NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564381992|ref|XP_006250416|]
View 

BRO1 domain-containing protein BROX isoform X2 [Rattus norvegicus]

Protein Classification

BRO1 domain-containing protein( domain architecture ID 52469)

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

PubMed:  15935782|19403673

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
BRO1_Alix_like super family cl14649
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
4-288 0e+00

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.


The actual alignment was detected with superfamily member cd09243:

Pssm-ID: 472700  Cd Length: 353  Bit Score: 540.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   4 WFHRNPLKATAPVSFNYYGMITGPPASKICN------------------------------------------------- 34
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSdlrtararllellsdpsndvdtvktafnaylsllqgfilaldgktqesk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  35 -------------------AQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIP 95
Cdd:cd09243   81 lrylinfkwtdsllgnepsVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  96 KLLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSSLEPAHSAKWRKYLH 175
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 176 LKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKC 255
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 564381992 256 QRENGFIYFQKIPTEAPQLELKANYGLVEPVPF 288
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 ...
4-288 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: 540.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   4 WFHRNPLKATAPVSFNYYGMITGPPASKICN------------------------------------------------- 34
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSdlrtararllellsdpsndvdtvktafnaylsllqgfilaldgktqesk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  35 -------------------AQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIP 95
Cdd:cd09243   81 lrylinfkwtdsllgnepsVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  96 KLLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSSLEPAHSAKWRKYLH 175
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 176 LKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKC 255
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 564381992 256 QRENGFIYFQKIPTEAPQLELKANYGLVEPVPF 288
Cdd:cd09243  321 ERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
15-316 3.44e-73

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: 231.47  E-value: 3.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992    15 PVSFNYYGMITGPPASKicnaQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKHLKESHI 94
Cdd:smart01041  82 KLSFTWYDSLDTGVPST----QSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNYLKENFL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992    95 PKLltPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAI--ELKHAPGLIAALAYETASFYQKADHTLSSLEPAHS---AK 169
Cdd:smart01041 155 HAL--STEPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVKGyipKS 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   170 WRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKeygeTKGPGPTAKPSGHLFFrkLGSLVK 249
Cdd:smart01041 233 WIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG--LKDVVE 306
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564381992   250 NTLDKCQRENGFIYFQKIPTEAPQLELKAnYGLVEPVPF----EFPPMSALWTPEALAAFDLTKRPKDDSI 316
Cdd:smart01041 307 EKLKEAEKDNDFIYHERVPDIVSLPPIKK-APLVKPPPFsevlKGPDLFAKLVPMAVHEAASLYSEEKAKL 376
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
7-289 4.07e-33

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: 125.77  E-value: 4.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992    7 RNPLKATAPVSFNYYGMItGPPASKICnaQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGI 85
Cdd:pfam03097  75 RFPIDIQIGIEFTWYDAF-GTSSKKVS--QSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGC 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   86 FKHLKESHipkLLTPAEkgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKAdHTLSSLEPA 165
Cdd:pfam03097 148 FQYLKENF---LHAPSP---DLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGL 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  166 HSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEAlCKEYGETKGpgptakpsghlFFRKLG 245
Cdd:pfam03097 221 IDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLL 288
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 564381992  246 SLVKNTLDKCQRENGFIYFQKIPTEA--PQLElKANygLVEPVPFE 289
Cdd:pfam03097 289 DVVEEKLKRAEKDNDFIYHERVPSESslPPIK-PAS--MVKPIPPL 331
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
4-288 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: 540.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   4 WFHRNPLKATAPVSFNYYGMITGPPASKICN------------------------------------------------- 34
Cdd:cd09243    1 WFHRNPLKATAPVKFDLKGVATTPAASKLCSdlrtararllellsdpsndvdtvktafnaylsllqgfilaldgktqesk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  35 -------------------AQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIP 95
Cdd:cd09243   81 lrylinfkwtdsllgnepsVQQDAIFELASMLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  96 KLLTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSSLEPAHSAKWRKYLH 175
Cdd:cd09243  161 KLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 176 LKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKC 255
Cdd:cd09243  241 LKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKC 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 564381992 256 QRENGFIYFQKIPTEAPQLELKANYGLVEPVPF 288
Cdd:cd09243  321 ERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
15-316 3.44e-73

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: 231.47  E-value: 3.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992    15 PVSFNYYGMITGPPASKicnaQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKHLKESHI 94
Cdd:smart01041  82 KLSFTWYDSLDTGVPST----QSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNYLKENFL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992    95 PKLltPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAI--ELKHAPGLIAALAYETASFYQKADHTLSSLEPAHS---AK 169
Cdd:smart01041 155 HAL--STEPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVKGyipKS 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   170 WRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKeygeTKGPGPTAKPSGHLFFrkLGSLVK 249
Cdd:smart01041 233 WIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG--LKDVVE 306
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564381992   250 NTLDKCQRENGFIYFQKIPTEAPQLELKAnYGLVEPVPF----EFPPMSALWTPEALAAFDLTKRPKDDSI 316
Cdd:smart01041 307 EKLKEAEKDNDFIYHERVPDIVSLPPIKK-APLVKPPPFsevlKGPDLFAKLVPMAVHEAASLYSEEKAKL 376
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
36-287 8.47e-60

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: 195.65  E-value: 8.47e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  36 QQDAVFELISMGFNVALWYtkyaSRLAGKENIT--EDEAKEVHRSLKIAAGIFKHLKESHIPklLTPAEKGRDLEARLID 113
Cdd:cd09034  103 ATSLRYELLSILFNLAALA----SQLANEKLITgsEEDLKQAIKSLQKAAGYFEYLKEHVLP--LPPDELPVDLTEAVLS 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 114 AYIIQCQAEAQEVTIARAIELKHA-PGLIAALAYETASFYQKADHTLSSLEPA----HSAKWRKYLHLKMCFYTAYAYCY 188
Cdd:cd09034  177 ALSLIMLAQAQECFLLKAEEDKKAkLSLLARLACEAAKYYEEALKCLSGVDLEtiknIPKKWLLFLKWKKCIFKALAYYY 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 189 HGQTLLASDKCGEAIRSLQEAEKLYAEAEALCKEYGEtkgpgptakpSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIP 268
Cdd:cd09034  257 HGLKLDEANKIGEAIARLQAALELLKESERLCKSFLL----------DVWGNLKKLKEKIEKELEKAERENDFIYFEEVP 326
                        250
                 ....*....|....*....
gi 564381992 269 TEAPQLELKANYGLVEPVP 287
Cdd:cd09034  327 PEDPLPEIKGALLVKPPPL 345
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
7-289 4.07e-33

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: 125.77  E-value: 4.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992    7 RNPLKATAPVSFNYYGMItGPPASKICnaQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGI 85
Cdd:pfam03097  75 RFPIDIQIGIEFTWYDAF-GTSSKKVS--QSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGC 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   86 FKHLKESHipkLLTPAEkgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKAdHTLSSLEPA 165
Cdd:pfam03097 148 FQYLKENF---LHAPSP---DLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGL 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  166 HSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAEAlCKEYGETKGpgptakpsghlFFRKLG 245
Cdd:pfam03097 221 IDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLL 288
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 564381992  246 SLVKNTLDKCQRENGFIYFQKIPTEA--PQLElKANygLVEPVPFE 289
Cdd:pfam03097 289 DVVEEKLKRAEKDNDFIYHERVPSESslPPIK-PAS--MVKPIPPL 331
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
37-289 3.02e-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: 104.01  E-value: 3.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  37 QDAVFELISMGFNVALWYTKYASRLagkeNITEDeAKEVHRSLKIAAGIFKHLKESHIPKL---LTPAEKGRDLEARLID 113
Cdd:cd09247  106 DSLRFELGMVLFLYGAALRERASEV----LPTED-FKEAATHLRRAAGVFEFLAHDELPRLrgaLSADERPPECTPSLAL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 114 AYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSSLE---PAHSAKWRKYLHLKMCFYTAYAYCYHG 190
Cdd:cd09247  181 AMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEAKNVLRSLAtdlKDLDPRFLRFISSCIALHEARSQLYLA 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 191 QTLLASDKCGEAIRSLQEAEKLYAEAEalckeygetkgpgPTAKPSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIP-- 268
Cdd:cd09247  261 RRLKEAGHIGVAVGVLREALRNLKKKL-------------PGSDISSPVIFRDERAEVATLLQKYEKENEVIYFEKVPdi 327
                        250       260
                 ....*....|....*....|.
gi 564381992 269 TEAPQLELKAnygLVEPVPFE 289
Cdd:cd09247  328 DELPLPEGKV---IVKPVPYK 345
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
4-311 6.35e-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: 103.50  E-value: 6.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992   4 WFHRNPLKATAPVSFNyygmitgppaskicnaqqDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIA 82
Cdd:cd09241   84 WYPTLGYKSSGPVSLS------------------SLKFERANILYNLGALY----SQLALSENRYTDEGlKRACSYFQAS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  83 AGIFKHLKESHIPKLLTPaekgRDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKAdhtLSSL 162
Cdd:cd09241  142 AGCFEYILQHLLPTLSPP----PDLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEA---LKYA 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 163 EPAHSAK--WRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQeaeklyaEAEALCKE-YGETKGPGPTAKPSghl 239
Cdd:cd09241  215 NKSDLIRsdWINHLKVKKHHFKAAAHYRMALVALEKSKYGEEVARLR-------VALAACKEaLKEARYGNKAVLED--- 284
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564381992 240 fFRKLGSLVKNTLDKCQRENGFIYFQKIPTEApqlELKanygLVEPVpfefpPMSALWTPEALAAFDLTKRP 311
Cdd:cd09241  285 -LQGLKDIVKESLKRAERDNDLIYLQPVPPAS---ELP----PIKPA-----SMVKAIVPPELEEGSKLGKP 343
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
40-271 1.50e-20

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: 90.80  E-value: 1.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  40 VFELISMGFNVALWYTKYAsrlagKENITEDEA--KEVHRSLKIAAGIFKHLKES--HIPklltpaekGRDLEARLIDAY 115
Cdd:cd09242  103 AFEKASVLFNIGALLSQLA-----AEKYREDEDdlKEAITNLQQAAGCFQYINENflHAP--------SVDLQQENVKFL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 116 IIQCQAEAQEV----TIARAIELKHApGLIAALAYETASFYQKADHTLSSLEPAHS----AKWRKYLHLKMCFYTAYAYC 187
Cdd:cd09242  170 VKLMLAQAQEIfllkLINGDDAQKKA-SLISKLASATANLYESCVEFLKEIQEKGIsygdPKWISLVQCKAHYYKSLAAY 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 188 YHGQTLLASDKCGEAIRSLQEAEKLYAEAEALckeygeTKGPGPTAKPSGHL---FFRKLGSLVKNTLDKCQRENGFIYF 264
Cdd:cd09242  249 YHALALEAAGKYGEAIAYLTQAESILKEANPQ------KLSLKASAGDAAYAlndDFKGQKDTVEEKLKELEKDNDFIYH 322

                 ....*..
gi 564381992 265 QKIPTEA 271
Cdd:cd09242  323 DIVPSEV 329
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
38-288 6.54e-18

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: 83.50  E-value: 6.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  38 DAVFELISMGFNVAlwytKYASRLAGKENI-TEDEAKEVHRSLKIAAGIFKHLKE---SHIPKLLTPaekgrDLEARLID 113
Cdd:cd09240  113 SLGYEKVCVLFNIA----ALQSQIAAEQNLdTDEGLKLAAKLFQQAAGIFNHLKEtvlSALQQEPTP-----DLSPDTLS 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 114 AYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSslEPAHSAKWRK----YLHLKMCFYTAYAYcYH 189
Cdd:cd09240  184 ALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQ--REDVRSLLPKdwipVLAGKQAYFHALAE-YH 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 190 gQTLLA--SDKCGEAIRSLQEAEKLYAEAEALCKEYgetkgpgptakpsghLFFRKLGSLVKNTLDKCQRENGFIYFQKI 267
Cdd:cd09240  261 -QSLVAkaQKKFGEEIARLQHALELIKTAQSRAGEY---------------VDVKDFAAKISRALTAAKKDNDFIYHDRV 324
                        250       260
                 ....*....|....*....|...
gi 564381992 268 PtEAPQLEL--KANygLVEPVPF 288
Cdd:cd09240  325 P-DVKSLPPigKAA--LAKPTPV 344
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
16-288 5.67e-14

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: 72.04  E-value: 5.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  16 VSFNYYGmiTGPPASKICnaQQDAVFELISMGFNV-ALWytkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESH 93
Cdd:cd09246   87 VSFSWYD--AFRPHRKAT--QANVHFEKAAVLFNLgALS-----SQLGLQQDRTTAEGiKQACHAFQAAAGAFAHLRDKV 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  94 IPKLLTPAEKgrDLEARLIDAYIIQCQAEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSS--LEPAHSAKWR 171
Cdd:cd09246  158 SGKTGGFRTP--DLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSppLKGHFDKSWV 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 172 KYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEAealCKEYGETKGpgptakPSGHLFFRKLGSLVKNT 251
Cdd:cd09246  236 AHVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEA---RKQAKGVNG------DELIEAVSELEQVINEL 306
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564381992 252 LDKCQRENGFIYFQKIPT--EAPQLELKAnygLVEPVPF 288
Cdd:cd09246  307 LERAEKENDCVYLDRVPApsDLPPLGAAS---MVKPAAP 342
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
41-290 1.89e-12

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: 67.45  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  41 FELISMGFNVALWYTKYAsrlAGKENITEDEAKEVHRSLKIAAGIFKHLKESHipkllTPAEKGRDLEARLIDAYIIQCQ 120
Cdd:cd09239  111 FEEASVLYNIGALHSQLG---ASDKRDSEEGMKVACTHFQCAAWAFAYLREHY-----PQVYGAVDMSSQLLSFNYSLML 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 121 AEAQEVTIARAIELKHAPGLIAALAYETASFYQKADHTLSSLE-------PAHSAKWRKYLHLKMCFYTAYAYCYHGQTL 193
Cdd:cd09239  183 AQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRALENWEsnskiilGKIQKEWRKLVQMKIAYYASIAHLHMGKQS 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 194 LASDKCGEAIRSLQEAEKLYAEAEALCKEYGETKGPGPTAkpsghlffRKLGSLVKNTLDKCQRENGFIYFQKIPtEAPQ 273
Cdd:cd09239  263 EEQQKMGERVAYYQLANDKLEEAIKNAKGQPDTVNLQEAL--------SFTMDVIGGKRNSAKKENDFIYHEAVP-KLDT 333
                        250
                 ....*....|....*..
gi 564381992 274 LELKANYGLVEPVPFEF 290
Cdd:cd09239  334 LQAVKGANLVKGIPFSP 350
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
16-290 2.56e-07

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: 51.57  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  16 VSFNYYGMITGPPASkicnaQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SH 93
Cdd:cd09244   83 IYFHWYDSLTGVPSV-----QRSVAFEKASVLFNIGALYTQIGAK---QDRTTEEGIEAAVDAFQRAAGAFNYLREnfSN 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  94 IPKLltpaekgrDLEARLIDAYIIQCQAEAQEVT---IARAIELKHAPGLIAALAYETASF---YQKAdHTLSSLEPAHS 167
Cdd:cd09244  155 APSM--------DLSPEMLEALIKLMLAQAQECVfekLVLPGEDSKDIQACLDLAQEAAQVsdcYSEV-HKLMNQEPVKD 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992 168 A---KWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAEKLYAEA---EALCKEygetkgpgPTAKPSGHLFF 241
Cdd:cd09244  226 YipySWISLVEVKSEHYKALAHYYAAMGLLLEERRLLGKAHLKEALLLHEEAlrlHRMCRF--------LRNVDSLQEVL 297
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564381992 242 RKLGSLVKNTLDKCQRENGFiyfqKIPTEAPQLELKANYGLvEPVPFEF 290
Cdd:cd09244  298 KEAHDRSLNKYSSLEEEDDF----SDALDAPDIQAKTKQQL-EIIPPDF 341
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
18-194 1.07e-03

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: 40.60  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  18 FNYYGMITGPPASkicnaQQDAVFELISMGFNVALWYTKYASR-----LAGKENITEdeakevhrSLKIAAGIFKHLKE- 91
Cdd:cd09249   85 FTWYDSFTGVPVS-----QQNLLLEKASILFNIGALYTQIGTRcnrqtQAGLESAVD--------AFQRAAGVLNYLKEt 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381992  92 -SHIPKLltpaekgrDLEARLIDAYIIQCQAEAQEVTIARAIelkhAPGL---------IAALAYETASFYQKAdHTLSS 161
Cdd:cd09249  152 fTHTPSY--------DMSPAMLSVLVKMMLAQAQECLFEKIS----LPGIrnefftlvkMAQEAAKVGEVYMQV-HTAMN 218
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564381992 162 LEPAHSA---KWRKYLHLKMCFYTAYAYCYHGQTLL 194
Cdd:cd09249  219 QAPVKENipySWSSLVQVKAHHYNALAHYFVATLLI 254
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH