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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825909227 300 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSTDTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 378
Cdd:cd14947     1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1825909227 379 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 410
Cdd:cd14947    80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112

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 1825909227 146 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPySHdTNHVLLKL 190
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAKG-VH-PEHAMLKI 43

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825909227 300 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSTDTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 378
Cdd:cd14947     1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1825909227 379 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 410
Cdd:cd14947    80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112

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 1825909227 843 QTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELL 881
Cdd:cd14319     1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39

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 1825909227  142 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPySHDTNHV 186
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1825909227 210 RLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRK 259
Cdd:COG4942   164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825909227 300 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSTDTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 378
Cdd:cd14947     1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1825909227 379 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 410
Cdd:cd14947    80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112

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 1825909227 843 QTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELL 881
Cdd:cd14319     1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39

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 1825909227  142 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPySHDTNHV 186
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 1825909227 146 IACNNCQRRIVGVRYQCSLCPSYNICEDC-EAGPYSHDTNH 185
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 1825909227 146 IACNNCQRR-IVGVRYQCSLCPSYNICEDCEAGPySHDTNH 185
Cdd:cd02339     1 IICDTCRKQgIIGIRWKCAECPNYDLCTTCYHGD-KHDLEH 40

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 1825909227 148 CNNCQRRIVG-VRYQCSLCPSYNICEDC-----EAGPysHDTNH 185
Cdd:cd02335     3 CDYCSKDITGtIRIKCAECPDFDLCLECfsagaEIGK--HRNDH 44

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.

                          10        20        30
                  ....*....|....*....|....*....|
gi 1825909227 146 IACNNCQR-RIVGVRYQCSLCPSYNICEDC 174
Cdd:cd02344     1 VTCDGCQMfPINGPRFKCRNCDDFDFCENC 30

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.

                          10        20
                  ....*....|....*....|....*..
gi 1825909227 148 CNNCqRRIVGVRYQCSLCPSYNICEDC 174
Cdd:cd02337     3 CNEC-KHHVETRWHCTVCEDYDLCITC 28