGCNG-PVVGTRYKCSVCPDYDLCSVCEGKGLH-REHSK 168
Cdd:cd02334    1 AKCNICKEfPITGFRYRCLKCFNYDLCQSCFFSGRTsKSHKN 42
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 131-161 4.52e-03

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.


Pssm-ID: 239085  Cd Length: 49  Bit Score: 34.87  E-value: 4.52e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 148701771 131 CDGCN-GPVVGTRYKCSVCPDYDLCSVCEGKG 161
Cdd:cd02345    3 CSACRkQDISGIRFPCQVCRDYSLCLGCYTKG 34
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH