NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564374238|ref|XP_006247384|]
View 

next to BRCA1 gene 1 protein isoform X1 [Rattus norvegicus]

Protein Classification

next to BRCA1 gene 1 protein( domain architecture ID 10157312)

next to BRCA1 gene 1 protein (NBR1) acts probably as a receptor for selective autophagosomal degradation of ubiquitinated targets

Gene Symbol:  NBR1
Gene Ontology:  GO:0016236|GO:0043130|GO:0051019|GO:0008270
PubMed:  19250911

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 371-481 1.75e-44

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


:

Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 155.91  E-value: 1.75e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238 371 PTLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHIGVVSVEFI 449
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564374238 450 APTLEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 481
Cdd:cd14947   80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112
PB1_NBR1 cd06396
The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein ...
 5-86 6.14e-41

The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. 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. The NBR1 protein contains a type I PB1 domain.


:

Pssm-ID: 99718  Cd Length: 81  Bit Score: 144.99  E-value: 6.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238   5 VTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMAnIKQGNQLQMQVH 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSA-VRQGNLLQMNVY 79


                 ..
gi 564374238  85 EG 86
Cdd:cd06396   80 EH 81
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 217-261 1.78e-16

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: 73.83  E-value: 1.78e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564374238 217 IACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPySHdTNHILLKF 261
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43
UBA_NBR1 cd14319
UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins; NBR1, also called cell ...
 933-971 4.93e-16

UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins; NBR1, also called cell migration-inducing gene 19 protein, membrane component chromosome 17 surface marker 2, neighbor of BRCA1 gene 1 protein, or protein 1A1-3B, is a scaffold protein that may be involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Moreover, NBR1 functions as an autophagic receptor for ubiquitinated cargo. It interacts with ATG8-family proteins for its degradation by autophagy. NBR1 contains an N-terminal Phox and Bem1p (PB1) domain that plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. NBR1 also has a LC3-interaction region (LIR) and a ubiquitin-associated (UBA) domain. The LIR is required for the autophagic clearance of NBR1. UBA domain is responsible for the ubiquitin binding which is necessary for the puromycin-induced formation of ubiquitinated protein aggregates.


:

Pssm-ID: 270504  Cd Length: 39  Bit Score: 72.46  E-value: 4.93e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 564374238 933 QTAALMAHLFEMGFCDRQLNLRLLRKHNHNILQVVTELL 971
Cdd:cd14319    1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39
 
Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 371-481 1.75e-44

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 155.91  E-value: 1.75e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238 371 PTLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHIGVVSVEFI 449
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564374238 450 APTLEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 481
Cdd:cd14947   80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112
N_BRCA1_IG pfam16158
Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human ...
 381-480 1.25e-41

Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries


Pssm-ID: 465035  Cd Length: 98  Bit Score: 147.34  E-value: 1.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238  381 NLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTekkDVLVPCLKAGHIGVVSVEFIAPTLEGTYTSH 460
Cdd:pfam16158   1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFVGGDNMGNVS---TVLVPPVAPGEEVDVSVELKAPSRPGRYISY 77

                          90       100
                  ....*....|....*....|.
gi 564374238  461 WRLSHK-GQQFGPRVWCSIIV 480
Cdd:pfam16158  78 WRLKTPdGTPFGDRLWVDITV 98
PB1_NBR1 cd06396
The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein ...
 5-86 6.14e-41

The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. 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. The NBR1 protein contains a type I PB1 domain.


Pssm-ID: 99718  Cd Length: 81  Bit Score: 144.99  E-value: 6.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238   5 VTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMAnIKQGNQLQMQVH 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSA-VRQGNLLQMNVY 79


                 ..
gi 564374238  85 EG 86
Cdd:cd06396   80 EH 81
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 4-84 1.08e-16

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: 75.70  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238     4 QVTLNVTFKNETQSFLVsdPENTTWADVEAMVKVSFDL--NTIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQM 81
Cdd:smart00666   1 TVDVKLRYGGETRRLSV--PRDISFEDLRSKVAKRFGLdnQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRL 78


                   ...
gi 564374238    82 QVH 84
Cdd:smart00666  79 HVF 81
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 217-261 1.78e-16

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: 73.83  E-value: 1.78e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564374238 217 IACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPySHdTNHILLKF 261
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43
UBA_NBR1 cd14319
UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins; NBR1, also called cell ...
 933-971 4.93e-16

UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins; NBR1, also called cell migration-inducing gene 19 protein, membrane component chromosome 17 surface marker 2, neighbor of BRCA1 gene 1 protein, or protein 1A1-3B, is a scaffold protein that may be involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Moreover, NBR1 functions as an autophagic receptor for ubiquitinated cargo. It interacts with ATG8-family proteins for its degradation by autophagy. NBR1 contains an N-terminal Phox and Bem1p (PB1) domain that plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. NBR1 also has a LC3-interaction region (LIR) and a ubiquitin-associated (UBA) domain. The LIR is required for the autophagic clearance of NBR1. UBA domain is responsible for the ubiquitin binding which is necessary for the puromycin-induced formation of ubiquitinated protein aggregates.


Pssm-ID: 270504  Cd Length: 39  Bit Score: 72.46  E-value: 4.93e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 564374238 933 QTAALMAHLFEMGFCDRQLNLRLLRKHNHNILQVVTELL 971
Cdd:cd14319    1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 213-256 2.26e-14

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: 67.85  E-value: 2.26e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 564374238   213 FSWHIACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPySHDTNH 256
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEH 43
PB1 pfam00564
PB1 domain;
4-86 9.43e-14

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 67.32  E-value: 9.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238    4 QVTLNVTFKNETQSFLVSDPeNTTWADVEAMVKVSF--DLNTIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQM 81
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSR-GISFEELRALVEQRFglDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRL 79


                  ....*
gi 564374238   82 QVHEG 86
Cdd:pfam00564  80 HVFPT 84
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 211-253 1.49e-04

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: 40.16  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564374238  211 NQFSWHIaCSHCQkrIVGVRYQCSLCPSYNICEDCEAGPYSHD 253
Cdd:pfam00569   3 KVYTCNG-CSNDP--SIGVRYHCLRCSDYDLCQSCFQTHKGGN 42
 
Name Accession Description Interval E-value
NBR1_like cd14947
Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has ...
 371-481 1.75e-44

Functionally uncharacterized domain in neighbor of Brca1 Gene 1 and related proteins; NBR1 has been characterized as a specific late endosomal protein, which might play a role in receptor (RTK) trafficking. Specifically, NBR1 was shown to inhibit ligand-mediated receptor internalization from the cell surface. The region covered by this domain model may be involved in that function, as the C-terminus (which contains a UBA domain) was shown to be essential but not sufficient by itself. In an earlier yeast two-hybrid study, the region in mouse NBR1 covered by this domain has been shown to interact with CIB (calcium and integrin-binding protein) and FEZ1 (fasciculation and elongation protein zeta-1). Thus, NBR1 may play a role in cellular signalling pathways and possibly in neural development.


Pssm-ID: 271343 [Multi-domain]  Cd Length: 112  Bit Score: 155.91  E-value: 1.75e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238 371 PTLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHIGVVSVEFI 449
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564374238 450 APTLEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 481
Cdd:cd14947   80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112
N_BRCA1_IG pfam16158
Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human ...
 381-480 1.25e-41

Ig-like domain from next to BRCA1 gene; Domain present between positions 365-485 in the human next to BRCA1 gene 1 protein Q14596 (NBR1_HUMAN) Distant homology and fold prediction analysis suggests this domain has an immunoglobulin like fold and is distantly homologous to domains involved in cell adhesion such as CARDB (PF07705). JCSG construct was crystalized confirming the domain boundaries


Pssm-ID: 465035  Cd Length: 98  Bit Score: 147.34  E-value: 1.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238  381 NLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTekkDVLVPCLKAGHIGVVSVEFIAPTLEGTYTSH 460
Cdd:pfam16158   1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFVGGDNMGNVS---TVLVPPVAPGEEVDVSVELKAPSRPGRYISY 77

                          90       100
                  ....*....|....*....|.
gi 564374238  461 WRLSHK-GQQFGPRVWCSIIV 480
Cdd:pfam16158  78 WRLKTPdGTPFGDRLWVDITV 98
PB1_NBR1 cd06396
The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein ...
 5-86 6.14e-41

The PB1 domain is an essential part of NBR1 protein, next to BRCA1, a scaffold protein mediating specific protein-protein interaction with both titin protein kinase and with another scaffold protein p62. 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. The NBR1 protein contains a type I PB1 domain.


Pssm-ID: 99718  Cd Length: 81  Bit Score: 144.99  E-value: 6.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238   5 VTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMAnIKQGNQLQMQVH 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSA-VRQGNLLQMNVY 79


                 ..
gi 564374238  85 EG 86
Cdd:cd06396   80 EH 81
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 4-84 1.08e-16

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: 75.70  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238     4 QVTLNVTFKNETQSFLVsdPENTTWADVEAMVKVSFDL--NTIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQM 81
Cdd:smart00666   1 TVDVKLRYGGETRRLSV--PRDISFEDLRSKVAKRFGLdnQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKLRL 78


                   ...
gi 564374238    82 QVH 84
Cdd:smart00666  79 HVF 81
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 217-261 1.78e-16

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: 73.83  E-value: 1.78e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564374238 217 IACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPySHdTNHILLKF 261
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43
UBA_NBR1 cd14319
UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins; NBR1, also called cell ...
 933-971 4.93e-16

UBA domain of next to BRCA1 gene 1 protein (NBR1) and similar proteins; NBR1, also called cell migration-inducing gene 19 protein, membrane component chromosome 17 surface marker 2, neighbor of BRCA1 gene 1 protein, or protein 1A1-3B, is a scaffold protein that may be involved in signal transmission downstream of the serine/protein kinase from the giant muscle protein titin. Moreover, NBR1 functions as an autophagic receptor for ubiquitinated cargo. It interacts with ATG8-family proteins for its degradation by autophagy. NBR1 contains an N-terminal Phox and Bem1p (PB1) domain that plays a critical role in mediating protein-protein interactions with both titin kinase and with another scaffold protein, p62. NBR1 also has a LC3-interaction region (LIR) and a ubiquitin-associated (UBA) domain. The LIR is required for the autophagic clearance of NBR1. UBA domain is responsible for the ubiquitin binding which is necessary for the puromycin-induced formation of ubiquitinated protein aggregates.


Pssm-ID: 270504  Cd Length: 39  Bit Score: 72.46  E-value: 4.93e-16
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 564374238 933 QTAALMAHLFEMGFCDRQLNLRLLRKHNHNILQVVTELL 971
Cdd:cd14319    1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 213-256 2.26e-14

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: 67.85  E-value: 2.26e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 564374238   213 FSWHIACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPySHDTNH 256
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEH 43
PB1 pfam00564
PB1 domain;
4-86 9.43e-14

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 67.32  E-value: 9.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238    4 QVTLNVTFKNETQSFLVSDPeNTTWADVEAMVKVSF--DLNTIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQM 81
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSR-GISFEELRALVEQRFglDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSLRL 79


                  ....*
gi 564374238   82 QVHEG 86
Cdd:pfam00564  80 HVFPT 84
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 5-84 3.82e-13

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: 65.76  E-value: 3.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374238   5 VTLNVTFKNETQSFLVSDPeNTTWADVEAMVKVSFDLN--TIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQMQ 82
Cdd:cd05992    1 VRVKVKYGGEIRRFVVVSR-SISFEDLRSKIAEKFGLDavSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKLRLF 79


                 ..
gi 564374238  83 VH 84
Cdd:cd05992   80 VF 81
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 217-260 3.43e-07

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: 47.43  E-value: 3.43e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 564374238 217 IACSHCQKRIVGVRYQCSLCPSYNICEDC-EAGPYSHDTNHILLK 260
Cdd:cd02249    1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCyAKGKKGHPPDHSFTE 45
ZZ_ZZZ3 cd02341
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ...
 217-260 2.01e-06

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: 45.50  E-value: 2.01e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564374238 217 IACSHCQKR-IVGVRYQCSLCPS--YNICEDCEAGPYSHDTNHILLK 260
Cdd:cd02341    1 FKCDSCGIEpIPGTRYHCSECDDgdFDLCQDCVVKGESHQEDHWLVK 47
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 217-263 8.00e-06

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: 43.60  E-value: 8.00e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 564374238 217 IACSHCQKR-IVGVRYQCSLCPSYNICEDCeagpYSHDTNHILLKFRR 263
Cdd:cd02339    1 IICDTCRKQgIIGIRWKCAECPNYDLCTTC----YHGDKHDLEHRFYR 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 211-253 1.49e-04

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: 40.16  E-value: 1.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 564374238  211 NQFSWHIaCSHCQkrIVGVRYQCSLCPSYNICEDCEAGPYSHD 253
Cdd:pfam00569   3 KVYTCNG-CSNDP--SIGVRYHCLRCSDYDLCQSCFQTHKGGN 42
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
 217-258 2.28e-04

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: 39.88  E-value: 2.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 564374238 217 IACSHCQKR-IVGVRYQCSLCPSYNICEDCEAGPYS---HDTNHIL 258
Cdd:cd02345    1 LSCSACRKQdISGIRFPCQVCRDYSLCLGCYTKGREtkrHNSLHIM 46
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 217-256 4.63e-04

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: 38.87  E-value: 4.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 564374238 217 IACSHCQKR-IVGVRYQCSLCPSYNICEDC-EAGPYS--HDTNH 256
Cdd:cd02338    1 VSCDGCGKSnFTGRRYKCLICYDYDLCADCyDSGVTTerHLFDH 44
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 219-245 1.44e-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: 37.34  E-value: 1.44e-03
                         10        20
                 ....*....|....*....|....*...
gi 564374238 219 CSHCQKR-IVGVRYQCSLCPSYNICEDC 245
Cdd:cd02334    3 CNICKEFpITGFRYRCLKCFNYDLCQSC 30
PB1_aPKC cd06404
PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in ...
 29-83 1.59e-03

PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in complex with Par6 and Par3 proteins is crucial for establishment of apical-basal polarity of animal cells. 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. The aPKC protein contains a type I/II PB1 domain.


Pssm-ID: 99725  Cd Length: 83  Bit Score: 38.48  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564374238  29 ADVEAMVKVSFDlNTIQIKYLDEENEEISINSQGEYEEALKMANIKQGNQLQMQV 83
Cdd:cd06404   27 NEVRDMCRFHND-QPFTLKWIDEEGDPCTISSQMELEEAFRLYELNKDSELNIHV 80
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
 219-256 4.96e-03

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: 36.12  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 564374238 219 CSHCQKRIVG-VRYQCSLCPSYNICEDC-----EAGPysHDTNH 256
Cdd:cd02335    3 CDYCSKDITGtIRIKCAECPDFDLCLECfsagaEIGK--HRNDH 44
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 219-245 9.19e-03

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: 34.85  E-value: 9.19e-03
                         10        20
                 ....*....|....*....|....*..
gi 564374238 219 CSHCqKRIVGVRYQCSLCPSYNICEDC 245
Cdd:cd02337    3 CNEC-KHHVETRWHCTVCEDYDLCITC 28
 
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