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Conserved domains on  [gi|4505571|ref|NP_003891|]
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sequestosome-1 isoform 1 [Homo sapiens]

Protein Classification

sequestosome-1( domain architecture ID 10866441)

sequestosome-1 (SQSTM) functions as a bridge between polyubiquitinated cargo and autophagosomes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBA_5 pfam16577
UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome ...
379-440 1.47e-41

UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome 1/p62 has recently been shown to interact with polyubiquitinated proteins through its UBA domain. This domain selectively binds K63-polyubiquitinated proteins.


:

Pssm-ID: 318725  Cd Length: 62  Bit Score: 141.34  E-value: 1.47e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505571    379 EAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL 440
Cdd:pfam16577   1 EAALYPHLPPDADPRLIESLAQMLSMGFSDEGGWLTRLLHTKNFDIGAALDAIHFSKHPPPA 62
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
4-102 5.78e-40

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: 138.24  E-value: 5.78e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505571    4 LTVKAYLLGKeDAAREIRRFSFCCSPEPEaeaeaaagpgpCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd06402   1 LTVKAYLLGK-DANAEIRRFAIDEDVSTS-----------YEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEEL 68
                        90
                ....*....|....*....
gi 4505571   84 TMAMSYVKDDIFRIYIKEK 102
Cdd:cd06402  69 VMALGSLNDDTFRIYIKEK 87
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
126-168 1.01e-21

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: 87.32  E-value: 1.01e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4505571  126 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAF 168
Cdd:cd02340   1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
 
Name Accession Description Interval E-value
UBA_5 pfam16577
UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome ...
379-440 1.47e-41

UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome 1/p62 has recently been shown to interact with polyubiquitinated proteins through its UBA domain. This domain selectively binds K63-polyubiquitinated proteins.


Pssm-ID: 318725  Cd Length: 62  Bit Score: 141.34  E-value: 1.47e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505571    379 EAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL 440
Cdd:pfam16577   1 EAALYPHLPPDADPRLIESLAQMLSMGFSDEGGWLTRLLHTKNFDIGAALDAIHFSKHPPPA 62
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
4-102 5.78e-40

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: 138.24  E-value: 5.78e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505571    4 LTVKAYLLGKeDAAREIRRFSFCCSPEPEaeaeaaagpgpCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd06402   1 LTVKAYLLGK-DANAEIRRFAIDEDVSTS-----------YEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEEL 68
                        90
                ....*....|....*....
gi 4505571   84 TMAMSYVKDDIFRIYIKEK 102
Cdd:cd06402  69 VMALGSLNDDTFRIYIKEK 87
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
126-168 1.01e-21

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: 87.32  E-value: 1.01e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4505571  126 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAF 168
Cdd:cd02340   1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
UBA_SQSTM cd14320
UBA domain of sequestosome-1 (SQSTM) and similar proteins; SQSTM, also called EBI3-associated ...
393-432 1.15e-20

UBA domain of sequestosome-1 (SQSTM) and similar proteins; SQSTM, also called EBI3-associated protein of 60 kDa (EBIAP /p60), phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, or ubiquitin-binding protein p62, is a widely expressed multifunctional cytoplasmic protein that is able to noncovalently bind ubiquitin and several signaling proteins, suggesting a regulatory role connected to the ubiquitin-proteasome pathway. It functions as a scaffolding protein that regulates a diverse range of signaling pathways leading to activation of the nuclear factor kappa B (NF-kappaB) family of transcription factors. It also plays a novel role in connecting receptor signals with the endosomal signaling network required for mediating TrkA-induced differentiation. SQSTM contains a PB1 dimerization domain, a tumor necrosis factor receptor-associated factor 6 (TRAF6) binding site, and a C-terminal ubiquitin-associated (UBA) domain that mediates the recognition of polyubiquitin chains and ubiquitylated substrates.


Pssm-ID: 270505  Cd Length: 40  Bit Score: 84.55  E-value: 1.15e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4505571  393 RLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQ 432
Cdd:cd14320   1 KIEEALSQMLAMGFSNEGGWLTRLLEAKNGDIGKVLDVIQ 40
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
122-160 2.39e-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: 69.78  E-value: 2.39e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4505571     122 VHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLH 160
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSA 39
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
3-99 1.56e-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: 62.60  E-value: 1.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505571       3 SLTVKAYLLGkedaarEIRRFSFCCSPEpeaeaeaaagpgpCERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEE 82
Cdd:smart00666   1 TVDVKLRYGG------ETRRLSVPRDIS-------------FEDLRSKVAKRFG-LDNQSFTLKYQDEDGDLVSLTSDED 60
                           90       100
                   ....*....|....*....|
gi 4505571      83 LTMAMSYVK---DDIFRIYI 99
Cdd:smart00666  61 LEEAIEEYDslgSKKLRLHV 80
PB1 pfam00564
PB1 domain;
44-102 2.40e-10

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 56.53  E-value: 2.40e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505571     44 CERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVK---DDIFRIYIKEK 102
Cdd:pfam00564  24 FEELRALVEQRFG-LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARslgSKSLRLHVFPT 84
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
123-163 7.45e-09

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: 51.33  E-value: 7.45e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 4505571    123 HPNVICDGC-NGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGH 163
Cdd:pfam00569   2 HKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNH 43
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
394-431 1.00e-04

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 39.39  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 4505571     394 LIESLSQMLSMGFSDEggWLTRLLQTKNYDIGAALDTI 431
Cdd:smart00165   1 DEEKIDQLLEMGFSRE--EALKALRAANGNVERAAEYL 36
 
Name Accession Description Interval E-value
UBA_5 pfam16577
UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome ...
379-440 1.47e-41

UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome 1/p62 has recently been shown to interact with polyubiquitinated proteins through its UBA domain. This domain selectively binds K63-polyubiquitinated proteins.


Pssm-ID: 318725  Cd Length: 62  Bit Score: 141.34  E-value: 1.47e-41
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505571    379 EAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL 440
Cdd:pfam16577   1 EAALYPHLPPDADPRLIESLAQMLSMGFSDEGGWLTRLLHTKNFDIGAALDAIHFSKHPPPA 62
PB1_p62 cd06402
The PB1 domain is an essential part of p62 scaffold protein (alias sequestosome 1,SQSTM) ...
4-102 5.78e-40

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: 138.24  E-value: 5.78e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505571    4 LTVKAYLLGKeDAAREIRRFSFCCSPEPEaeaeaaagpgpCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd06402   1 LTVKAYLLGK-DANAEIRRFAIDEDVSTS-----------YEYLVEKVAAVFPSLRGKNFQLFWKDEEGDLVAFSSDEEL 68
                        90
                ....*....|....*....
gi 4505571   84 TMAMSYVKDDIFRIYIKEK 102
Cdd:cd06402  69 VMALGSLNDDTFRIYIKEK 87
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
126-168 1.01e-21

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: 87.32  E-value: 1.01e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4505571  126 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAF 168
Cdd:cd02340   1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKGVHPEHAMLKI 43
UBA_SQSTM cd14320
UBA domain of sequestosome-1 (SQSTM) and similar proteins; SQSTM, also called EBI3-associated ...
393-432 1.15e-20

UBA domain of sequestosome-1 (SQSTM) and similar proteins; SQSTM, also called EBI3-associated protein of 60 kDa (EBIAP /p60), phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, or ubiquitin-binding protein p62, is a widely expressed multifunctional cytoplasmic protein that is able to noncovalently bind ubiquitin and several signaling proteins, suggesting a regulatory role connected to the ubiquitin-proteasome pathway. It functions as a scaffolding protein that regulates a diverse range of signaling pathways leading to activation of the nuclear factor kappa B (NF-kappaB) family of transcription factors. It also plays a novel role in connecting receptor signals with the endosomal signaling network required for mediating TrkA-induced differentiation. SQSTM contains a PB1 dimerization domain, a tumor necrosis factor receptor-associated factor 6 (TRAF6) binding site, and a C-terminal ubiquitin-associated (UBA) domain that mediates the recognition of polyubiquitin chains and ubiquitylated substrates.


Pssm-ID: 270505  Cd Length: 40  Bit Score: 84.55  E-value: 1.15e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4505571  393 RLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQ 432
Cdd:cd14320   1 KIEEALSQMLAMGFSNEGGWLTRLLEAKNGDIGKVLDVIQ 40
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
122-160 2.39e-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: 69.78  E-value: 2.39e-15
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4505571     122 VHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLH 160
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSA 39
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
126-165 8.91e-13

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: 62.45  E-value: 8.91e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4505571  126 VICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGlHRGHTK 165
Cdd:cd02249   1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKG-KKGHPP 39
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
3-99 1.56e-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: 62.60  E-value: 1.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505571       3 SLTVKAYLLGkedaarEIRRFSFCCSPEpeaeaeaaagpgpCERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEE 82
Cdd:smart00666   1 TVDVKLRYGG------ETRRLSVPRDIS-------------FEDLRSKVAKRFG-LDNQSFTLKYQDEDGDLVSLTSDED 60
                           90       100
                   ....*....|....*....|
gi 4505571      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 1.20e-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: 60.37  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505571    4 LTVKAYLLGkedaarEIRRFSFCCSPEPeaeaeaaagpgpCERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEEL 83
Cdd:cd05992   1 VRVKVKYGG------EIRRFVVVSRSIS------------FEDLRSKIAEKFG-LDAVSFKLKYPDEDGDLVTISSDEDL 61
                        90       100
                ....*....|....*....|
gi 4505571   84 TMAMSYVK---DDIFRIYIK 100
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. ...
126-160 4.58e-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: 4.58e-11
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 4505571  126 VICDGCN-GPVVGTRYKCSVCPDYDLCSVCEGKGLH 160
Cdd:cd02339   1 IICDTCRkQGIIGIRWKCAECPNYDLCTTCYHGDKH 36
PB1 pfam00564
PB1 domain;
44-102 2.40e-10

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 56.53  E-value: 2.40e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505571     44 CERLLSRVAALFPaLRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVK---DDIFRIYIKEK 102
Cdd:pfam00564  24 FEELRALVEQRFG-LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARslgSKSLRLHVFPT 84
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
123-163 7.45e-09

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: 51.33  E-value: 7.45e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 4505571    123 HPNVICDGC-NGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGH 163
Cdd:pfam00569   2 HKVYTCNGCsNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNH 43
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
128-166 8.78e-06

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: 42.55  E-value: 8.78e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 4505571  128 CDGCNGpVVGTRYKCSVCPDYDLCSVC-EGKGLHRGHTKL 166
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 ...
126-154 1.15e-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: 42.33  E-value: 1.15e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 4505571  126 VICDGC-NGPVVGTRYKCSVCPDYDLCSVC 154
Cdd:cd02338   1 VSCDGCgKSNFTGRRYKCLICYDYDLCADC 30
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
128-159 2.37e-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: 41.65  E-value: 2.37e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 4505571  128 CDGCN-GPVVGTRYKCSVCP--DYDLCSVCEGKGL 159
Cdd:cd02341   3 CDSCGiEPIPGTRYHCSECDdgDFDLCQDCVVKGE 37
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
128-154 4.20e-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: 40.64  E-value: 4.20e-05
                        10        20
                ....*....|....*....|....*...
gi 4505571  128 CDGCN-GPVVGTRYKCSVCPDYDLCSVC 154
Cdd:cd02342   3 CDGCGvLPITGPRYKSKVKEDYDLCTIC 30
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
126-154 6.49e-05

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: 40.26  E-value: 6.49e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 4505571  126 VICDGCNG-PVVGTRYKCSVCPDYDLCSVC 154
Cdd:cd02344   1 VTCDGCQMfPINGPRFKCRNCDDFDFCENC 30
UBA smart00165
Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 ...
394-431 1.00e-04

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.


Pssm-ID: 197551 [Multi-domain]  Cd Length: 37  Bit Score: 39.39  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 4505571     394 LIESLSQMLSMGFSDEggWLTRLLQTKNYDIGAALDTI 431
Cdd:smart00165   1 DEEKIDQLLEMGFSRE--EALKALRAANGNVERAAEYL 36
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
128-154 3.42e-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: 38.04  E-value: 3.42e-04
                        10        20
                ....*....|....*....|....*...
gi 4505571  128 CDGCNGPVVGT-RYKCSVCPDYDLCSVC 154
Cdd:cd02335   3 CDYCSKDITGTiRIKCAECPDFDLCLEC 30
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
126-169 3.99e-04

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: 38.11  E-value: 3.99e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 4505571  126 VICDGCNG-PVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAFP 169
Cdd:cd02334   1 AKCNICKEfPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHP 45
PB1_Joka2 cd06398
The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with ...
47-89 7.98e-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: 38.54  E-value: 7.98e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 4505571   47 LLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSY 89
Cdd:cd06398  30 LREKVEELFSLSPDADLSLTYTDEDGDVVTLVDDNDLTDAIQY 72
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
128-158 3.14e-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: 35.64  E-value: 3.14e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 4505571  128 CDGCN-GPVVGTRYKCSVCPDYDLCSVCEGKG 158
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.
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