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 119581353 300 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 378
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119581353 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 119581353 146 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHdTNHVLLKL 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 119581353 300 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 378
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119581353 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 119581353 847 QTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELL 885
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 119581353   142 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHDTNHV 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 119581353 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 119581353 300 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 378
Cdd:cd14947    1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 119581353 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 119581353 847 QTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELL 885
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 119581353   142 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHDTNHV 186
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119581353 146 IACNNCQRR-IVGVRYQCSLCPS--YNICEDCEAGPYGHDTNHVLLK 189
Cdd:cd02341    1 FKCDSCGIEpIPGTRYHCSECDDgdFDLCQDCVVKGESHQEDHWLVK 47

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 119581353 146 IACNNCQRR-IVGVRYQCSLCPSYNICEDC-EAGPYG--HDTNH 185
Cdd:cd02338    1 VSCDGCGKSnFTGRRYKCLICYDYDLCADCyDSGVTTerHLFDH 44

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 119581353 148 CNNCQRRIVG-VRYQCSLCPSYNICEDC-----EAGPygHDTNH 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 119581353 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 119581353 148 CNNCqRRIVGVRYQCSLCPSYNICEDC 174
Cdd:cd02337    3 CNEC-KHHVETRWHCTVCEDYDLCITC 28