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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582316   5 VTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMAnIKQGNQLQMQVH 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSA-VRQGNLLQMNVY 79

                 ..
gi 356582316  85 EG 86
Cdd:cd06396   80 EH 81

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 356582316 216 IACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPyTHdTNHVLLKL 260
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582316   5 VTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMAnIKQGNQLQMQVH 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSA-VRQGNLLQMNVY 79

                 ..
gi 356582316  85 EG 86
Cdd:cd06396   80 EH 81

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 356582316 938 QTTALMAHLFEMGFCDRQLNLRLLRKHNYNILQVVTELL 976
Cdd:cd14319    1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 356582316 216 IACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPyTHdTNHVLLKL 260
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 356582316   212 FSWHIACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPyTHDTNHV 256
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582316   5 VTLNVTFKNETQSFLVSDPENTTWADVEAMVKVSFDLNTIQIKYLDEENEEISINSQGEYEEALKMAnIKQGNQLQMQVH 84
Cdd:cd06396    1 VNLKVTYNGESQSFLVSDSENTTWASVEAMVKVSFGLNDIQIKYVDEENEEVSVNSQGEYEEALKSA-VRQGNLLQMNVY 79

                 ..
gi 356582316  85 EG 86
Cdd:cd06396   80 EH 81

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 356582316 938 QTTALMAHLFEMGFCDRQLNLRLLRKHNYNILQVVTELL 976
Cdd:cd14319    1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 356582316 216 IACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPyTHdTNHVLLKL 260
Cdd:cd02340    1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 356582316   212 FSWHIACSHCQKRIVGVRYQCSLCPSYNICEDCEAGPyTHDTNHV 256
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 356582316 216 IACSHCQKRIVGVRYQCSLCPSYNICEDC-EAGPYTHDTNH 255
Cdd:cd02249    1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCyAKGKKGHPPDH 41

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 356582316 216 IACSHCQKR-IVGVRYQCSLCPSYNICEDCEAGPyTHDTNH 255
Cdd:cd02339    1 IICDTCRKQgIIGIRWKCAECPNYDLCTTCYHGD-KHDLEH 40

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 356582316 216 IACSHCQKR-IVGVRYQCSLCPSYNICEDC-EAGPYT--HDTNH 255
Cdd:cd02338    1 VSCDGCGKSnFTGRRYKCLICYDYDLCADCyDSGVTTerHLFDH 44

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.

                         10        20
                 ....*....|....*....|....*...
gi 356582316 218 CSHCQKR-IVGVRYQCSLCPSYNICEDC 244
Cdd:cd02334    3 CNICKEFpITGFRYRCLKCFNYDLCQSC 30

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 356582316 218 CSHCQKRIVG-VRYQCSLCPSYNICEDC-----EAGPytHDTNH 255
Cdd:cd02335    3 CDYCSKDITGtIRIKCAECPDFDLCLECfsagaEIGK--HRNDH 44