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Conserved domains on  [gi|42572093|ref|NP_974137|]
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Endosomal targeting BRO1-like domain-containing protein [Arabidopsis thaliana]

Protein Classification

BRO1 domain-containing protein( domain architecture ID 10173280)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 17-398 5.00e-98

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: 296.57  E-value: 5.00e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  17 KPTSIGDVSVYVPGlRIPKPVEFSQslgDQLPKTLVERLTALRTRIVVManqegptitrtrrktQHGGSTLADLHHALED 96
Cdd:cd09034   7 KKTKEVDVKVPLSK-FIPKNYGELE---ATAVEDLIEKLSKLRNNIVTE---------------QNNDTTCENLLEALKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  97 YIPVLLGLTK--DGSHLQFKVQFNWVNQEDEEEETAMSnVWYEILSVLHLMAMLQMSQANLLLLPRgssdgyhpkiSEEN 174
Cdd:cd09034  68 YLPYLLGLEKklPFQKLRDNVEFTWTDSFDTKKESATS-LRYELLSILFNLAALASQLANEKLITG----------SEED 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 175 RRASIDIFLKAAGYLDCAVKHVLPHFSTEqrrsLPIDLAEGALRALCLQALGQGVDIQLGMAIDSAKATLAVKRRLSCEM 254
Cdd:cd09034 137 LKQAIKSLQKAAGYFEYLKEHVLPLPPDE----LPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAKLSLLARLACEA 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 255 VKYWQQAQDNL--MNLPLANGWGEKHMLFVKWKYVEAKAAAYYYHGLILDEGNtekSHGMAVAALQAADECLKESKKASE 332
Cdd:cd09034 213 AKYYEEALKCLsgVDLETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEAN---KIGEAIARLQAALELLKESERLCK 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572093 333 AFNTssptsrtpSLFGTMKYLSEKIPKETSSKVRINRDLYSYEKIMETapTLPDFALALKPDEYQL 398
Cdd:cd09034 290 SFLL--------DVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPED--PLPEIKGALLVKPPPL 345
 
Name Accession Description Interval E-value
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 17-398 5.00e-98

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: 296.57  E-value: 5.00e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  17 KPTSIGDVSVYVPGlRIPKPVEFSQslgDQLPKTLVERLTALRTRIVVManqegptitrtrrktQHGGSTLADLHHALED 96
Cdd:cd09034   7 KKTKEVDVKVPLSK-FIPKNYGELE---ATAVEDLIEKLSKLRNNIVTE---------------QNNDTTCENLLEALKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  97 YIPVLLGLTK--DGSHLQFKVQFNWVNQEDEEEETAMSnVWYEILSVLHLMAMLQMSQANLLLLPRgssdgyhpkiSEEN 174
Cdd:cd09034  68 YLPYLLGLEKklPFQKLRDNVEFTWTDSFDTKKESATS-LRYELLSILFNLAALASQLANEKLITG----------SEED 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 175 RRASIDIFLKAAGYLDCAVKHVLPHFSTEqrrsLPIDLAEGALRALCLQALGQGVDIQLGMAIDSAKATLAVKRRLSCEM 254
Cdd:cd09034 137 LKQAIKSLQKAAGYFEYLKEHVLPLPPDE----LPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAKLSLLARLACEA 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 255 VKYWQQAQDNL--MNLPLANGWGEKHMLFVKWKYVEAKAAAYYYHGLILDEGNtekSHGMAVAALQAADECLKESKKASE 332
Cdd:cd09034 213 AKYYEEALKCLsgVDLETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEAN---KIGEAIARLQAALELLKESERLCK 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572093 333 AFNTssptsrtpSLFGTMKYLSEKIPKETSSKVRINRDLYSYEKIMETapTLPDFALALKPDEYQL 398
Cdd:cd09034 290 SFLL--------DVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPED--PLPEIKGALLVKPPPL 345
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 26-415 1.83e-59

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: 198.34  E-value: 1.83e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093     26 VYVPGLRIPKPVEFSQSLGDQLPKTLVERLTALRtrivvmanQEGPTITRTRRKTQHGGSTLADLHHALEdYIPVLLGLT 105
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSEDSSSYE--------DEIAELNRLRQAARTPSRDESGLELLLK-YYGQLEALE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    106 K--DGSHLQFKVQFNWVNQEDEEEETAMSNVWYEILSVLHLMAMLQMSQANllllprgssdgYHPKISEENRRASIDIFL 183
Cdd:smart01041  72 LrfPPPEGQLKLSFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAA-----------EQNRDTEEGLKEACKAFQ 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    184 KAAGYLDCAVKHVLPHFSTEQRRslpiDLAEGALRALCLQALGQGVDIQLGMAI-DSAKATLAVKRRLSCEMVKYWQQAQ 262
Cdd:smart01041 141 QAAGVFNYLKENFLHALSTEPSV----DLSPETLSALSSLMLAQAQECFFEKAIlDGMKNKDSLIAKLAAQAAEYYEEAL 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    263 DNLMNL-PLANGWGEKHMLFVKWKYVEAKAAAYYYHGLILDEGNtekSHGMAVAALQAADECLKESKKASEafntSSPTS 341
Cdd:smart01041 217 KALQTSePVKGYIPKSWIKLVQVKAHHFKALAHYYQALDLEEAN---KYGEAIARLQEALERLKEAKKHLR----CKKLG 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    342 RTPSLFGTMKYLSEKIPKETSSKVRINRDLYsYEKI-------------------METAPTLPDFALALKPDEYQLPSVD 402
Cdd:smart01041 290 KADKLQEDLSGLKDVVEEKLKEAEKDNDFIY-HERVpdivslppikkaplvkpppFSEVLKGPDLFAKLVPMAVHEAASL 368

                          410
                   ....*....|...
gi 42572093    403 ASWSEASLRTKNT 415
Cdd:smart01041 369 YSEEKAKLVRAEI 381
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 110-370 1.98e-08

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: 55.66  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093   110 HLQFKVQFNWVNQED-EEEETAMSNVWYEILSVLHLMAMLQMSQAnlLLLPRGSSDGYhpkiseenrRASIDIFLKAAGY 188
Cdd:pfam03097  79 DIQIGIEFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALYSQLA--ASQNRSTDEGL---------KRACKYFQQAAGC 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093   189 LdcavKHVLPHFSteqrRSLPIDLAEGALRALCLQALGQGVDIQLGMAI-DSAKATLAVKrrLSCEMVKYWQQAQDNLMN 267
Cdd:pfam03097 148 F----QYLKENFL----HAPSPDLSPETLKALSNLMLAQAQECFWEKAInDNKKDSLIAK--LAAQVSELYEEALEALKL 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093   268 LPLAN-GWgeKHMLFVKWKYVeaKAAAYYYHGLILDEgntEKSHGMAVAALQAADECLKESKKAseafntssptSRTPSL 346
Cdd:pfam03097 218 SGLIDkEW--ISHVQAKAHHF--KALAQYRQALDDEE---AKKYGEEIARLQLALSLLKEALKS----------DRYKKV 280

                         250       260
                  ....*....|....*....|....
gi 42572093   347 FGTMKYLSEKIpkeTSSKVRINRD 370
Cdd:pfam03097 281 LEDLKGLLDVV---EEKLKRAEKD 301
 
Name Accession Description Interval E-value
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 17-398 5.00e-98

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: 296.57  E-value: 5.00e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  17 KPTSIGDVSVYVPGlRIPKPVEFSQslgDQLPKTLVERLTALRTRIVVManqegptitrtrrktQHGGSTLADLHHALED 96
Cdd:cd09034   7 KKTKEVDVKVPLSK-FIPKNYGELE---ATAVEDLIEKLSKLRNNIVTE---------------QNNDTTCENLLEALKE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  97 YIPVLLGLTK--DGSHLQFKVQFNWVNQEDEEEETAMSnVWYEILSVLHLMAMLQMSQANLLLLPRgssdgyhpkiSEEN 174
Cdd:cd09034  68 YLPYLLGLEKklPFQKLRDNVEFTWTDSFDTKKESATS-LRYELLSILFNLAALASQLANEKLITG----------SEED 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 175 RRASIDIFLKAAGYLDCAVKHVLPHFSTEqrrsLPIDLAEGALRALCLQALGQGVDIQLGMAIDSAKATLAVKRRLSCEM 254
Cdd:cd09034 137 LKQAIKSLQKAAGYFEYLKEHVLPLPPDE----LPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAKLSLLARLACEA 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 255 VKYWQQAQDNL--MNLPLANGWGEKHMLFVKWKYVEAKAAAYYYHGLILDEGNtekSHGMAVAALQAADECLKESKKASE 332
Cdd:cd09034 213 AKYYEEALKCLsgVDLETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEAN---KIGEAIARLQAALELLKESERLCK 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572093 333 AFNTssptsrtpSLFGTMKYLSEKIPKETSSKVRINRDLYSYEKIMETapTLPDFALALKPDEYQL 398
Cdd:cd09034 290 SFLL--------DVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPED--PLPEIKGALLVKPPPL 345
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 26-415 1.83e-59

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: 198.34  E-value: 1.83e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093     26 VYVPGLRIPKPVEFSQSLGDQLPKTLVERLTALRtrivvmanQEGPTITRTRRKTQHGGSTLADLHHALEdYIPVLLGLT 105
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSEDSSSYE--------DEIAELNRLRQAARTPSRDESGLELLLK-YYGQLEALE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    106 K--DGSHLQFKVQFNWVNQEDEEEETAMSNVWYEILSVLHLMAMLQMSQANllllprgssdgYHPKISEENRRASIDIFL 183
Cdd:smart01041  72 LrfPPPEGQLKLSFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAA-----------EQNRDTEEGLKEACKAFQ 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    184 KAAGYLDCAVKHVLPHFSTEQRRslpiDLAEGALRALCLQALGQGVDIQLGMAI-DSAKATLAVKRRLSCEMVKYWQQAQ 262
Cdd:smart01041 141 QAAGVFNYLKENFLHALSTEPSV----DLSPETLSALSSLMLAQAQECFFEKAIlDGMKNKDSLIAKLAAQAAEYYEEAL 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    263 DNLMNL-PLANGWGEKHMLFVKWKYVEAKAAAYYYHGLILDEGNtekSHGMAVAALQAADECLKESKKASEafntSSPTS 341
Cdd:smart01041 217 KALQTSePVKGYIPKSWIKLVQVKAHHFKALAHYYQALDLEEAN---KYGEAIARLQEALERLKEAKKHLR----CKKLG 289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093    342 RTPSLFGTMKYLSEKIPKETSSKVRINRDLYsYEKI-------------------METAPTLPDFALALKPDEYQLPSVD 402
Cdd:smart01041 290 KADKLQEDLSGLKDVVEEKLKEAEKDNDFIY-HERVpdivslppikkaplvkpppFSEVLKGPDLFAKLVPMAVHEAASL 368

                          410
                   ....*....|...
gi 42572093    403 ASWSEASLRTKNT 415
Cdd:smart01041 369 YSEEKAKLVRAEI 381
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 110-370 1.98e-08

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: 55.66  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093   110 HLQFKVQFNWVNQED-EEEETAMSNVWYEILSVLHLMAMLQMSQAnlLLLPRGSSDGYhpkiseenrRASIDIFLKAAGY 188
Cdd:pfam03097  79 DIQIGIEFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALYSQLA--ASQNRSTDEGL---------KRACKYFQQAAGC 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093   189 LdcavKHVLPHFSteqrRSLPIDLAEGALRALCLQALGQGVDIQLGMAI-DSAKATLAVKrrLSCEMVKYWQQAQDNLMN 267
Cdd:pfam03097 148 F----QYLKENFL----HAPSPDLSPETLKALSNLMLAQAQECFWEKAInDNKKDSLIAK--LAAQVSELYEEALEALKL 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093   268 LPLAN-GWgeKHMLFVKWKYVeaKAAAYYYHGLILDEgntEKSHGMAVAALQAADECLKESKKAseafntssptSRTPSL 346
Cdd:pfam03097 218 SGLIDkEW--ISHVQAKAHHF--KALAQYRQALDDEE---AKKYGEEIARLQLALSLLKEALKS----------DRYKKV 280

                         250       260
                  ....*....|....*....|....
gi 42572093   347 FGTMKYLSEKIpkeTSSKVRINRD 370
Cdd:pfam03097 281 LEDLKGLLDVV---EEKLKRAEKD 301
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 112-403 1.19e-07

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: 53.05  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 112 QFKVQFNWVNQEDEEEETAMSNVWYEILSVLHLMAML--QMSQANLlllpRGSSDGYhpkiseenrRASIDIFLKAAGYL 189
Cdd:cd09242  80 ELKVDFTWYDAFYKSKKVKQHSLAFEKASVLFNIGALlsQLAAEKY----REDEDDL---------KEAITNLQQAAGCF 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 190 DcavkhvlphFSTEQRRSLP-IDLAEGALRALCLQALGQGVDIQLGMAID----SAKATLAVKrrLSCEMVKYWQQAQDN 264
Cdd:cd09242 147 Q---------YINENFLHAPsVDLQQENVKFLVKLMLAQAQEIFLLKLINgddaQKKASLISK--LASATANLYESCVEF 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 265 LMNLPLAN-GWGEKhmlfvKWKY-VEAKAAAY-----YYHGLILDEGNtekSHGMAVAALQAADECLKESKKASEAFnTS 337
Cdd:cd09242 216 LKEIQEKGiSYGDP-----KWISlVQCKAHYYkslaaYYHALALEAAG---KYGEAIAYLTQAESILKEANPQKLSL-KA 286

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572093 338 SPTSRTPSLFGTMKYLSEKIPKETSSKVRINrDLYSYEKImetaptlpdfalalkPDEYQLPSVDA 403
Cdd:cd09242 287 SAGDAAYALNDDFKGQKDTVEEKLKELEKDN-DFIYHDIV---------------PSEVTLPSIKP 336
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 166-337 1.04e-05

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: 47.26  E-value: 1.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 166 YHPKISEENRRASIDI------FLKAAGYLDCAVKHVLPhfsteqRRSLPIDLAEG---ALRALCLqALGQGVDIQlgMA 236
Cdd:cd09241 116 YSQLALSENRYTDEGLkracsyFQASAGCFEYILQHLLP------TLSPPPDLDENtlkALESLML-AQAQECFWQ--KA 186

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 237 I-DSAKATLAVKrrLSCEMVKYWQQAQDNLMNLPLA-NGWgEKHMlfvKWKYVEAKAAAYYYHGLILDEGNtekSHGMAV 314
Cdd:cd09241 187 IsDGTKDSLIAK--LAAQVSDYYQEALKYANKSDLIrSDW-INHL---KVKKHHFKAAAHYRMALVALEKS---KYGEEV 257

                       170       180
                ....*....|....*....|...
gi 42572093 315 AALQAADECLKESKKASEAFNTS 337
Cdd:cd09241 258 ARLRVALAACKEALKEARYGNKA 280
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 32-397 3.61e-05

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: 45.46  E-value: 3.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  32 RIPKP----VEFSQSLGDQLPKTLVERL-TALRTRIVVMANQEGPTITR--TRRKTQhggstlaDLHHaLEDYIPVLLGL 104
Cdd:cd09247   2 DFAKPktkkIVFEKTFQARDSLTLEQLKeLSLRRRAIIESINGSPFIALaiAREKAQ-------YLPY-LEGYLPALENL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 105 TK--DGSHLQFKVQFNWVNQEDEEEETA---MSNVWYEILSVLHLMAMLQMSQAnLLLLPRgssdgyhpkiseENRRASI 179
Cdd:cd09247  74 VNhrDKVQLNEQLSFRWTSGLGSSKGPKafqSDSLRFELGMVLFLYGAALRERA-SEVLPT------------EDFKEAA 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 180 DIFLKAAGYLDCAVKHVLPHFSTEQRR-SLPIDLAEG---ALRALCLqALGQGVDIQLGMAIDSAKATLAvkrRLSCEMV 255
Cdd:cd09247 141 THLRRAAGVFEFLAHDELPRLRGALSAdERPPECTPSlalAMSLLCL-AEAQAVTARKAEEKGTSPSLLA---KLHYGAT 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 256 KYWQQAQDNLMNLplANGWGEKHMLFvkWKYVEA-----KAAAYYYHGLILDEgntEKSHGMAVAALQAADECLKESKKA 330
Cdd:cd09247 217 QFLEEAKNVLRSL--ATDLKDLDPRF--LRFISScialhEARSQLYLARRLKE---AGHIGVAVGVLREALRNLKKKLPG 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42572093 331 SEafntssptSRTPSLFGTMkylSEKIPKETSSKVRINRDLYsYEKI--METAPTLPDfALALKPDEYQ 397
Cdd:cd09247 290 SD--------ISSPVIFRDE---RAEVATLLQKYEKENEVIY-FEKVpdIDELPLPEG-KVIVKPVPYK 345
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
 36-227 2.17e-04

Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; This family contains the Bro1-like domain of Ustilago maydis Rim23 (also known as PalC), and related 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, 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. Through its Bro1-like domain, Rim23 allows the interaction between the endosomal and plasma membrane complexes. Bro1-like domains are boomerang-shape, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Intermediates in the Rim101 pathway may play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185768  Cd Length: 413  Bit Score: 43.16  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093  36 PVEFSQSLGDQLPKTLVERLTALRT--RIVVMANQEGPTitrtrrktQHGGSTLADLHHALEDYIPVLLGLTKDGSH--L 111
Cdd:cd09245  11 SISFSDFFNSDSYPSLPLNATTARAvlRAALKAHKRTPP--------GSQASNLLTVVKALEEYLPYLLAIDACLSHdeL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572093 112 QFKVQ--FNW-----VNQEDEEEETAMSNVWYEILSVLHLMAMLQMSQANLLL--LPRGSSDGYHPKISEENRRASI--- 179
Cdd:cd09245  83 ILKSEptFEWrttlsSTSGRESPRLPLPGLHYELAFVLLTYAYALSNLARSILapLGAYETDRSISDASRKQRDERLkaa 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42572093 180 -DIFLKAAGYLDCAVKHVLPHFSTEQRR-SLPIDLAEGALRALCLQALGQ 227
Cdd:cd09245 163 tKLLCKAAGIFDYLATRVLPQWESNRGGaPPPPDLSPEVLSALSSLALAE 212
 
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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