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 2031717847  13 LIIKAQLGDDIRRIPIHNEDITYDELVLMMQRVFRGKLQSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 92
Cdd:cd06401     1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80

                  .
gi 2031717847  93 N 93
Cdd:cd06401    81 N 81

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031717847 223 PGAQQHQQSYTAVQPQAGQMEgQMYQQYQQPGYAPQQQQPQAQPQYGLQYSGYSQQPSSQQQAQFQAYNQQASQAPAPGF 302
Cdd:pfam09770 208 KKPAQQPAPAPAQPPAAPPAQ-QAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQ 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2031717847 303 sAQAQQLPSQPAQPYQggsyAPQNYTTQPSQPANYTMPPASQPGIGPNQPGayQPRPGFTPSPGSNVTPPPS 374
Cdd:pfam09770 287 -QFHQQPPPVPVQPTQ----ILQNPNRLSAARVGYPQNPQPGVQPAPAHQA--HRQQGSFGRQAPIITHPQQ 351

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 2031717847  13 LIIKAQLGDDIRRIPIHNEDITYDELVLMMQRVFRGKLQSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 92
Cdd:cd06401     1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80

                  .
gi 2031717847  93 N 93
Cdd:cd06401    81 N 81

PB1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031717847  15 IKAQLGDDIRRIPIHNEDITYDELVLMMQRVFrgKLQSNDeVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 89
Cdd:pfam00564   4 LKLRYGGGIRRFLSVSRGISFEELRALVEQRF--GLDDVD-FKLKYPDEDGDLVSLTSDEDLEEALEearslGSKSLRLH 80

                  ...
gi 2031717847  90 LFV 92
Cdd:pfam00564  81 VFP 83

chromosomal replication initiator protein DnaA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031717847 295 SQAPAPGFSAQAQQLPSQPAQPY------------QGGSYAPQNYTTQPSQPANYtmpPASQPGIGPNQPGAY---QPRP 359
Cdd:PRK14086   96 APPPPHARRTSEPELPRPGRRPYegyggpraddrpPGLPRQDQLPTARPAYPAYQ---QRPEPGAWPRAADDYgwqQQRL 172

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2031717847 360 GFTPSpgSNVTPPPSGSNPYARNRPPFAQGYTQPGPGYR 398
Cdd:PRK14086  173 GFPPR--APYASPASYAPEQERDREPYDAGRPEYDQRRR 209

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 2031717847  13 LIIKAQLGDDIRRIPIHNEDITYDELVLMMQRVFRGKLQSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 92
Cdd:cd06401     1 LILKAQLGDDIRRIPIHNEDITYDELLLMMQRVFRGKLGSSDDVLIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFV 80

                  .
gi 2031717847  93 N 93
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 2031717847   15 IKAQLGDDIRRIPIHnEDITYDELVLMMQRVFRgklQSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ-----CSRILKLT 89
Cdd:smart00666   4 VKLRYGGETRRLSVP-RDISFEDLRSKVAKRFG---LDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEeydslGSKKLRLH 79

                   ..
gi 2031717847   90 LF 91
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 2031717847  13 LIIKAQLGDDIRRI--PIHNE--DITYDELVLMMQRVFrgKLQSNDEVTIKYKDEDGDLITIFDSSDLSFAIQ--CSRIL 86
Cdd:cd06398     1 LVVKVKYGGTLRRFtfPVAENqlDLNMDGLREKVEELF--SLSPDADLSLTYTDEDGDVVTLVDDNDLTDAIQyfCSGSR 78

                  ....*..
gi 2031717847  87 KLTLFVN 93
Cdd:cd06398    79 LNPLRID 85

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 2031717847  12 KLIIKAQLGDDIRRIPIhNEDITYDELvlmMQRVfRGKLQSNDEVTIKYKDeDGDLITIFDSSDLSFAIQCSR 84
Cdd:cd06408     2 KIRVKVHAQDDTRYIMI-GPDTGFADF---EDKI-RDKFGFKRRLKIKMKD-DGDMITMGDQDDLDMAIDTAR 68

chromosomal replication initiator protein DnaA;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031717847 295 SQAPAPGFSAQAQQLPSQPAQPY------------QGGSYAPQNYTTQPSQPANYtmpPASQPGIGPNQPGAY---QPRP 359
Cdd:PRK14086   96 APPPPHARRTSEPELPRPGRRPYegyggpraddrpPGLPRQDQLPTARPAYPAYQ---QRPEPGAWPRAADDYgwqQQRL 172

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2031717847 360 GFTPSpgSNVTPPPSGSNPYARNRPPFAQGYTQPGPGYR 398
Cdd:PRK14086  173 GFPPR--APYASPASYAPEQERDREPYDAGRPEYDQRRR 209

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031717847  15 IKAQLGDDIRRIPIH-NEDITYDElvlmmqrvFRGKLQS-----NDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILkL 88
Cdd:cd06403     3 VKSKFDAEFRRFSLDrNKPGKFED--------FYKLLEHlhhipNVDFLIGYTDPHGDLLPINNDDNFLKALSSANPL-L 73

                  ....
gi 2031717847  89 TLFV 92
Cdd:cd06403    74 RIFI 77

The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. 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 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031717847  36 DELV-LMMQRVFRGKLQSNDeVTIKYKDEDGDLITIFDSSDLSFAIQCSRIL---KLTLFV 92
Cdd:cd06409    24 EELRtLISQRLGDDDFETHL-YALSYVDDEGDIVLITSDSDLVAAVLVARSAglkKLDLHL 83