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Conserved domains on  [gi|568384725|ref|NP_001275510|]
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BRO1 domain-containing protein BROX isoform c [Homo sapiens]

Protein Classification

BRO1_Brox_like domain-containing protein( domain architecture ID 10174120)

BRO1_Brox_like domain-containing protein

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 ...
 4-330 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: 641.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   4 WFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESK 83
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFILALDGKTQESK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  84 LRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLP 163
Cdd:cd09243   81 LRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 164 KLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLH 243
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 244 LKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKC 323
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320


                 ....*..
gi 568384725 324 QRENGFI 330
Cdd:cd09243  321 ERENGFI 327
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 4-330 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: 641.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   4 WFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESK 83
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFILALDGKTQESK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  84 LRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLP 163
Cdd:cd09243   81 LRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 164 KLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLH 243
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 244 LKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKC 323
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320


                 ....*..
gi 568384725 324 QRENGFI 330
Cdd:cd09243  321 ERENGFI 327
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 5-330 1.87e-79

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: 247.27  E-value: 1.87e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725     5 FHRNPLKATAPVSF-----NYYGVVTGPSASKICNDLrssrARLLELFTDLsCNPEMMKNAADS---YFSLLQGFINSLD 76
Cdd:smart01041   1 LIPLPLKETKEVDFskplkDYIKETYSEDSSSYEDEI----AELNRLRQAA-RTPSRDESGLELllkYYGQLEALELRFP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725    77 ESTQESKLryiqNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKH 156
Cdd:smart01041  76 PPEGQLKL----SFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   157 LKESHLPKLITpaEKGRDLESRLIEAYVIQCQAEAQEVTIARAI--ELKHAPGLIAALAYETANFYQKADHTLSSLEPAY 234
Cdd:smart01041 149 LKENFLHALST--EPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVK 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   235 S---AKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKeygeTKGPGPTVKPSGHLFFrk 311
Cdd:smart01041 227 GyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG-- 300

                          330
                   ....*....|....*....
gi 568384725   312 LGNLVKNTLEKCQRENGFI 330
Cdd:smart01041 301 LKDVVEEKLKEAEKDNDFI 319
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 89-330 2.98e-31

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: 120.76  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   89 NFKWTDTLQ-GQVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKli 166
Cdd:pfam03097  85 EFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENFLHA-- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  167 tpaeKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKAdHTLSSLEPAYSAKWRKYLHLKM 246
Cdd:pfam03097 159 ----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  247 CFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEAlCKEYGETKGpgptvkpsghlFFRKLGNLVKNTLEKCQRE 326
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKD 301


                  ....
gi 568384725  327 NGFI 330
Cdd:pfam03097 302 NDFI 305
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 4-330 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: 641.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   4 WFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESK 83
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSDLRTARARLLELLSDPSNDVDTVKTAFNAYLSLLQGFILALDGKTQESK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  84 LRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLP 163
Cdd:cd09243   81 LRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 164 KLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLH 243
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 244 LKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKC 323
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320


                 ....*..
gi 568384725 324 QRENGFI 330
Cdd:cd09243  321 ERENGFI 327
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 5-330 1.87e-79

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: 247.27  E-value: 1.87e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725     5 FHRNPLKATAPVSF-----NYYGVVTGPSASKICNDLrssrARLLELFTDLsCNPEMMKNAADS---YFSLLQGFINSLD 76
Cdd:smart01041   1 LIPLPLKETKEVDFskplkDYIKETYSEDSSSYEDEI----AELNRLRQAA-RTPSRDESGLELllkYYGQLEALELRFP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725    77 ESTQESKLryiqNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKH 156
Cdd:smart01041  76 PPEGQLKL----SFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   157 LKESHLPKLITpaEKGRDLESRLIEAYVIQCQAEAQEVTIARAI--ELKHAPGLIAALAYETANFYQKADHTLSSLEPAY 234
Cdd:smart01041 149 LKENFLHALST--EPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVK 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   235 S---AKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKeygeTKGPGPTVKPSGHLFFrk 311
Cdd:smart01041 227 GyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG-- 300

                          330
                   ....*....|....*....
gi 568384725   312 LGNLVKNTLEKCQRENGFI 330
Cdd:smart01041 301 LKDVVEEKLKEAEKDNDFI 319
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 5-330 8.91e-64

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: 205.66  E-value: 8.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   5 FHRNPLKATAPVSFnyygvvTGPSASKICNDLRSSRA----RLLELFTDLSCNPEMM----------KNAADSYFSLLQG 70
Cdd:cd09034    1 FIGLPLKKTKEVDV------KVPLSKFIPKNYGELEAtaveDLIEKLSKLRNNIVTEqnndttcenlLEALKEYLPYLLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  71 FINSLDEStqesKLRYIQNFKWTDTLQGQVPSAQqDAVFELISMGFNVALWYtkyaSRLAGKENIT--EDEAKEVHRSLK 148
Cdd:cd09034   75 LEKKLPFQ----KLRDNVEFTWTDSFDTKKESAT-SLRYELLSILFNLAALA----SQLANEKLITgsEEDLKQAIKSLQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 149 IAAGIFKHLKESHLPKliTPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHA-PGLIAALAYETANFYQKADHTL 227
Cdd:cd09034  146 KAAGYFEYLKEHVLPL--PPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAkLSLLARLACEAAKYYEEALKCL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 228 SSLEPAYS----AKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGEtkgpgptvkp 303
Cdd:cd09034  224 SGVDLETIknipKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKSFLL---------- 293

                        330       340
                 ....*....|....*....|....*..
gi 568384725 304 SGHLFFRKLGNLVKNTLEKCQRENGFI 330
Cdd:cd09034  294 DVWGNLKKLKEKIEKELEKAERENDFI 320
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 89-330 2.98e-31

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: 120.76  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725   89 NFKWTDTLQ-GQVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKli 166
Cdd:pfam03097  85 EFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENFLHA-- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  167 tpaeKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKAdHTLSSLEPAYSAKWRKYLHLKM 246
Cdd:pfam03097 159 ----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  247 CFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEAlCKEYGETKGpgptvkpsghlFFRKLGNLVKNTLEKCQRE 326
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKD 301


                  ....
gi 568384725  327 NGFI 330
Cdd:pfam03097 302 NDFI 305
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 90-330 1.66e-24

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: 101.96  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  90 FKWTDTL--QGQVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKLI 166
Cdd:cd09241   82 FTWYPTLgyKSSGPVSLSSLKFERANILYNLGALY----SQLALSENRYTDEGlKRACSYFQASAGCFEYILQHLLPTLS 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 167 TPaekgRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKAdHTLSSLEPAYSAKWRKYLHLKM 246
Cdd:cd09241  158 PP----PDLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEA-LKYANKSDLIRSDWINHLKVKK 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 247 CFYTAYAYCYHGETLLASDKCGEAIRSLQEaeklyakAEALCKE-YGETKGPGPTVKPSghlfFRKLGNLVKNTLEKCQR 325
Cdd:cd09241  233 HHFKAAAHYRMALVALEKSKYGEEVARLRV-------ALAACKEaLKEARYGNKAVLED----LQGLKDIVKESLKRAER 301


                 ....*
gi 568384725 326 ENGFI 330
Cdd:cd09241  302 DNDLI 306
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 63-330 2.47e-23

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: 98.62  E-value: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  63 SYFSLLQGFINSLDESTQESKLRyiqnFKWTDTLQGQVP--SAQQDAV-FELISMGFNVALWYTKYASRLagkeNITEDe 139
Cdd:cd09247   65 GYLPALENLVNHRDKVQLNEQLS----FRWTSGLGSSKGpkAFQSDSLrFELGMVLFLYGAALRERASEV----LPTED- 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 140 AKEVHRSLKIAAGIFKHLKESHLPKLIT---PAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYET 216
Cdd:cd09247  136 FKEAATHLRRAAGVFEFLAHDELPRLRGalsADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGA 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 217 ANFYQKADHTLSSLEPAYSA---KWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEalckeyge 293
Cdd:cd09247  216 TQFLEEAKNVLRSLATDLKDldpRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKL-------- 287

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568384725 294 tkgpgPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFI 330
Cdd:cd09247  288 -----PGSDISSPVIFRDERAEVATLLQKYEKENEVI 319
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 89-280 2.36e-21

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: 93.11  E-value: 2.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  89 NFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYAsrlagKENITEDEA--KEVHRSLKIAAGIFKHLKES--HLPk 164
Cdd:cd09242   84 DFTWYDAFYKSKKVKQHSLAFEKASVLFNIGALLSQLA-----AEKYREDEDdlKEAITNLQQAAGCFQYINENflHAP- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 165 litpaekGRDLESRLIEAYVIQCQAEAQEV----TIARAIELKHApGLIAALAYETANFYQKADHTLSSLEPA----YSA 236
Cdd:cd09242  158 -------SVDLQQENVKFLVKLMLAQAQEIfllkLINGDDAQKKA-SLISKLASATANLYESCVEFLKEIQEKgisyGDP 229

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568384725 237 KWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKL 280
Cdd:cd09242  230 KWISLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESI 273
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 89-330 3.76e-17

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: 81.19  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  89 NFKWTDTLQ------GQVPSAQQDAVFELISMGFNVAlwytKYASRLAGKENI-TEDEAKEVHRSLKIAAGIFKHLKE-- 159
Cdd:cd09240   90 TFTWKDAFDkgslfgGSKKLALSSLGYEKVCVLFNIA----ALQSQIAAEQNLdTDEGLKLAAKLFQQAAGIFNHLKEtv 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 160 -SHLPKLITPaekgrDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLS--SLEPAYSA 236
Cdd:cd09240  166 lSALQQEPTP-----DLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQreDVRSLLPK 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 237 KWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYgetkgpgptvkpsghLFFRKLGNLV 316
Cdd:cd09240  241 DWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEY---------------VDVKDFAAKI 305

                        250
                 ....*....|....
gi 568384725 317 KNTLEKCQRENGFI 330
Cdd:cd09240  306 SRALTAAKKDNDFI 319
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 90-327 2.01e-13

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: 70.12  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  90 FKWTDTLQGQVPSAQQDAVFELISMGFNV-ALWytkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKLIT 167
Cdd:cd09246   89 FSWYDAFRPHRKATQANVHFEKAAVLFNLgALS-----SQLGLQQDRTTAEGiKQACHAFQAAAGAFAHLRDKVSGKTGG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 168 PAEKgrDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSS--LEPAYSAKWRKYLHLK 245
Cdd:cd09246  164 FRTP--DLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSppLKGHFDKSWVAHVQLK 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 246 MCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAealCKEygETKGPGPTVKpsghLFFRKLGNLVKNTLEKCQR 325
Cdd:cd09246  242 AAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEA---RKQ--AKGVNGDELI----EAVSELEQVINELLERAEK 312


                 ..
gi 568384725 326 EN 327
Cdd:cd09246  313 EN 314
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 53-330 2.08e-11

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: 64.37  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  53 NPEMMKNAADSYFSLLQGFINSLDESTQESKLR-------YIQN-------------FKWTDTLQGQVpSAQQDAVFELI 112
Cdd:cd09239   36 DPELYSEELKSLEQLRQEAVNPPRDFEGCSVLKryygqlhLLQSrfpmgagqeaavpFTWTDIFSGSE-VTHEDIKFEEA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 113 SMGFNVALWYTKYAsrlAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPklitpAEKGRDLESRLIEAYVIQCQAEAQ 192
Cdd:cd09239  115 SVLYNIGALHSQLG---ASDKRDSEEGMKVACTHFQCAAWAFAYLREHYPQ-----VYGAVDMSSQLLSFNYSLMLAQAQ 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 193 EVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLE-------PAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASD 265
Cdd:cd09239  187 ECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRALENWEsnskiilGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQ 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568384725 266 KCGEAIRSLQEAEKlyaKAEALCKEYgetKGPGPTVKPSGHLFFrkLGNLVKNTLEKCQRENGFI 330
Cdd:cd09239  267 KMGERVAYYQLAND---KLEEAIKNA---KGQPDTVNLQEALSF--TMDVIGGKRNSAKKENDFI 323
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
 90-290 2.36e-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: 57.74  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  90 FKWTDTLQGqVPSAQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SHLPKLit 167
Cdd:cd09244   85 FHWYDSLTG-VPSVQRSVAFEKASVLFNIGALYTQIGAK---QDRTTEEGIEAAVDAFQRAAGAFNYLREnfSNAPSM-- 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 168 paekgrDLESRLIEAYVIQCQAEAQEVT---IARAIELKHAPGLIAALAYETANF---YQKAdHTLSSLEPA-----YSa 236
Cdd:cd09244  159 ------DLSPEMLEALIKLMLAQAQECVfekLVLPGEDSKDIQACLDLAQEAAQVsdcYSEV-HKLMNQEPVkdyipYS- 230

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568384725 237 kWRKYLHLKMCFYTAYAYCYHGETLLASDK-------CGEAIRSLQEAEKLYakaeALCKE 290
Cdd:cd09244  231 -WISLVEVKSEHYKALAHYYAAMGLLLEERrllgkahLKEALLLHEEALRLH----RMCRF 286
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
 63-262 1.12e-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: 46.77  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  63 SYFSLLqGFInsldESTQESKLRYIQN-FKWTDTLQGqVPSAQQDAVFELISMGFNVALWYTKYASR-----LAGKENIT 136
Cdd:cd09249   62 SYFSQL-GFL----ENRFFPPTRQMGIlFTWYDSFTG-VPVSQQNLLLEKASILFNIGALYTQIGTRcnrqtQAGLESAV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725 137 EdeakevhrSLKIAAGIFKHLKE--SHLPKLitpaekgrDLESRLIEAYVIQCQAEAQEVTIARAIelkhAPGL------ 208
Cdd:cd09249  136 D--------AFQRAAGVLNYLKEtfTHTPSY--------DMSPAMLSVLVKMMLAQAQECLFEKIS----LPGIrnefft 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568384725 209 ---IAALAYETANFYQKAdHTLSSLEPA-----YSakWRKYLHLKMCFYTAYAYCYHGETLL 262
Cdd:cd09249  196 lvkMAQEAAKVGEVYMQV-HTAMNQAPVkenipYS--WSSLVQVKAHHYNALAHYFVATLLI 254
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 90-187 3.18e-04

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: 42.17  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568384725  90 FKWTDTLQGqVPSAQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SHLPKLIT 167
Cdd:cd09248   85 FHWYDSLTG-VPAQQRALAFEKGSVLFNIGALHTQIGAR---QDRSCTEGTRRAIDAFQRAAGAFSLLREnfSNAPSPDM 160

                         90       100
                 ....*....|....*....|
gi 568384725 168 PAEKGRDLEsRLIEAYVIQC 187
Cdd:cd09248  161 STASLSMLE-QLMVAQAQEC 179
 
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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