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Conserved domains on  [gi|568911572|ref|XP_006535661|]
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BRO1 domain-containing protein BROX isoform X1 [Mus musculus]

Protein Classification

BRO1 domain-containing protein( domain architecture ID 10174120)

BRO1 domain-containing protein may adopt a boomerang structure with a concave face that contains a triple tetratricopeptide repeat, and may be involved in protein complex formation and protein-sorting

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 4-356 0e+00

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


:

Pssm-ID: 185766  Cd Length: 353  Bit Score: 682.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   4 WFHRNPLKATAPVSFNYYGMITGPPASKICNDLRSARTRLLELFTDLSCNPETMKNAADLYFSLLQGFINSVGDSTQESK 83
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFILALDGKTQESK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  84 LRYIQNFKWTDTLQGHVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIP 163
Cdd:cd09243   81 LRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 164 KLLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHSAKWRKYLH 243
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 244 LKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKC 323
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 568911572 324 QRENGFIYFQKIPTEAPQLELKANYGLVEPVPF 356
Cdd:cd09243  321 ERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 4-356 0e+00

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185766  Cd Length: 353  Bit Score: 682.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   4 WFHRNPLKATAPVSFNYYGMITGPPASKICNDLRSARTRLLELFTDLSCNPETMKNAADLYFSLLQGFINSVGDSTQESK 83
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFILALDGKTQESK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  84 LRYIQNFKWTDTLQGHVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIP 163
Cdd:cd09243   81 LRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 164 KLLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHSAKWRKYLH 243
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 244 LKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKC 323
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 568911572 324 QRENGFIYFQKIPTEAPQLELKANYGLVEPVPF 356
Cdd:cd09243  321 ERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 5-390 1.99e-88

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 214990  Cd Length: 381  Bit Score: 273.07  E-value: 1.99e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572     5 FHRNPLKATAPVSF-----NYYGMITGPPASKICNDLrsarTRLLELFTDLsCNPETMKNAADL---YFSLLQGFINSVG 76
Cdd:smart01041   1 LIPLPLKETKEVDFskplkDYIKETYSEDSSSYEDEI----AELNRLRQAA-RTPSRDESGLELllkYYGQLEALELRFP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572    77 DSTQESKLryiqNFKWTDTLQGHVPSAQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKH 156
Cdd:smart01041  76 PPEGQLKL----SFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   157 LKESHIPKLltPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAI--ELKHAPGLIAALAYDTASFYQKADHTLSSLEPAH 234
Cdd:smart01041 149 LKENFLHAL--STEPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVK 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   235 S---AKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKeygeTKGPGPTAKPSGHLFFrk 311
Cdd:smart01041 227 GyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG-- 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   312 LGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKAnYGLVEPVPF----EFPPMSAHWTPeaLAAFDLTKRPKDDSVKPK 387
Cdd:smart01041 301 LKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKK-APLVKPPPFsevlKGPDLFAKLVP--MAVHEAASLYSEEKAKLV 377


                   ...
gi 568911572   388 PEE 390
Cdd:smart01041 378 RAE 380
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 89-374 3.14e-37

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 460803  Cd Length: 366  Bit Score: 138.87  E-value: 3.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   89 NFKWTDTLQ-GHVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHipkLL 166
Cdd:pfam03097  85 EFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENF---LH 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  167 TPAEkgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKAdHTLSSLEPAHSAKWRKYLHLKM 246
Cdd:pfam03097 158 APSP---DLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  247 CFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEAlCKEYGETKGpgptakpsghlFFRKLGSLVKNTLDKCQRE 326
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKD 301

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911572  327 NGFIYFQKIPTEA--PQLElKANygLVEPVPFEFP--------------PMSAHwtpEALAAFD 374
Cdd:pfam03097 302 NDFIYHERVPSESslPPIK-PAS--MVKPIPPLELypfqigpdlfkklvPLSVH---EAASAYS 359
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 4-356 0e+00

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185766  Cd Length: 353  Bit Score: 682.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   4 WFHRNPLKATAPVSFNYYGMITGPPASKICNDLRSARTRLLELFTDLSCNPETMKNAADLYFSLLQGFINSVGDSTQESK 83
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFILALDGKTQESK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  84 LRYIQNFKWTDTLQGHVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIP 163
Cdd:cd09243   81 LRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 164 KLLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHSAKWRKYLH 243
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 244 LKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKC 323
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320

                        330       340       350
                 ....*....|....*....|....*....|...
gi 568911572 324 QRENGFIYFQKIPTEAPQLELKANYGLVEPVPF 356
Cdd:cd09243  321 ERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 5-390 1.99e-88

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 214990  Cd Length: 381  Bit Score: 273.07  E-value: 1.99e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572     5 FHRNPLKATAPVSF-----NYYGMITGPPASKICNDLrsarTRLLELFTDLsCNPETMKNAADL---YFSLLQGFINSVG 76
Cdd:smart01041   1 LIPLPLKETKEVDFskplkDYIKETYSEDSSSYEDEI----AELNRLRQAA-RTPSRDESGLELllkYYGQLEALELRFP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572    77 DSTQESKLryiqNFKWTDTLQGHVPSAQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKH 156
Cdd:smart01041  76 PPEGQLKL----SFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   157 LKESHIPKLltPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAI--ELKHAPGLIAALAYDTASFYQKADHTLSSLEPAH 234
Cdd:smart01041 149 LKENFLHAL--STEPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVK 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   235 S---AKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKeygeTKGPGPTAKPSGHLFFrk 311
Cdd:smart01041 227 GyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG-- 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   312 LGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKAnYGLVEPVPF----EFPPMSAHWTPeaLAAFDLTKRPKDDSVKPK 387
Cdd:smart01041 301 LKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKK-APLVKPPPFsevlKGPDLFAKLVP--MAVHEAASLYSEEKAKLV 377


                   ...
gi 568911572   388 PEE 390
Cdd:smart01041 378 RAE 380
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 5-355 2.97e-70

Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1 and Rim20 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, HD-PTP, and Brox) and Snf7 (in the case of yeast Bro1, and Rim20). The single domain protein human Brox, and the isolated Bro1-like domains of Alix, HD-PTP and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix, HD-PTP, Bro1, and Rim20 also have a V-shaped (V) domain, which in the case of Alix, has been shown to be a dimerization domain and to contain a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in this superfamily. Alix, HD-PTP and Bro1 also have a proline-rich region (PRR); the Alix PRR binds multiple partners. Rhophilin-1, and -2, in addition to this Bro1-like domain, have an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This protein has a C-terminal, catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185761 [Multi-domain]  Cd Length: 345  Bit Score: 224.92  E-value: 2.97e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   5 FHRNPLKATAPVSF---------NYYGMITGPPASKICNDLRSARTRLLELFTDLSCNPETmKNAADLYFSLLQGFINSV 75
Cdd:cd09034    1 FIGLPLKKTKEVDVkvplskfipKNYGELEATAVEDLIEKLSKLRNNIVTEQNNDTTCENL-LEALKEYLPYLLGLEKKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  76 GdstqESKLRYIQNFKWTDTLQGHVPSAQqDAVFELISMGFNVALWYtkyaSRLAGKENIT--EDEAKEVHRSLKIAAGI 153
Cdd:cd09034   80 P----FQKLRDNVEFTWTDSFDTKKESAT-SLRYELLSILFNLAALA----SQLANEKLITgsEEDLKQAIKSLQKAAGY 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 154 FKHLKESHIPklLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHA-PGLIAALAYDTASFYQKADHTLSSLEP 232
Cdd:cd09034  151 FEYLKEHVLP--LPPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAkLSLLARLACEAAKYYEEALKCLSGVDL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 233 A----HSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGEtkgpgptakpSGHLF 308
Cdd:cd09034  229 EtiknIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKSFLL----------DVWGN 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 568911572 309 FRKLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKANYGLVEPVP 355
Cdd:cd09034  299 LKKLKEKIEKELEKAERENDFIYFEEVPPEDPLPEIKGALLVKPPPL 345
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 89-374 3.14e-37

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.


Pssm-ID: 460803  Cd Length: 366  Bit Score: 138.87  E-value: 3.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572   89 NFKWTDTLQ-GHVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHipkLL 166
Cdd:pfam03097  85 EFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENF---LH 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  167 TPAEkgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKAdHTLSSLEPAHSAKWRKYLHLKM 246
Cdd:pfam03097 158 APSP---DLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  247 CFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEAlCKEYGETKGpgptakpsghlFFRKLGSLVKNTLDKCQRE 326
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKD 301

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911572  327 NGFIYFQKIPTEA--PQLElKANygLVEPVPFEFP--------------PMSAHwtpEALAAFD 374
Cdd:pfam03097 302 NDFIYHERVPSESslPPIK-PAS--MVKPIPPLELypfqigpdlfkklvPLSVH---EAASAYS 359
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 90-357 1.07e-25

Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily; This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. These domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185770  Cd Length: 346  Bit Score: 106.71  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  90 FKWTDTLqGHVPSAQ----QDAVFELISMGFNVALWYTKYASRLagkeNITEDeAKEVHRSLKIAAGIFKHLKESHIPKL 165
Cdd:cd09247   88 FRWTSGL-GSSKGPKafqsDSLRFELGMVLFLYGAALRERASEV----LPTED-FKEAATHLRRAAGVFEFLAHDELPRL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 166 ---LTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLE---PAHSAKWR 239
Cdd:cd09247  162 rgaLSADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEAKNVLRSLAtdlKDLDPRFL 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 240 KYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEalckeygetkgpgPTAKPSGHLFFRKLGSLVKNT 319
Cdd:cd09247  242 RFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKL-------------PGSDISSPVIFRDERAEVATL 308

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568911572 320 LDKCQRENGFIYFQKIP--TEAPQLELKAnygLVEPVPFE 357
Cdd:cd09247  309 LQKYEKENEVIYFEKVPdiDELPLPEGKV---IVKPVPYK 345
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 90-339 1.22e-25

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and related proteins; This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 (also known as PalA) and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Bro1, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Rim20 and Rim23 participate in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Rim20. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain is a dimerization domain that also contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. Rim20 localizes to endosomes under alkaline pH conditions. By binding Snf7, it may bring the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and thus aid in the proteolytic activation of the latter. Rim20 and other intermediates in the Rim101 pathway play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis.


Pssm-ID: 185764  Cd Length: 355  Bit Score: 106.58  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  90 FKWTDTLQGHV--PSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHIPKLL 166
Cdd:cd09241   82 FTWYPTLGYKSsgPVSLSSLKFERANILYNLGALY----SQLALSENRYTDEGlKRACSYFQASAGCFEYILQHLLPTLS 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 167 TPaekgRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKAdhtLSSLEPAHSAK--WRKYLHL 244
Cdd:cd09241  158 PP----PDLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEA---LKYANKSDLIRsdWINHLKV 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 245 KMCFYTAYAYCYHGQTLLASDKCGEAIRSLQeaeklyaEAEALCKE-YGETKGPGPTAKPSghlfFRKLGSLVKNTLDKC 323
Cdd:cd09241  231 KKHHFKAAAHYRMALVALEKSKYGEEVARLR-------VALAACKEaLKEARYGNKAVLED----LQGLKDIVKESLKRA 299

                        250
                 ....*....|....*.
gi 568911572 324 QRENGFIYFQKIPTEA 339
Cdd:cd09241  300 ERDNDLIYLQPVPPAS 315
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 89-339 1.12e-24

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins; This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Rim20 (also known as PalA), Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1 participates in endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Bro1. Snf7 binds to a conserved hydrophobic patch on the middle of the concave side of the Bro1 domain. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. The Alix V-domain is also a dimerization domain. The C-terminal portion (V-domain and proline rich-region) of Bro1 interacts with Doa4, a protease that deubiquitinates integral membrane proteins sorted into the lumenal vesicles of late-endosomal multivesicular bodies. It interacts with a YPxL motif in the Doa4 catalytic domain to stimulate its deubiquitination activity.


Pssm-ID: 185765  Cd Length: 348  Bit Score: 103.90  E-value: 1.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  89 NFKWTDTLQGHVPSAQQDAVFELISMGFNVALWYTKYAsrlagKENITEDEA--KEVHRSLKIAAGIFKHLKES--HIPk 164
Cdd:cd09242   84 DFTWYDAFYKSKKVKQHSLAFEKASVLFNIGALLSQLA-----AEKYREDEDdlKEAITNLQQAAGCFQYINENflHAP- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 165 lltpaekGRDLEARLIDAYIIQCQAEAQEV----TIARAIELKHApGLIAALAYDTASFYQKADHTLSSLEPAHS----A 236
Cdd:cd09242  158 -------SVDLQQENVKFLVKLMLAQAQEIfllkLINGDDAQKKA-SLISKLASATANLYESCVEFLKEIQEKGIsygdP 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 237 KWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALckeygeTKGPGPTAKPSGHL---FFRKLG 313
Cdd:cd09242  230 KWISLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPQ------KLSLKASAGDAAYAlndDFKGQK 303

                        250       260
                 ....*....|....*....|....*.
gi 568911572 314 SLVKNTLDKCQRENGFIYFQKIPTEA 339
Cdd:cd09242  304 DTVEEKLKELEKDNDFIYHDIVPSEV 329
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 89-356 4.52e-20

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2.


Pssm-ID: 185763  Cd Length: 346  Bit Score: 90.43  E-value: 4.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  89 NFKWTDTLQ------GHVPSAQQDAVFELISMGFNVAlwytKYASRLAGKENI-TEDEAKEVHRSLKIAAGIFKHLKE-- 159
Cdd:cd09240   90 TFTWKDAFDkgslfgGSKKLALSSLGYEKVCVLFNIA----ALQSQIAAEQNLdTDEGLKLAAKLFQQAAGIFNHLKEtv 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 160 -SHIPKLLTPaekgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSslEPAHSAKW 238
Cdd:cd09240  166 lSALQQEPTP-----DLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQ--REDVRSLL 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 239 RK----YLHLKMCFYTAYAYcYHgQTLLA--SDKCGEAIRSLQEAEKLYAEAEALCKEYgetkgpgptakpsghLFFRKL 312
Cdd:cd09240  239 PKdwipVLAGKQAYFHALAE-YH-QSLVAkaQKKFGEEIARLQHALELIKTAQSRAGEY---------------VDVKDF 301

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568911572 313 GSLVKNTLDKCQRENGFIYFQKIPtEAPQLEL--KANygLVEPVPF 356
Cdd:cd09240  302 AAKISRALTAAKKDNDFIYHDRVP-DVKSLPPigKAA--LAKPTPV 344
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 90-356 6.85e-18

Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily; This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to this Bro1-like domain, Alix, Bro1, Rim20, HD_PTP, and proteins belonging to this uncharacterized family, also have a V-shaped (V) domain. The Alix V-domain is a dimerization domain, and contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the BRO1_Alix_like superfamily. Many members of this superfamily also have a proline-rich region (PRR), a protein interaction domain.


Pssm-ID: 185769  Cd Length: 353  Bit Score: 84.37  E-value: 6.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  90 FKWTDTLQGHVPSAQQDAVFELISMGFNV-ALWytkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHIPKLLT 167
Cdd:cd09246   89 FSWYDAFRPHRKATQANVHFEKAAVLFNLgALS-----SQLGLQQDRTTAEGiKQACHAFQAAAGAFAHLRDKVSGKTGG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 168 PAEKgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSS--LEPAHSAKWRKYLHLK 245
Cdd:cd09246  164 FRTP--DLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSppLKGHFDKSWVAHVQLK 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 246 MCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAealCKEygETKGPGPTAKpsghLFFRKLGSLVKNTLDKCQR 325
Cdd:cd09246  242 AAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEA---RKQ--AKGVNGDELI----EAVSELEQVINELLERAEK 312

                        250       260       270
                 ....*....|....*....|....*....|...
gi 568911572 326 ENGFIYFQKIPT--EAPQLELKAnygLVEPVPF 356
Cdd:cd09246  313 ENDCVYLDRVPApsDLPPLGAAS---MVKPAAP 342
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 53-358 3.35e-14

Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP) and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. HD-PTP participates in cell migration and endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185762  Cd Length: 361  Bit Score: 73.23  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  53 NPETMKNAADLYFSLLQGFINSVGDSTQESKLR-------YIQN-------------FKWTDTLQGHVpSAQQDAVFELI 112
Cdd:cd09239   36 DPELYSEELKSLEQLRQEAVNPPRDFEGCSVLKryygqlhLLQSrfpmgagqeaavpFTWTDIFSGSE-VTHEDIKFEEA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 113 SMGFNVALWYTKYAsrlAGKENITEDEAKEVHRSLKIAAGIFKHLKESHipkllTPAEKGRDLEARLIDAYIIQCQAEAQ 192
Cdd:cd09239  115 SVLYNIGALHSQLG---ASDKRDSEEGMKVACTHFQCAAWAFAYLREHY-----PQVYGAVDMSSQLLSFNYSLMLAQAQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 193 EVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLE-------PAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASD 265
Cdd:cd09239  187 ECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRALENWEsnskiilGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQ 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 266 KCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAkpsghlffRKLGSLVKNTLDKCQRENGFIYFQKIPtEAPQLELK 345
Cdd:cd09239  267 KMGERVAYYQLANDKLEEAIKNAKGQPDTVNLQEAL--------SFTMDVIGGKRNSAKKENDFIYHEAVP-KLDTLQAV 337

                        330
                 ....*....|...
gi 568911572 346 ANYGLVEPVPFEF 358
Cdd:cd09239  338 KGANLVKGIPFSP 350
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
 90-358 6.40e-09

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; This family contains the Bro1-like domain of RhoA-binding proteins, Rhophilin-1 and -2, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 and -2 bind both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 and -2, contain an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Their PDZ domains have limited homology. Rhophilin-1 and -2 have different activities. The Drosophila knockout of Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. Roles of Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix _like superfamily.


Pssm-ID: 185767  Cd Length: 350  Bit Score: 56.97  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  90 FKWTDTLQGhVPSAQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SHIPKLlt 167
Cdd:cd09244   85 FHWYDSLTG-VPSVQRSVAFEKASVLFNIGALYTQIGAK---QDRTTEEGIEAAVDAFQRAAGAFNYLREnfSNAPSM-- 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 168 paekgrDLEARLIDAYIIQCQAEAQEVT---IARAIELKHAPGLIAALAYDTASF---YQKAdHTLSSLEPAHSA---KW 238
Cdd:cd09244  159 ------DLSPEMLEALIKLMLAQAQECVfekLVLPGEDSKDIQACLDLAQEAAQVsdcYSEV-HKLMNQEPVKDYipySW 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 239 RKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEA---EALCKEygetkgpgPTAKPSGHLFFRKLGSL 315
Cdd:cd09244  232 ISLVEVKSEHYKALAHYYAAMGLLLEERRLLGKAHLKEALLLHEEAlrlHRMCRF--------LRNVDSLQEVLKEAHDR 303

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568911572 316 VKNTLDKCQRENGFiyfqKIPTEAPQLELKANYGLvEPVPFEF 358
Cdd:cd09244  304 SLNKYSSLEEEDDF----SDALDAPDIQAKTKQQL-EIIPPDF 341
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
 90-262 5.88e-05

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily contains the Bro1-like domain of RhoA-binding protein, Rhophilin-2. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-1, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-2, binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-2 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Roles for Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. Rhophilin-2 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185772  Cd Length: 385  Bit Score: 44.84  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  90 FKWTDTLQGhVPSAQQDAVFELISMGFNVALWYTKYASR-----LAGKENITEdeakevhrSLKIAAGIFKHLKE--SHI 162
Cdd:cd09249   85 FTWYDSFTG-VPVSQQNLLLEKASILFNIGALYTQIGTRcnrqtQAGLESAVD--------AFQRAAGVLNYLKEtfTHT 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 163 PKLltpaekgrDLEARLIDAYIIQCQAEAQEVTIARAIelkhAPGL---------IAALAYDTASFYQKAdHTLSSLEPA 233
Cdd:cd09249  156 PSY--------DMSPAMLSVLVKMMLAQAQECLFEKIS----LPGIrnefftlvkMAQEAAKVGEVYMQV-HTAMNQAPV 222

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568911572 234 HSA---KWRKYLHLKMCFYTAYAYCYHGQTLL 262
Cdd:cd09249  223 KENipySWSSLVQVKAHHYNALAHYFVATLLI 254
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 90-276 1.56e-03

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily contains the Bro1-like domain of the RhoA-binding protein, Rhophilin-1. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. The Drosophila knockout of the Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Rhophilin-1 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_ like superfamily.


Pssm-ID: 185771  Cd Length: 384  Bit Score: 40.25  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572  90 FKWTDTLQGhVPSAQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SHIPKLlt 167
Cdd:cd09248   85 FHWYDSLTG-VPAQQRALAFEKGSVLFNIGALHTQIGAR---QDRSCTEGTRRAIDAFQRAAGAFSLLREnfSNAPSP-- 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911572 168 paekgrDLEARLIDAYIIQCQAEAQEVTIAR-AIELKHAPGL------IAALAYDTASFYQKADHTLSSlEPAHS---AK 237
Cdd:cd09248  159 ------DMSTASLSMLEQLMVAQAQECIFEGlLLPLLATPQDffaqlqLAQEAAQVAAEYRLVHRTMAQ-PPVRDyvpFS 231

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568911572 238 WRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQE 276
Cdd:cd09248  232 WTALVHVKAEHFCALAHYHAAMALCDSSPASEGELATQE 270
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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