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        40
                  ....*....|....*....|....*....|....*....|....*
gi 20141691   121 IHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLM 165
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45

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 20141691     6 LKITYQGAgpqKKINAYLRMPSqNYTILRREIELYLfqerQLPKCDVRTFWIDADKDEIEIVNQNDYEIFLAKCES---- 81
Cdd:pfam00564   4 LKLRYGGG---IRRFLSVSRGI-SFEELRALVEQRF----GLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSlgsk 75

                  ....*....
gi 20141691    82 --NMHVQVA 88
Cdd:pfam00564  76 slRLHVFPT 84

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        40
                  ....*....|....*....|....*....|....*....|....*
gi 20141691   121 IHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLM 165
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45

UBA domain of sequestosome-1 (SQSTM) and similar proteins; SQSTM, also called EBI3-associated protein of 60 kDa (EBIAP /p60), phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, or ubiquitin-binding protein p62, is a widely expressed multifunctional cytoplasmic protein that is able to noncovalently bind ubiquitin and several signaling proteins, suggesting a regulatory role connected to the ubiquitin-proteasome pathway. It functions as a scaffolding protein that regulates a diverse range of signaling pathways leading to activation of the nuclear factor kappa B (NF-kappaB) family of transcription factors. It also plays a novel role in connecting receptor signals with the endosomal signaling network required for mediating TrkA-induced differentiation. SQSTM contains a PB1 dimerization domain, a tumor necrosis factor receptor-associated factor 6 (TRAF6) binding site, and a C-terminal ubiquitin-associated (UBA) domain that mediates the recognition of polyubiquitin chains and ubiquitylated substrates.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 20141691 555 INKSIHAMMAMGFSNEGAWLTQLLESVQGNISAALDVMN 593
Cdd:cd14320   2 IEEALSQMLAMGFSNEGGWLTRLLEAKNGDIGKVLDVIQ 40

UBA domain; UBA_2 is a domain found on eukaryotic ubiquitin-interacting proteins. Sequestosome 1/p62 has recently been shown to interact with polyubiquitinated proteins through its UBA domain. This domain selectively binds K63-polyubiquitinated proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 20141691   552 DESINKSIHAMMAMGFSNEGAWLTQLLESVQGNISAALDVMNVSQN 597
Cdd:pfam16577  13 DPRLIESLAQMLSMGFSDEGGWLTRLLHTKNFDIGAALDAIHFSKH 58

Ubiquitin associated domain; Present in Rad23, SNF1-like kinases. The newly-found UBA in p62 is known to bind ubiquitin.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 20141691    556 NKSIHAMMAMGFSNEgaWLTQLLESVQGNISAALDVM 592
Cdd:smart00165   2 EEKIDQLLEMGFSRE--EALKALRAANGNVERAAEYL 36

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        40
                  ....*....|....*....|....*....|....*....|....*
gi 20141691   121 IHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLM 165
Cdd:pfam00569   1 IHKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKGGNHQM 45

UBA domain of sequestosome-1 (SQSTM) and similar proteins; SQSTM, also called EBI3-associated protein of 60 kDa (EBIAP /p60), phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, or ubiquitin-binding protein p62, is a widely expressed multifunctional cytoplasmic protein that is able to noncovalently bind ubiquitin and several signaling proteins, suggesting a regulatory role connected to the ubiquitin-proteasome pathway. It functions as a scaffolding protein that regulates a diverse range of signaling pathways leading to activation of the nuclear factor kappa B (NF-kappaB) family of transcription factors. It also plays a novel role in connecting receptor signals with the endosomal signaling network required for mediating TrkA-induced differentiation. SQSTM contains a PB1 dimerization domain, a tumor necrosis factor receptor-associated factor 6 (TRAF6) binding site, and a C-terminal ubiquitin-associated (UBA) domain that mediates the recognition of polyubiquitin chains and ubiquitylated substrates.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 20141691 555 INKSIHAMMAMGFSNEGAWLTQLLESVQGNISAALDVMN 593
Cdd:cd14320   2 IEEALSQMLAMGFSNEGGWLTRLLEAKNGDIGKVLDVIQ 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 20141691 125 VECDGCGLAPLIGFRYKCVQCSNYDLCQKC-ELAHKHPEHLM 165
Cdd:cd02338   1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCyDSGVTTERHLF 42

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 20141691 127 CDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKH-PEHLMLR 167
Cdd:cd02339   3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHdLEHRFYR 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        40
                ....*....|....*....|....*....|....*....|
gi 20141691 125 VECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKH-PEH 163
Cdd:cd02344   1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHnTRH 40

PB1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141691     6 LKITYQGAgpqKKINAYLRMPSqNYTILRREIELYLfqerQLPKCDVRTFWIDADKDEIEIVNQNDYEIFLAKCES---- 81
Cdd:pfam00564   4 LKLRYGGG---IRRFLSVSRGI-SFEELRALVEQRF----GLDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSlgsk 75

                  ....*....
gi 20141691    82 --NMHVQVA 88
Cdd:pfam00564  76 slRLHVFPT 84

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 20141691 125 VECDGCG-LAPLigFRYKCVQCSNYDLCQKCELAHKHPE-----HLMLRM 168
Cdd:cd02343   1 ISCDGCDeIAPW--HRYRCLQCTDMDLCKTCFLGGVKPEgheddHEMVNM 48

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 20141691 127 CDGCGLAPLIGFRYKCVQCSNYDLCQKC-----ELAHKHPEH 163
Cdd:cd02335   3 CDYCSKDITGTIRIKCAECPDFDLCLECfsagaEIGKHRNDH 44