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 14110381 369 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 447
Cdd:cd14947   1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 14110381 448 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 479
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 14110381 916 QTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELL 954
Cdd:cd14319   1 EWDSELEQLFEMGFTDRDLNQELLKKHNGDLDRVVDELL 39

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 14110381 279 RLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRK 328
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 14110381 369 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 447
Cdd:cd14947   1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 14110381 448 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 479
Cdd:cd14947  80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14110381   379 NLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTekkDVLVPCLKAGHVGVVSVEFIAPALEGTYTSH 458
Cdd:pfam16158   1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFVGGDNMGNVS---TVLVPPVAPGEEVDVSVELKAPSRPGRYISY 77

                          90       100
                  ....*....|....*....|.
gi 14110381   459 WRLSHK-GQQFGPRVWCSIIV 478
Cdd:pfam16158  78 WRLKTPdGTPFGDRLWVDITV 98

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 14110381 215 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHdTNHVLLKL 259
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 14110381    211 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHDTNHV 255
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 14110381   217 CNNCQ-RRIVGVRYQCSLCPSYNICEDCEAGPYGHD 251
Cdd:pfam00569   7 CNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKGGN 42

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 14110381 369 PMLSAAFV-DENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTeKKDVLVPCLKAGHVGVVSVEFI 447
Cdd:cd14947   1 PGLSAAFVeDVTIPDGTVVPPGTEFTKTWRLRNTGTVPWPAGTLLRFVGGDPGLLSA-PERVPVPSTVPGEEVDVSVELR 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 14110381 448 APALEGTYTSHWRLSHK-GQQFGPRVWCSIIVD 479
Cdd:cd14947  80 APSEPGRYISYWRLVTPdGLPFGDRLWVDITVE 112

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14110381   379 NLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTekkDVLVPCLKAGHVGVVSVEFIAPALEGTYTSH 458
Cdd:pfam16158   1 TIPDGTVVPPGTEFTKTWRLRNSGNVAWPAGTSLRFVGGDNMGNVS---TVLVPPVAPGEEVDVSVELKAPSRPGRYISY 77

                          90       100
                  ....*....|....*....|.
gi 14110381   459 WRLSHK-GQQFGPRVWCSIIV 478
Cdd:pfam16158  78 WRLKTPdGTPFGDRLWVDITV 98

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 14110381 215 IACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHdTNHVLLKL 259
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 14110381    211 FSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPyGHDTNHV 255
Cdd:smart00291   1 VHHSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKG-SAGGEHS 44

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14110381   5 VTLNVTFKNEIQSFLVSDPeNTTWADIEAMVKVSFDLN--TIQIKYLDEENEEVSINSQGEYEEALKMAVKQGN-QLQMQ 81
Cdd:cd05992   1 VRVKVKYGGEIRRFVVVSR-SISFEDLRSKIAEKFGLDavSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSkKLRLF 79

                ..
gi 14110381  82 VH 83
Cdd:cd05992  80 VF 81

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 14110381 215 IACNNCQRR-IVGVRYQCSLCPS--YNICEDCEAGPYGHDTNHVLLK 258
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 14110381 215 IACNNCQRR-IVGVRYQCSLCPSYNICEDC-EAGPYG--HDTNH 254
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 14110381 217 CNNCQRRIVG-VRYQCSLCPSYNICEDC-----EAGPygHDTNH 254
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 14110381 215 IACNNCQR-RIVGVRYQCSLCPSYNICEDC 243
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 14110381 217 CNNCqRRIVGVRYQCSLCPSYNICEDC 243
Cdd:cd02337   3 CNEC-KHHVETRWHCTVCEDYDLCITC 28