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Conserved domains on  [gi|568911576|ref|XP_006535663|]
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BRO1 domain-containing protein BROX isoform X3 [Mus musculus]

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

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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 ...
1-243 2.67e-174

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: 485.69  E-value: 2.67e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   1 MGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIPKLLTPAEKGRDLEARLIDAYIIQCQAEAQE 80
Cdd:cd09243  111 MLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  81 VTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRS 160
Cdd:cd09243  191 VTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRS 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 161 LQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKANYGLVEP 240
Cdd:cd09243  271 LQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSP 350

                 ...
gi 568911576 241 VPF 243
Cdd:cd09243  351 EEF 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 ...
1-243 2.67e-174

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: 485.69  E-value: 2.67e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   1 MGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIPKLLTPAEKGRDLEARLIDAYIIQCQAEAQE 80
Cdd:cd09243  111 MLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  81 VTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRS 160
Cdd:cd09243  191 VTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRS 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 161 LQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKANYGLVEP 240
Cdd:cd09243  271 LQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSP 350

                 ...
gi 568911576 241 VPF 243
Cdd:cd09243  351 EEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
1-277 2.84e-66

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: 211.83  E-value: 2.84e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576     1 MGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKHLKESHIPKLltPAEKGRDLEARLIDAYIIQCQAEAQE 80
Cdd:smart01041 109 VLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNYLKENFLHAL--STEPSVDLSPETLSALSSLMLAQAQE 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576    81 VTIARAI--ELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHS---AKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCG 155
Cdd:smart01041 184 CFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVKGyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYG 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   156 EAIRSLQEAEKLYAEAEALCKeygeTKGPGPTAKPSGHLFFrkLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKAnY 235
Cdd:smart01041 264 EAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG--LKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKK-A 336
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 568911576   236 GLVEPVPF----EFPPMSAHWTPeaLAAFDLTKRPKDDSVKPKPEE 277
Cdd:smart01041 337 PLVKPPPFsevlKGPDLFAKLVP--MAVHEAASLYSEEKAKLVRAE 380
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
3-261 5.13e-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: 119.22  E-value: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576    3 FNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHipkLLTPAEkgrDLEARLIDAYIIQCQAEAQEV 81
Cdd:pfam03097 113 FNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENF---LHAPSP---DLSPETLKALSNLMLAQAQEC 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   82 TIARAIELKHAPGLIAALAYDTASFYQKAdHTLSSLEPAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSL 161
Cdd:pfam03097 183 FWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARL 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  162 QEAEKLYAEAEAlCKEYGETKGpgptakpsghlFFRKLGSLVKNTLDKCQRENGFIYFQKIPTEA--PQLElKANygLVE 239
Cdd:pfam03097 262 QLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKDNDFIYHERVPSESslPPIK-PAS--MVK 326
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568911576  240 PVPFEFP--------------PMSAHwtpEALAAFD 261
Cdd:pfam03097 327 PIPPLELypfqigpdlfkklvPLSVH---EAASAYS 359
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
1-243 2.67e-174

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: 485.69  E-value: 2.67e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   1 MGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIPKLLTPAEKGRDLEARLIDAYIIQCQAEAQE 80
Cdd:cd09243  111 MLFNVALWYTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  81 VTIARAIELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRS 160
Cdd:cd09243  191 VTVARAIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRS 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 161 LQEAEKLYAEAEALCKEYGETKGPGPTAKPSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKANYGLVEP 240
Cdd:cd09243  271 LQESEKLYNKAEALCKEYAKTKGPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSP 350

                 ...
gi 568911576 241 VPF 243
Cdd:cd09243  351 EEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
1-277 2.84e-66

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: 211.83  E-value: 2.84e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576     1 MGFNVALWYTKYASRLAgkeNITEDEAKEVHRSLKIAAGIFKHLKESHIPKLltPAEKGRDLEARLIDAYIIQCQAEAQE 80
Cdd:smart01041 109 VLFNLGALYSQIAAEQN---RDTEEGLKEACKAFQQAAGVFNYLKENFLHAL--STEPSVDLSPETLSALSSLMLAQAQE 183
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576    81 VTIARAI--ELKHAPGLIAALAYDTASFYQKADHTLSSLEPAHS---AKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCG 155
Cdd:smart01041 184 CFFEKAIldGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVKGyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYG 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   156 EAIRSLQEAEKLYAEAEALCKeygeTKGPGPTAKPSGHLFFrkLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKAnY 235
Cdd:smart01041 264 EAIARLQEALERLKEAKKHLR----CKKLGKADKLQEDLSG--LKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKK-A 336
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 568911576   236 GLVEPVPF----EFPPMSAHWTPeaLAAFDLTKRPKDDSVKPKPEE 277
Cdd:smart01041 337 PLVKPPPFsevlKGPDLFAKLVP--MAVHEAASLYSEEKAKLVRAE 380
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
1-242 7.38e-55

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: 181.39  E-value: 7.38e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   1 MGFNVALWYtkyaSRLAGKENIT--EDEAKEVHRSLKIAAGIFKHLKESHIPklLTPAEKGRDLEARLIDAYIIQCQAEA 78
Cdd:cd09034  113 ILFNLAALA----SQLANEKLITgsEEDLKQAIKSLQKAAGYFEYLKEHVLP--LPPDELPVDLTEAVLSALSLIMLAQA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  79 QEVTIARAIELKHA-PGLIAALAYDTASFYQKADHTLSSLEPA----HSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDK 153
Cdd:cd09034  187 QECFLLKAEEDKKAkLSLLARLACEAAKYYEEALKCLSGVDLEtiknIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANK 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 154 CGEAIRSLQEAEKLYAEAEALCKEYGEtkgpgptakpSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIPTEAPQLELKA 233
Cdd:cd09034  267 IGEAIARLQAALELLKESERLCKSFLL----------DVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPEDPLPEIKG 336

                 ....*....
gi 568911576 234 NYGLVEPVP 242
Cdd:cd09034  337 ALLVKPPPL 345
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
3-261 5.13e-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: 119.22  E-value: 5.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576    3 FNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHipkLLTPAEkgrDLEARLIDAYIIQCQAEAQEV 81
Cdd:pfam03097 113 FNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENF---LHAPSP---DLSPETLKALSNLMLAQAQEC 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   82 TIARAIELKHAPGLIAALAYDTASFYQKAdHTLSSLEPAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSL 161
Cdd:pfam03097 183 FWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARL 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  162 QEAEKLYAEAEAlCKEYGETKGpgptakpsghlFFRKLGSLVKNTLDKCQRENGFIYFQKIPTEA--PQLElKANygLVE 239
Cdd:pfam03097 262 QLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKDNDFIYHERVPSESslPPIK-PAS--MVK 326
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568911576  240 PVPFEFP--------------PMSAHwtpEALAAFD 261
Cdd:pfam03097 327 PIPPLELypfqigpdlfkklvPLSVH---EAASAYS 359
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
12-244 2.97e-24

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: 100.16  E-value: 2.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  12 YASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHIPKL---LTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIE 88
Cdd:cd09247  121 AALRERASEVLPTEDFKEAATHLRRAAGVFEFLAHDELPRLrgaLSADERPPECTPSLALAMSLLCLAEAQAVTARKAEE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  89 LKHAPGLIAALAYDTASFYQKADHTLSSLE---PAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAE 165
Cdd:cd09247  201 KGTSPSLLAKLHYGATQFLEEAKNVLRSLAtdlKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREAL 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 166 KLYAEAEalckeygetkgpgPTAKPSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIP--TEAPQLELKAnygLVEPVPF 243
Cdd:cd09247  281 RNLKKKL-------------PGSDISSPVIFRDERAEVATLLQKYEKENEVIYFEKVPdiDELPLPEGKV---IVKPVPY 344

                 .
gi 568911576 244 E 244
Cdd:cd09247  345 K 345
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
3-226 6.54e-23

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: 96.57  E-value: 6.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   3 FNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHIPKLLTPaekgRDLEARLIDAYIIQCQAEAQEV 81
Cdd:cd09241  110 YNLGALY----SQLALSENRYTDEGlKRACSYFQASAGCFEYILQHLLPTLSPP----PDLDENTLKALESLMLAQAQEC 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  82 TIARAIELKHAPGLIAALAYDTASFYQKAdhtLSSLEPAHSAK--WRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIR 159
Cdd:cd09241  182 FWQKAISDGTKDSLIAKLAAQVSDYYQEA---LKYANKSDLIRsdWINHLKVKKHHFKAAAHYRMALVALEKSKYGEEVA 258
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911576 160 SLQeaeklyaEAEALCKE-YGETKGPGPTAKPSghlfFRKLGSLVKNTLDKCQRENGFIYFQKIPTEA 226
Cdd:cd09241  259 RLR-------VALAACKEaLKEARYGNKAVLED----LQGLKDIVKESLKRAERDNDLIYLQPVPPAS 315
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
3-226 7.65e-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: 88.11  E-value: 7.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   3 FNVALWYTKYAsrlagKENITEDEA--KEVHRSLKIAAGIFKHLKES--HIPklltpaekGRDLEARLIDAYIIQCQAEA 78
Cdd:cd09242  111 FNIGALLSQLA-----AEKYREDEDdlKEAITNLQQAAGCFQYINENflHAP--------SVDLQQENVKFLVKLMLAQA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  79 QEV----TIARAIELKHApGLIAALAYDTASFYQKADHTLSSLEPAHS----AKWRKYLHLKMCFYTAYAYCYHGQTLLA 150
Cdd:cd09242  178 QEIfllkLINGDDAQKKA-SLISKLASATANLYESCVEFLKEIQEKGIsygdPKWISLVQCKAHYYKSLAAYYHALALEA 256
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911576 151 SDKCGEAIRSLQEAEKLYAEAEALckeygeTKGPGPTAKPSGHL---FFRKLGSLVKNTLDKCQRENGFIYFQKIPTEA 226
Cdd:cd09242  257 AGKYGEAIAYLTQAESILKEANPQ------KLSLKASAGDAAYAlndDFKGQKDTVEEKLKELEKDNDFIYHDIVPSEV 329
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
3-243 4.99e-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: 80.03  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   3 FNVAlwytKYASRLAGKENI-TEDEAKEVHRSLKIAAGIFKHLKE---SHIPKLLTPaekgrDLEARLIDAYIIQCQAEA 78
Cdd:cd09240  123 FNIA----ALQSQIAAEQNLdTDEGLKLAAKLFQQAAGIFNHLKEtvlSALQQEPTP-----DLSPDTLSALSALMLAQA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  79 QEVTIARAIELKHAPGLIAALAYDTASFYQKADHTLSslEPAHSAKWRK----YLHLKMCFYTAYAYcYHgQTLLA--SD 152
Cdd:cd09240  194 QEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQ--REDVRSLLPKdwipVLAGKQAYFHALAE-YH-QSLVAkaQK 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 153 KCGEAIRSLQEAEKLYAEAEALCKEYgetkgpgptakpsghLFFRKLGSLVKNTLDKCQRENGFIYFQKIPtEAPQLEL- 231
Cdd:cd09240  270 KFGEEIARLQHALELIKTAQSRAGEY---------------VDVKDFAAKISRALTAAKKDNDFIYHDRVP-DVKSLPPi 333
                        250
                 ....*....|...
gi 568911576 232 -KANygLVEPVPF 243
Cdd:cd09240  334 gKAA--LAKPTPV 344
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
3-243 1.42e-12

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: 67.04  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576   3 FNV-ALWytkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHIPKLLTPAEKgrDLEARLIDAYIIQCQAEAQE 80
Cdd:cd09246  115 FNLgALS-----SQLGLQQDRTTAEGiKQACHAFQAAAGAFAHLRDKVSGKTGGFRTP--DLTAECLGMLESLMLAQAQE 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  81 VTIARAIELKHAPGLIAALAYDTASFYQKADHTLSS--LEPAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAI 158
Cdd:cd09246  188 CFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSppLKGHFDKSWVAHVQLKAAYFRAEALYRAAKDLHEKEDIGEEI 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 159 RSLQEAEKLYAEAealCKEYGETKGpgptakPSGHLFFRKLGSLVKNTLDKCQRENGFIYFQKIPT--EAPQLELKAnyg 236
Cdd:cd09246  268 ARLRAASDALAEA---RKQAKGVNG------DELIEAVSELEQVINELLERAEKENDCVYLDRVPApsDLPPLGAAS--- 335

                 ....*..
gi 568911576 237 LVEPVPF 243
Cdd:cd09246  336 MVKPAAP 342
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
14-245 1.44e-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: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  14 SRLAGKEN-ITEDEAKEVHRSLKIAAGIFKHLKESHipkllTPAEKGRDLEARLIDAYIIQCQAEAQEVTIARAIELKHA 92
Cdd:cd09239  125 SQLGASDKrDSEEGMKVACTHFQCAAWAFAYLREHY-----PQVYGAVDMSSQLLSFNYSLMLAQAQECLLEKSLLDNRK 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576  93 PGLIAALAYDTASFYQKADHTLSSLE-------PAHSAKWRKYLHLKMCFYTAYAYCYHGQTLLASDKCGEAIRSLQEAE 165
Cdd:cd09239  200 SHITAKVSAQVVEYYKEALRALENWEsnskiilGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVAYYQLAN 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911576 166 KLYAEAEALCKEYGETKGPGPTAkpsghlffRKLGSLVKNTLDKCQRENGFIYFQKIPtEAPQLELKANYGLVEPVPFEF 245
Cdd:cd09239  280 DKLEEAIKNAKGQPDTVNLQEAL--------SFTMDVIGGKRNSAKKENDFIYHEAVP-KLDTLQAVKGANLVKGIPFSP 350
 
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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