The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve growth factor tyrosine kinase receptor TrkA and to the tyrosine kinase ALK. The PB1 domain is a modular domain mediating specific protein-protein interaction 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 domains, 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 PB1 domains of TFG represent a type I/II PB1 domain. The physiological function of TFG remains unknown.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564376571  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 90
Cdd:cd06401    1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80

                 .
gi 564376571  91 N 91
Cdd:cd06401   81 N 81

The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve growth factor tyrosine kinase receptor TrkA and to the tyrosine kinase ALK. The PB1 domain is a modular domain mediating specific protein-protein interaction 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 domains, 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 PB1 domains of TFG represent a type I/II PB1 domain. The physiological function of TFG remains unknown.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564376571  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 90
Cdd:cd06401    1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80

                 .
gi 564376571  91 N 91
Cdd:cd06401   81 N 81

PB1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564376571   13 IKAQLGEDIRRIPIHNEDITYDELVLMMQRVFrgKLLSNDeVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 87
Cdd:pfam00564   4 LKLRYGGGIRRFLSVSRGISFEELRALVEQRF--GLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEearslGSKSLRLH 80

                  ...
gi 564376571   88 LFV 90
Cdd:pfam00564  81 VFP 83

The PB1 domain found in TFG protein, an oncogenic gene product and fusion partner to nerve growth factor tyrosine kinase receptor TrkA and to the tyrosine kinase ALK. The PB1 domain is a modular domain mediating specific protein-protein interaction 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 domains, 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 PB1 domains of TFG represent a type I/II PB1 domain. The physiological function of TFG remains unknown.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564376571  11 LIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 90
Cdd:cd06401    1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80

                 .
gi 564376571  91 N 91
Cdd:cd06401   81 N 81

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564376571    13 IKAQLGEDIRRIPIHnEDITYDELVLMMQRVFRgklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 87
Cdd:smart00666   4 VKLRYGGETRRLSVP-RDISFEDLRSKVAKRFG---LDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEeydslGSKKLRLH 79

                   ..
gi 564376571    88 LF 89
Cdd:smart00666  80 VF 81

The PB1 domain is present in the Nicotiana plumbaginifolia Joka2 protein which interacts with sulfur stress inducible UP9 protein. 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 noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564376571  11 LIIKAQLGEDIRRI--PIHNE--DITYDELVLMMQRVFrgKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ--CSRIL 84
Cdd:cd06398    1 LVVKVKYGGTLRRFtfPVAENqlDLNMDGLREKVEELF--SLSPDADLSLTYTDEDGDVVTLVDDNDLTDAIQyfCSGSR 78

                 ....*..
gi 564376571  85 KLTLFVN 91
Cdd:cd06398   79 LNPLRID 85

The PB1 domain is an essential part of Par6 protein which in complex with Par3 and aPKC proteins is crucial for establishment of apical-basal polarity of animal cells. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, 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 noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The Par6 protein contains a type II PB1 domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564376571  13 IKAQLGEDIRRIPIH-NEDITYDELVLMMQRVFRgklLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILkLTLFV 90
Cdd:cd06403    3 VKSKFDAEFRRFSLDrNKPGKFEDFYKLLEHLHH---IPNVDFLIGYTDPHGDLLPINNDDNFLKALSSANPL-LRIFI 77

The PB1 domain is present in the Epichloe festucae NoxR protein (NADPH oxidase regulator), a key regulator of NADPH oxidase isoform, NoxA. NoxA is essential for growth control of the fungal endophyte in plant tissue in the process of symbiotic interaction between a fungi and its plant host. The Epichloe festucae p67(phox)-like regulator, NoxR, dispensable in culture but essential in plants for the symbiotic interaction. Plants infected with a noxR deletion mutant show severe stunting and premature senescence, whereas hyphae in the meristematic tissues show increased branching leading to increased fungal colonization of pseudostem and leaf blade tissue. The PB1 domain is a modular domain mediating specific protein-protein interactions which a play 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 domains, 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 noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564376571  10 KLIIKAQLGEDIRRIPIhNEDITYDELvlmMQRVfRGKLLSNDEVTIKYKDeDGDLITIFDSSDLSFAIQCSR 82
Cdd:cd06408    2 KIRVKVHAQDDTRYIMI-GPDTGFADF---EDKI-RDKFGFKRRLKIKMKD-DGDMITMGDQDDLDMAIDTAR 68

DNA polymerase III subunit gamma/tau;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564376571 300 ASTYPPQTYT-TQTSQPANYTVPPGSQPGMAPSQPGAYQPRPgfTPSPASTMAPPSTGANPYARNRP 365
Cdd:PRK14971 387 AAAPQPSAAAaASPSPSQSSAAAQPSAPQSATQPAGTPPTVS--VDPPAAVPVNPPSTAPQAVRPAQ 451

PB1 domain is an essential modular domain of the atypical protein kinase C (aPKC) which in complex with Par6 and Par3 proteins is crucial for establishment of apical-basal polarity of animal cells. PB1 domain is a modular domain mediating specific protein-protein interaction which play roles in many critical cell processes. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, 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 noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants. The aPKC protein contains a type I/II PB1 domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564376571  13 IKAQLGEDIRRIPIhNEDITYDELVLMMQRVFRgklLSNDEV-TIKYKDEDGDLITIFDSSDLSFAIQC 80
Cdd:cd06404    3 VKAAYNGDIMITSI-DPSISLEELCNEVRDMCR---FHNDQPfTLKWIDEEGDPCTISSQMELEEAFRL 67