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Conserved domains on  [gi|19115164|ref|NP_594252|]
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vacuolar protein-sorting protein [Schizosaccharomyces pombe]

Protein Classification

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 ...
 8-345 2.57e-128

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 cd09242:

Pssm-ID: 472700  Cd Length: 348  Bit Score: 386.25  E-value: 2.57e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   8 FFYLNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNG 86
Cdd:cd09242   1 LISLPLKDTEEVDWKKPLSSYLKRSYGsSTFYYEEEIAEFDRLRQDANGVLADETGRDLLYKYYGQLELLELRFPFNNKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  87 INISFEWSDILDPdADFVKQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRESFIHAPG 166
Cdd:cd09242  81 LKVDFTWYDAFYK-SKKVKQHSLAFEKASVLFNIGALLSQLAAEKYRE-DEDDLKEAITNLQQAAGCFQYINENFLHAPS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 167 RDLDSNFLLGIYNLFLGQAQECVLGHMSFSaSDSNMNYSLAAKIASSAATLYDSCVHAFESMEPAC----NPNFIRLASA 242
Cdd:cd09242 159 VDLQQENVKFLVKLMLAQAQEIFLLKLING-DDAQKKASLISKLASATANLYESCVEFLKEIQEKGisygDPKWISLVQC 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 243 KKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDfihkpSLSDYPQTISTFIKSSLSHLLKT 322
Cdd:cd09242 238 KAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPQKLSLKASAG-----DAAYALNDDFKGQKDTVEEKLKE 312

                       330       340
                ....*....|....*....|...
gi 19115164 323 AEKDNDFVFHDLVVKEVELPKIS 345
Cdd:cd09242 313 LEKDNDFIYHDIVPSEVTLPSIK 335
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 382-745 8.87e-110

Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.


:

Pssm-ID: 185750 [Multi-domain]  Cd Length: 356  Bit Score: 338.50  E-value: 8.87e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRAEQAEVERQNTQMATVFASLDLSRLQEITHSDSKTNFipkELIEARSQLISFNPTFKIHE 461
Cdd:cd09237   1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLKERFEGEN---ELMEIVSGLKSSSVDSQLEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 462 LFAKSTKLKQIIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQQYALVKDD 541
Cdd:cd09237  78 LRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPVKED 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 542 VETLCNSSKISALLESsISSTDNSGQSLLDIPIEQEEQErdMKIQLDLLEELQSRVQKLVPERQTTLQALQQKCLQDDIS 621
Cdd:cd09237 158 IALLLNGGSLWEELFG-FSSSGSPEPSLLDLDDSQNEQT--VLKQIKQLEELLEDLNLIKEERQRVLKDLKQKIHNDDIS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 622 ESLMQNSKRKDSalDTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVTQKLKQNPEFLRKMEVYNNQFSKNKELCS 701
Cdd:cd09237 235 DILILNSKSKSE--IEKQLFPEELEKFKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQSKEKSKQKLRKEFFE 312

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 19115164 702 NLLSSSLTAKAISEGVSKGLEYYKTVEQRLAEINKTLGEQLLLR 745
Cdd:cd09237 313 KLKKAYNSFKKFSAGLPKGLEFYDDLLKMAKDLAKNVQAFVNQR 356
 
Name Accession Description Interval E-value
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 8-345 2.57e-128

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: 386.25  E-value: 2.57e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   8 FFYLNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNG 86
Cdd:cd09242   1 LISLPLKDTEEVDWKKPLSSYLKRSYGsSTFYYEEEIAEFDRLRQDANGVLADETGRDLLYKYYGQLELLELRFPFNNKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  87 INISFEWSDILDPdADFVKQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRESFIHAPG 166
Cdd:cd09242  81 LKVDFTWYDAFYK-SKKVKQHSLAFEKASVLFNIGALLSQLAAEKYRE-DEDDLKEAITNLQQAAGCFQYINENFLHAPS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 167 RDLDSNFLLGIYNLFLGQAQECVLGHMSFSaSDSNMNYSLAAKIASSAATLYDSCVHAFESMEPAC----NPNFIRLASA 242
Cdd:cd09242 159 VDLQQENVKFLVKLMLAQAQEIFLLKLING-DDAQKKASLISKLASATANLYESCVEFLKEIQEKGisygDPKWISLVQC 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 243 KKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDfihkpSLSDYPQTISTFIKSSLSHLLKT 322
Cdd:cd09242 238 KAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPQKLSLKASAG-----DAAYALNDDFKGQKDTVEEKLKE 312

                       330       340
                ....*....|....*....|...
gi 19115164 323 AEKDNDFVFHDLVVKEVELPKIS 345
Cdd:cd09242 313 LEKDNDFIYHDIVPSEVTLPSIK 335
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 382-745 8.87e-110

Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.


Pssm-ID: 185750 [Multi-domain]  Cd Length: 356  Bit Score: 338.50  E-value: 8.87e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRAEQAEVERQNTQMATVFASLDLSRLQEITHSDSKTNFipkELIEARSQLISFNPTFKIHE 461
Cdd:cd09237   1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLKERFEGEN---ELMEIVSGLKSSSVDSQLEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 462 LFAKSTKLKQIIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQQYALVKDD 541
Cdd:cd09237  78 LRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPVKED 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 542 VETLCNSSKISALLESsISSTDNSGQSLLDIPIEQEEQErdMKIQLDLLEELQSRVQKLVPERQTTLQALQQKCLQDDIS 621
Cdd:cd09237 158 IALLLNGGSLWEELFG-FSSSGSPEPSLLDLDDSQNEQT--VLKQIKQLEELLEDLNLIKEERQRVLKDLKQKIHNDDIS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 622 ESLMQNSKRKDSalDTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVTQKLKQNPEFLRKMEVYNNQFSKNKELCS 701
Cdd:cd09237 235 DILILNSKSKSE--IEKQLFPEELEKFKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQSKEKSKQKLRKEFFE 312

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 19115164 702 NLLSSSLTAKAISEGVSKGLEYYKTVEQRLAEINKTLGEQLLLR 745
Cdd:cd09237 313 KLKKAYNSFKKFSAGLPKGLEFYDDLLKMAKDLAKNVQAFVNQR 356
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 8-403 1.48e-94

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: 299.65  E-value: 1.48e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164      8 FFYLNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNG 86
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSeDSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPPPEGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164     87 INISFEWSDILDPDADfVKQSSLAFEKASVLFNLVSLLSRMAANHaSAYTVDDYKAAANCLQCASGIAKLLRESFIHAP- 165
Cdd:smart01041  81 LKLSFTWYDSLDTGVP-STQSSLAFEKASVLFNLGALYSQIAAEQ-NRDTEEGLKEACKAFQQAAGVFNYLKENFLHALs 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    166 ---GRDLDSNFLLGIYNLFLGQAQECVLGHMSFsaSDSNMNYSLAAKIASSAATLYDSCVHAFESMEPA---CNPNFIRL 239
Cdd:smart01041 159 tepSVDLSPETLSALSSLMLAQAQECFFEKAIL--DGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVkgyIPKSWIKL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    240 ASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLStdfiHKPSLSDYPQtistFIKSSLSHL 319
Cdd:smart01041 237 VQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLRCKKLG----KADKLQEDLS----GLKDVVEEK 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    320 LKTAEKDNDFVFHDLVVKEVELPKISPLQALPPLPLEKLYgsqdgfetakkiVGDDLFKAFVPSAVTTASSLYSEETAKV 399
Cdd:smart01041 309 LKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSEVL------------KGPDLFAKLVPMAVHEAASLYSEEKAKL 376


                   ....
gi 19115164    400 FRAE 403
Cdd:smart01041 377 VRAE 380
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 8-398 1.34e-93

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: 296.80  E-value: 1.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164     8 FFYLNKKETKHSDWVEPFTTFVSRIYG--NSVDVEDQIKAFNTLRENAAD-VDDTVAGKDILYSYYGQLDYLSFRFPTGg 84
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTYGsqDPSSFEDDLAELNKLRQDAVRgANEDESGLDLLYKYYAQLELLELRFPID- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    85 NGINISFEWSDILDPDADFVKQSSLAFEKASVLFNLVSLLSRMAANHaSAYTVDDYKAAANCLQCASGIAKLLRESFIHA 164
Cdd:pfam03097  80 IQIGIEFTWYDAFGTSSKKVSQSSLAFEKASVLFNIAALYSQLAASQ-NRSTDEGLKRACKYFQQAAGCFQYLKENFLHA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   165 PGRDLDSNFLLGIYNLFLGQAQECVLghmsFSASDSNMNYSLAAKIASSAATLYDSCVHAFESMEPAcNPNFIRLASAKK 244
Cdd:pfam03097 159 PSPDLSPETLKALSNLMLAQAQECFW----EKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLI-DKEWISHVQAKA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   245 AALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDFihkpslsdypqtisTFIKSSLSHLLKTAE 324
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALKSDRYKKVLEDL--------------KGLLDVVEEKLKRAE 299

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115164   325 KDNDFVFHDLVVKEVELPKISPLQALPPLPLEKLYGSQdgfetakkiVGDDLFKAFVPSAVTTASSLYSEETAK 398
Cdd:pfam03097 300 KDNDFIYHERVPSESSLPPIKPASMVKPIPPLELYPFQ---------IGPDLFKKLVPLSVHEAASAYSERKAK 364
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 439-748 3.46e-41

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 152.77  E-value: 3.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   439 IPKELIEARSQLISFNPTFKIHELFAKSTKLKQ----IIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSEL 514
Cdd:pfam13949   2 LPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQrnreILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   515 NNYLKTLAEASATDSAISQQYALVKDDVETLCNS-SKISALLESSISSTDNSgqslldipieqeeqerDMKIQLDLLEEL 593
Cdd:pfam13949  82 RKYREILEQASESDSQVRSKFREHEEDLELLSGPdEDLEAFLPSSRRAKNSP----------------SVEEQVAKLREL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   594 QSRVQKLVPERQTTLQALQQKCLQDDISESLMQNSKRKDSALDTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVT 673
Cdd:pfam13949 146 LNKLNELKREREQLLKDLKEKARNDDISPKLLLEKARLIAPNQEEQLFEEELEKYDPLQNRLEQNLHKQEELLKEITEAN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   674 QKLKQNPEFL--------RKMEVYNNQFSKNKElcsnllsssltakaISEGVSKGLEYYKTVEQRLAEINKTLGEQLLLR 745
Cdd:pfam13949 226 NEFLQDKRVDsekqrqreEALQKLENAYDKYKE--------------LVSNLQEGLKFYNDLTEILEKLLKKVKDFVNAR 291


                  ...
gi 19115164   746 RKQ 748
Cdd:pfam13949 292 RSE 294
 
Name Accession Description Interval E-value
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 8-345 2.57e-128

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: 386.25  E-value: 2.57e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   8 FFYLNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNG 86
Cdd:cd09242   1 LISLPLKDTEEVDWKKPLSSYLKRSYGsSTFYYEEEIAEFDRLRQDANGVLADETGRDLLYKYYGQLELLELRFPFNNKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  87 INISFEWSDILDPdADFVKQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRESFIHAPG 166
Cdd:cd09242  81 LKVDFTWYDAFYK-SKKVKQHSLAFEKASVLFNIGALLSQLAAEKYRE-DEDDLKEAITNLQQAAGCFQYINENFLHAPS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 167 RDLDSNFLLGIYNLFLGQAQECVLGHMSFSaSDSNMNYSLAAKIASSAATLYDSCVHAFESMEPAC----NPNFIRLASA 242
Cdd:cd09242 159 VDLQQENVKFLVKLMLAQAQEIFLLKLING-DDAQKKASLISKLASATANLYESCVEFLKEIQEKGisygDPKWISLVQC 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 243 KKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDfihkpSLSDYPQTISTFIKSSLSHLLKT 322
Cdd:cd09242 238 KAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPQKLSLKASAG-----DAAYALNDDFKGQKDTVEEKLKE 312

                       330       340
                ....*....|....*....|...
gi 19115164 323 AEKDNDFVFHDLVVKEVELPKIS 345
Cdd:cd09242 313 LEKDNDFIYHDIVPSEVTLPSIK 335
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 382-745 8.87e-110

Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.


Pssm-ID: 185750 [Multi-domain]  Cd Length: 356  Bit Score: 338.50  E-value: 8.87e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRAEQAEVERQNTQMATVFASLDLSRLQEITHSDSKTNFipkELIEARSQLISFNPTFKIHE 461
Cdd:cd09237   1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLKERFEGEN---ELMEIVSGLKSSSVDSQLEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 462 LFAKSTKLKQIIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQQYALVKDD 541
Cdd:cd09237  78 LRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPVKED 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 542 VETLCNSSKISALLESsISSTDNSGQSLLDIPIEQEEQErdMKIQLDLLEELQSRVQKLVPERQTTLQALQQKCLQDDIS 621
Cdd:cd09237 158 IALLLNGGSLWEELFG-FSSSGSPEPSLLDLDDSQNEQT--VLKQIKQLEELLEDLNLIKEERQRVLKDLKQKIHNDDIS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 622 ESLMQNSKRKDSalDTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVTQKLKQNPEFLRKMEVYNNQFSKNKELCS 701
Cdd:cd09237 235 DILILNSKSKSE--IEKQLFPEELEKFKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQSKEKSKQKLRKEFFE 312

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 19115164 702 NLLSSSLTAKAISEGVSKGLEYYKTVEQRLAEINKTLGEQLLLR 745
Cdd:cd09237 313 KLKKAYNSFKKFSAGLPKGLEFYDDLLKMAKDLAKNVQAFVNQR 356
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 8-403 1.48e-94

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: 299.65  E-value: 1.48e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164      8 FFYLNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNG 86
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSeDSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPPPEGQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164     87 INISFEWSDILDPDADfVKQSSLAFEKASVLFNLVSLLSRMAANHaSAYTVDDYKAAANCLQCASGIAKLLRESFIHAP- 165
Cdd:smart01041  81 LKLSFTWYDSLDTGVP-STQSSLAFEKASVLFNLGALYSQIAAEQ-NRDTEEGLKEACKAFQQAAGVFNYLKENFLHALs 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    166 ---GRDLDSNFLLGIYNLFLGQAQECVLGHMSFsaSDSNMNYSLAAKIASSAATLYDSCVHAFESMEPA---CNPNFIRL 239
Cdd:smart01041 159 tepSVDLSPETLSALSSLMLAQAQECFFEKAIL--DGMKNKDSLIAKLAAQAAEYYEEALKALQTSEPVkgyIPKSWIKL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    240 ASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLStdfiHKPSLSDYPQtistFIKSSLSHL 319
Cdd:smart01041 237 VQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLRCKKLG----KADKLQEDLS----GLKDVVEEK 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    320 LKTAEKDNDFVFHDLVVKEVELPKISPLQALPPLPLEKLYgsqdgfetakkiVGDDLFKAFVPSAVTTASSLYSEETAKV 399
Cdd:smart01041 309 LKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSEVL------------KGPDLFAKLVPMAVHEAASLYSEEKAKL 376


                   ....
gi 19115164    400 FRAE 403
Cdd:smart01041 377 VRAE 380
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 8-398 1.34e-93

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: 296.80  E-value: 1.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164     8 FFYLNKKETKHSDWVEPFTTFVSRIYG--NSVDVEDQIKAFNTLRENAAD-VDDTVAGKDILYSYYGQLDYLSFRFPTGg 84
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTYGsqDPSSFEDDLAELNKLRQDAVRgANEDESGLDLLYKYYAQLELLELRFPID- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164    85 NGINISFEWSDILDPDADFVKQSSLAFEKASVLFNLVSLLSRMAANHaSAYTVDDYKAAANCLQCASGIAKLLRESFIHA 164
Cdd:pfam03097  80 IQIGIEFTWYDAFGTSSKKVSQSSLAFEKASVLFNIAALYSQLAASQ-NRSTDEGLKRACKYFQQAAGCFQYLKENFLHA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   165 PGRDLDSNFLLGIYNLFLGQAQECVLghmsFSASDSNMNYSLAAKIASSAATLYDSCVHAFESMEPAcNPNFIRLASAKK 244
Cdd:pfam03097 159 PSPDLSPETLKALSNLMLAQAQECFW----EKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLI-DKEWISHVQAKA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   245 AALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDFihkpslsdypqtisTFIKSSLSHLLKTAE 324
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALKSDRYKKVLEDL--------------KGLLDVVEEKLKRAE 299

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115164   325 KDNDFVFHDLVVKEVELPKISPLQALPPLPLEKLYGSQdgfetakkiVGDDLFKAFVPSAVTTASSLYSEETAK 398
Cdd:pfam03097 300 KDNDFIYHERVPSESSLPPIKPASMVKPIPPLELYPFQ---------IGPDLFKKLVPLSVHEAASAYSERKAK 364
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 439-748 3.46e-41

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 152.77  E-value: 3.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   439 IPKELIEARSQLISFNPTFKIHELFAKSTKLKQ----IIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSEL 514
Cdd:pfam13949   2 LPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQrnreILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   515 NNYLKTLAEASATDSAISQQYALVKDDVETLCNS-SKISALLESSISSTDNSgqslldipieqeeqerDMKIQLDLLEEL 593
Cdd:pfam13949  82 RKYREILEQASESDSQVRSKFREHEEDLELLSGPdEDLEAFLPSSRRAKNSP----------------SVEEQVAKLREL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   594 QSRVQKLVPERQTTLQALQQKCLQDDISESLMQNSKRKDSALDTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVT 673
Cdd:pfam13949 146 LNKLNELKREREQLLKDLKEKARNDDISPKLLLEKARLIAPNQEEQLFEEELEKYDPLQNRLEQNLHKQEELLKEITEAN 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   674 QKLKQNPEFL--------RKMEVYNNQFSKNKElcsnllsssltakaISEGVSKGLEYYKTVEQRLAEINKTLGEQLLLR 745
Cdd:pfam13949 226 NEFLQDKRVDsekqrqreEALQKLENAYDKYKE--------------LVSNLQEGLKFYNDLTEILEKLLKKVKDFVNAR 291


                  ...
gi 19115164   746 RKQ 748
Cdd:pfam13949 292 RSE 294
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 8-344 3.27e-39

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: 148.60  E-value: 3.27e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   8 FFYLNKKETKHSDWVEPFTTFVSRIY---GNSVDVEDQIKAFNTLRENAA--DVDDTVAGKDILYSYYGQLDYLSFRFPT 82
Cdd:cd09240   3 FISVPLKKSSEVDLVKPLEKFIKNTYssgEEQADYKEAIKELNKLRNNAVcrPLDKHESSLELLLRYYDQLCAIEPKFPF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  83 GGNGINISFEWSDILDPDADF---VKQ--SSLAFEKASVLFNLVSLLSRMAANhASAYTVDDYKAAANCLQCASGIAKLL 157
Cdd:cd09240  83 SESQIQVTFTWKDAFDKGSLFggsKKLalSSLGYEKVCVLFNIAALQSQIAAE-QNLDTDEGLKLAAKLFQQAAGIFNHL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 158 RES----FIHAPGRDLDSNFLLGIYNLFLGQAQECVLghmsFSASDSNMNYSLAAKIASSAATLYDSCVHAFEsmEPACN 233
Cdd:cd09240 162 KETvlsaLQQEPTPDLSPDTLSALSALMLAQAQEVFY----LKATRDKMKDAIIAKLAAQAADYYGDAFKQCQ--REDVR 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 234 PNF----IRLASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLSTDFIHKpslsdypqtis 309
Cdd:cd09240 236 SLLpkdwIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAK----------- 304

                       330       340       350
                ....*....|....*....|....*....|....*
gi 19115164 310 tfikssLSHLLKTAEKDNDFVFHDLVVKEVELPKI 344
Cdd:cd09240 305 ------ISRALTAAKKDNDFIYHDRVPDVKSLPPI 333
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 8-345 1.37e-38

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: 146.73  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   8 FFYLNKKETKHSDWVEPFTTFVSRIYG--NSVDVEDQIKAFNTLRENAA--DVDDTV--AGKDILYSYYGQLDYLSFRFP 81
Cdd:cd09034   1 FIGLPLKKTKEVDVKVPLSKFIPKNYGelEATAVEDLIEKLSKLRNNIVteQNNDTTceNLLEALKEYLPYLLGLEKKLP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  82 TGGNGINISFEWSDILDPDADfvKQSSLAFEKASVLFNLVSLLSRMAANHASAYTVDDYKAAANCLQCASGIAKLLRESF 161
Cdd:cd09034  81 FQKLRDNVEFTWTDSFDTKKE--SATSLRYELLSILFNLAALASQLANEKLITGSEEDLKQAIKSLQKAAGYFEYLKEHV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 162 IHAP----GRDLDSNFLLGIYNLFLGQAQECVLGhmsFSASDSNMNYSLAAKIASSAATLYDSCVHAFESMEPA----CN 233
Cdd:cd09034 159 LPLPpdelPVDLTEAVLSALSLIMLAQAQECFLL---KAEEDKKAKLSLLARLACEAAKYYEEALKCLSGVDLEtiknIP 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 234 PNFIRLASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLStdfihkpslsdyPQTISTFIK 313
Cdd:cd09034 236 KKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKSFLLD------------VWGNLKKLK 303

                       330       340       350
                ....*....|....*....|....*....|..
gi 19115164 314 SSLSHLLKTAEKDNDFVFHDLVVKEVELPKIS 345
Cdd:cd09034 304 EKIEKELEKAERENDFIYFEEVPPEDPLPEIK 335
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 8-344 1.17e-37

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: 144.33  E-value: 1.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   8 FFYLNKKETKHSDWVEPFTTFVSRIYGNSVDV-EDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTggng 86
Cdd:cd09241   2 LLSIPFKRTLPVDLKDALRNYISNHYFQTPSSfEDDLAEIDKLRNDAINPEPSVNGLSLLKEYYAQLVVLSKKFPD---- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  87 INISFEWSDILDPDADF-VKQSSLAFEKASVLFNLVSLLSRMAANhASAYTVDDYKAAANCLQCASGIAKLLRESFI--H 163
Cdd:cd09241  78 DQLEFTWYPTLGYKSSGpVSLSSLKFERANILYNLGALYSQLALS-ENRYTDEGLKRACSYFQASAGCFEYILQHLLptL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 164 APGRDLDSNFLLGIYNLFLGQAQECVLghmsFSASDSNMNYSLAAKIASSAATLYDScvhAFESMEPAcnpNFIRLA--- 240
Cdd:cd09241 157 SPPPDLDENTLKALESLMLAQAQECFW----QKAISDGTKDSLIAKLAAQVSDYYQE---ALKYANKS---DLIRSDwin 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 241 --SAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAqklfngiKLSTDFIHKPSLSDYpQTISTFIKSSLsh 318
Cdd:cd09241 227 hlKVKKHHFKAAAHYRMALVALEKSKYGEEVARLRVALAACKEA-------LKEARYGNKAVLEDL-QGLKDIVKESL-- 296

                       330       340
                ....*....|....*....|....*.
gi 19115164 319 llKTAEKDNDFVFHDLVVKEVELPKI 344
Cdd:cd09241 297 --KRAERDNDLIYLQPVPPASELPPI 320
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 7-344 1.82e-36

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: 141.03  E-value: 1.82e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164   7 PFFYLNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTG-G 84
Cdd:cd09239   7 PMLWLQLKSSGEFTFQPALKKYILENYGeDPELYSEELKSLEQLRQEAVNPPRDFEGCSVLKRYYGQLHLLQSRFPMGaG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  85 NGINISFEWSDILDPDAdfVKQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRESFIHA 164
Cdd:cd09239  87 QEAAVPFTWTDIFSGSE--VTHEDIKFEEASVLYNIGALHSQLGASDKRD-SEEGMKVACTHFQCAAWAFAYLREHYPQV 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 165 PG-RDLDSNFLLGIYNLFLGQAQECVLGHmsfSASDsNMNYSLAAKIASSAATLYDSCVHAFESMEpaCNPNFI------ 237
Cdd:cd09239 164 YGaVDMSSQLLSFNYSLMLAQAQECLLEK---SLLD-NRKSHITAKVSAQVVEYYKEALRALENWE--SNSKIIlgkiqk 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 238 ---RLASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKlstdfihkpsLSDYPQTISTFIKS 314
Cdd:cd09239 238 ewrKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVAYYQLANDKLEEAIKNAKGQP----------DTVNLQEALSFTMD 307

                       330       340       350
                ....*....|....*....|....*....|
gi 19115164 315 SLSHLLKTAEKDNDFVFHDLVVKEVELPKI 344
Cdd:cd09239 308 VIGGKRNSAKKENDFIYHEAVPKLDTLQAV 337
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
 14-275 3.89e-33

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: 130.92  E-value: 3.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  14 KETKHSDWVEPFTTFVSRIYGNSVDV-EDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNGINISFE 92
Cdd:cd09244   7 KETKEIDFMEPFKDFILEHYSEDPSLyEDEIADFTDLRQAMRTPSRDEAGIELLFEYYNQLYFVERRFFPPDRSLGIYFH 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  93 WSDILD--PdadfVKQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRESFIHAPGRDLD 170
Cdd:cd09244  87 WYDSLTgvP----SVQRSVAFEKASVLFNIGALYTQIGAKQDRT-TEEGIEAAVDAFQRAAGAFNYLRENFSNAPSMDLS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 171 SNFLLGIYNLFLGQAQECVLGHMSFSASDSNmNYSLAAKIASSAATLYDSCVHAFESM-EPACNPN----FIRLASAKKA 245
Cdd:cd09244 162 PEMLEALIKLMLAQAQECVFEKLVLPGEDSK-DIQACLDLAQEAAQVSDCYSEVHKLMnQEPVKDYipysWISLVEVKSE 240

                       250       260       270
                ....*....|....*....|....*....|
gi 19115164 246 ALEGFSSYFMARAQLEKSKQGLAIGYLQQA 275
Cdd:cd09244 241 HYKALAHYYAAMGLLLEERRLLGKAHLKEA 270
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 12-345 9.98e-32

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: 127.13  E-value: 9.98e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  12 NKKETKHSDWVEPFTTFVSRIYGNSV--DVEDQIKAFNTLRENAADVDDTVAG-KDILYSYYGQLDYLSFRFP--TGGNG 86
Cdd:cd09246   5 HRKKTETVDLVSPLRAYISETYSEREaqDAEDDLAELQQLRSEVRTLQEKHAAsRELLLRYYRALCAVESRFPisEESGH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  87 INISFEWSDILDPDADFVkQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRE-SFIHAP 165
Cdd:cd09246  85 ARVSFSWYDAFRPHRKAT-QANVHFEKAAVLFNLGALSSQLGLQQDRT-TAEGIKQACHAFQAAAGAFAHLRDkVSGKTG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 166 GR---DLDSNFLLGIYNLFLGQAQECVLGhmsfSASDSNMNYSLAAKIASSAATLYDSCVHAFESmePACNPNFIRLASA 242
Cdd:cd09246 163 GFrtpDLTAECLGMLESLMLAQAQECFYE----KAVADGKSPAVCSKLAKQARSYYEEALEALDS--PPLKGHFDKSWVA 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 243 ----KKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKLFNGIKLstdfihkPSLSDYPQTISTFIKSslsh 318
Cdd:cd09246 237 hvqlKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEARKQAKGVNG-------DELIEAVSELEQVINE---- 305

                       330       340
                ....*....|....*....|....*..
gi 19115164 319 LLKTAEKDNDFVFHDLVVKEVELPKIS 345
Cdd:cd09246 306 LLERAEKENDCVYLDRVPAPSDLPPLG 332
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 11-215 2.68e-24

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


Pssm-ID: 185771  Cd Length: 384  Bit Score: 105.73  E-value: 2.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  11 LNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNGINI 89
Cdd:cd09248   4 LGLKETKELDLPTPLKELISEHFGeDGTSYEAEIRELEDLRQAMRTPSRSEAGLELLMAYYNQLCFLDARFFPPAKSLGL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  90 SFEWSDILD--PdadfVKQSSLAFEKASVLFNLVSLLSRMAANHASAyTVDDYKAAANCLQCASGIAKLLRESFIHAPGR 167
Cdd:cd09248  84 FFHWYDSLTgvP----AQQRALAFEKGSVLFNIGALHTQIGARQDRS-CTEGTRRAIDAFQRAAGAFSLLRENFSNAPSP 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19115164 168 DLDSNFLLGIYNLFLGQAQECVLGHMSFSASDSNMNYSLAAKIASSAA 215
Cdd:cd09248 159 DMSTASLSMLEQLMVAQAQECIFEGLLLPLLATPQDFFAQLQLAQEAA 206
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
 11-196 3.93e-18

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: 87.21  E-value: 3.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  11 LNKKETKHSDWVEPFTTFVSRIYG-NSVDVEDQIKAFNTLRENAADVDDTVAGKDILYSYYGQLDYLSFRFPTGGNGINI 89
Cdd:cd09249   4 LGLKETKDVDFSVPLKDFILEHYSeDGSEYEDEIADLMDLRQACRTPSRDEAGVELLMSYFSQLGFLENRFFPPTRQMGI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  90 SFEWSDILD--PdadfVKQSSLAFEKASVLFNLVSLLSRMAAnHASAYTVDDYKAAANCLQCASGIAKLLRESFIHAPGR 167
Cdd:cd09249  84 LFTWYDSFTgvP----VSQQNLLLEKASILFNIGALYTQIGT-RCNRQTQAGLESAVDAFQRAAGVLNYLKETFTHTPSY 158

                       170       180
                ....*....|....*....|....*....
gi 19115164 168 DLDSNFLLGIYNLFLGQAQECVLGHMSFS 196
Cdd:cd09249 159 DMSPAMLSVLVKMMLAQAQECLFEKISLP 187
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 382-698 1.10e-17

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all 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. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 85.09  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRAE-QAEVERQNTQMATVFASLDLSRLqeITHSDSKTNFIPkelIEARSQLISFNPTFKIH 460
Cdd:cd08915   1 PYDVIESASAYNERQDDYVREHiVEPIEALNKLLNSFLAERNLPAS--IDDLQKPENLPD---SIQHSQEIIEEGGLDNI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 461 ELFAK-----STKLKQIIAKIKSDLEVEANENAKMKAKLGP-SWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQQ 534
Cdd:cd08915  76 EQSFKelsklRQNVEELLQECEELLEEEAAEDDQLRAKFGTlRWRRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQC 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 535 YALVKDDVETLCNSSKISALLESSISSTdnsgqslLDIPIEQEEQErdmkiqldlLEELQSRVQKLVPERQTTLQALQQK 614
Cdd:cd08915 156 YESIDPNLVLLCGGYKELKAFIPSPYPA-------LDPEVSEVVSS---------LRPLLNEVSELEKERERFISELEIK 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 615 CLQDDISESLMQNSKRKDSaLDTNQLFELELKKFDPLrnrlhasyrqqqlllneMRNVTQKLKQNPEFLRKMEVYNNQFS 694
Cdd:cd08915 220 SRNNDILPKLITEYKKNGT-TEFEDLFEEHLKKFDKD-----------------LTYVEKTKKKQIELIKEIDAANQEFS 281


                ....
gi 19115164 695 KNKE 698
Cdd:cd08915 282 QVKN 285
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 88-342 9.93e-17

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: 82.44  E-value: 9.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  88 NISFEWSDIL--DPDADFVKQSSLAFEKASVLFnLVSLLSRmaanhASAYTV---DDYKAAANCLQCASGIAKLLRESFI 162
Cdd:cd09247  85 QLSFRWTSGLgsSKGPKAFQSDSLRFELGMVLF-LYGAALR-----ERASEVlptEDFKEAATHLRRAAGVFEFLAHDEL 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 163 -------HAPGR--DLDSNFLLGIYNLFLGQAQECVLGhmsfSASDSNMNYSLAAKIASSAATLYDSCVHAFESMEPACN 233
Cdd:cd09247 159 prlrgalSADERppECTPSLALAMSLLCLAEAQAVTAR----KAEEKGTSPSLLAKLHYGATQFLEEAKNVLRSLATDLK 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 234 ---PNFIRLASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAqklfngiklstdfihKPSLSDYPQTIST 310
Cdd:cd09247 235 dldPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKK---------------LPGSDISSPVIFR 299

                       250       260       270
                ....*....|....*....|....*....|..
gi 19115164 311 FIKSSLSHLLKTAEKDNDFVFHDLVVKEVELP 342
Cdd:cd09247 300 DERAEVATLLQKYEKENEVIYFEKVPDIDELP 331
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 89-339 7.51e-16

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: 79.69  E-value: 7.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  89 ISFEWSDILDPDADFVKQSSLaFEKASVLFNLVSLLSRMAANHASA--YTVDDYKAAANCLQCASGIAKLLRESFIH--- 163
Cdd:cd09243  85 INFKWTDSLLGNEPSVQQDAI-FELASMLFNVALWYTKHASKLAGKedITEDEAKDVHKSLRTAAGIFQFVKENYIPkli 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 164 ---APGRDLDSNFLLGIYNLFLGQAQECVLGHmsfsASDSNMNYSLAAKIASSAATLYDSCVHAFESMEPACNPNFIRLA 240
Cdd:cd09243 164 epaEKGSDLDPRVLEAYINQCTAEAQEVTVAR----AIELKHNAGLISALAYETAKLFQKADDSLSSLDPEYSGKWRKYL 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 241 SAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILSSAQKL------FNGIKLSTdfihKPSLSDYPQTISTFIKS 314
Cdd:cd09243 240 QLKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALckeyakTKGPGTTA----KPDQHLFFRKLGPLVKR 315

                       250       260
                ....*....|....*....|....*
gi 19115164 315 SLShllkTAEKDNDFVFHDLVVKEV 339
Cdd:cd09243 316 TLE----KCERENGFIYHQKVPDEV 336
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
 382-685 4.10e-10

Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.


Pssm-ID: 185749 [Multi-domain]  Cd Length: 353  Bit Score: 62.37  E-value: 4.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRaEQAEVERQN--TQMATVFASLDL-SRLQEIthsdSKTNFIPKELIEARSQLISFNPTFK 458
Cdd:cd09236   1 PFGVHLAISIYDDRKDRLVN-ESIIDELEEltNRAHSTLRSLNLpGSLQAL----EKPLGLPPSLLRHAEEIRQEDGLER 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 459 IHELFAKSTKLK----QIIAKIKSDLEVEANENAKMKAKLGPS-WTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQ 533
Cdd:cd09236  76 IRASLDDVARLAasdrAILEEAMDILDDEASEDESLRRKFGTDrWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRR 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 534 QYALVKDDVETLcNSSKISalLESSISSTDNSgqsllDIPIEQEEQERDMKIQLDLLEELQSRVQKLVperqttlQALQQ 613
Cdd:cd09236 156 KLDEWEDLIQIL-TGDERD--LENFVPSSRRP-----SIPPELERHVRALRVSLEELDRLESRRRRKV-------ERART 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 614 KCLQDDISESLMQNSKRKDSALDTNQ--------LFELELKKFDPLRNRLHASYRQQQLLLNEMRNvtqklkQNPEFLRK 685
Cdd:cd09236 221 KARADDIRPEILREAARLEREYPATEvapahfedLFDKRLAKYDKDLDAVSEEAQEQEEILQQIEV------ANKAFLQS 294
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 382-656 1.08e-09

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to 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 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: 185747 [Multi-domain]  Cd Length: 337  Bit Score: 60.77  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRAEQAEVERQNTQMATVFASLDLSRLQEIthSDSKTNFIPKELIEaRSQLISFNPTfKIHE 461
Cdd:cd09234   1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPLNVM--DMDGQFELPQDLVE-RCAALSVRPD-TIKN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 462 LFAKSTKLKQI-------IAKIKSDLEVEANENAKMKAKLGPSwtlSDSLEFAAPYQSELNNYLKTLAEASATDS----A 530
Cdd:cd09234  77 LVEAMGELSDVyqdveamLNEIESLLEEEELQEKEFQEAVGKR---GSSIAHVTELKRELKKYKEAHEKASQSNTelhkA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 531 ISQQYA---LVKDDVETLcnsskiSALLESsisstdnsgQSLLDIPIEqEEQERDMKIQLDLLEELQSRVQKLVPERQTT 607
Cdd:cd09234 154 MNLHIAnlkLLAGPLDEL------QKKLPS---------PSLLDRPED-EAIEKELKRILNKVNEMRKQRRSLEQQLRDA 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 19115164 608 LQalqqkclQDDISESLMQNSKRkdsalDTNQLFELELKKFDPLRNRLH 656
Cdd:cd09234 218 IH-------EDDITSKLVTTTGG-----DMEDLFKEELKKHDQLVNLIE 254
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
 471-740 1.20e-07

Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This domain family is comprised of uncharacterized plant proteins. It belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), (His-Domain) type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. 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. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_Rim20_Bro1_like superfamily also have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members of the V_Alix_like superfamily also have a proline-rich region (PRR).


Pssm-ID: 185751  Cd Length: 339  Bit Score: 54.40  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 471 QIIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAIsqqyalvkddvetlcnssk 550
Cdd:cd09238  93 ELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFRVNLEQAGDSDESL------------------- 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 551 isallESSISSTDNSGQSLLDIPIEQeeQERDMKIQLDLLEELQSRVqklVPERQTTLQALQQKCLQDDISESLMQNSKR 630
Cdd:cd09238 154 -----RRRIEDAMDGMLILDDEPAAA--AAPTLRAPMLSTDEDDASI---VGTLRSNLEELEALGNERAGIEDMMKALKR 223

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 631 KDSAL--------DTNQLFELELKKFDPLRNRLHASYRQQQLLLNEMRNVTQKLKQnpeflrkmeVYNNQFSKNKELCSN 702
Cdd:cd09238 224 NDNILakvmattgSYDALFKEELKKYDSVREAVSKNISSQDDLLSRLRALNEKFSQ---------IFDVEGWRAATESHA 294

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 19115164 703 LLSSSLTAK--AISEGVSKGLEYYKTVeqrLAEINKTLGE 740
Cdd:cd09238 295 TQIRAAVAKyrELREGMEEGLRFYSGF---QEAVRRLKQE 331
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 382-675 5.40e-06

Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction modules; This family contains the middle V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X) and related domains. It belongs to the V_Alix_like superfamily which includes the V-domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), is part of the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in membrane remodeling processes, including the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), the abscission reactions of mammalian cell division, and in apoptosis. The Alix V-domain is a dimerization domain, and contains a binding site, partially conserved in the V_Alix_like superfamily, for the retroviral late assembly (L) domain YPXnL motif. In addition to the V-domain, Alix also has an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex, in particular CHMP4. The Bro1-like domain of Alix can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. 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: 185748  Cd Length: 339  Bit Score: 49.20  E-value: 5.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 382 PSAVTTASSLYSEETAKVFRAEQAEVeRQNTQ-MATVFASLDLSRLQEITHSDSktnfIPKELIEARSQLISFNPTFKIH 460
Cdd:cd09235   1 PVSVHQALAAYNQRKAELVNREIGKL-REATQlLNGVLASLNLPAAIEDVSGDT----VPQSLLEKSRTVIEKGGIQTID 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 461 ELFAKSTKL----KQIIAKIKSDLEVEANENAKMKAKLGPSWTLSDSLEFAAPYQSELNNYLKTLAEASATDSAISQQYA 536
Cdd:cd09235  76 QLIKELPELlqrnREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 537 LVKDDVETLC-NSSKISALLESSISSTDNSGQSLLDIPIEQEEQERDMKIQLDLLE-ELQSRVQKLvpeRQTTLQALQQk 614
Cdd:cd09235 156 SHREGIELLSkPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIEsELKSATFDM---KSKFLSALAQ- 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115164 615 clqddiseslmqnskrkDSALDTNQLFELELKK-FDPLRNRLHASYRQQQLLLNEMRNVTQK 675
Cdd:cd09235 232 -----------------DGAINEEAISVEELDRvYGPLQKQVQESLSRQESLLANIQVAHQE 276
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
 91-330 2.80e-05

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: 47.40  E-value: 2.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164  91 FEW----SDILDPDADFVKQSSLAFEKASVLFNL---VSLLSR------MAANHASAYTVDDYKAAANCLQ------C-A 150
Cdd:cd09245  90 FEWrttlSSTSGRESPRLPLPGLHYELAFVLLTYayaLSNLARsilaplGAYETDRSISDASRKQRDERLKaatkllCkA 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 151 SGIAKLLRESFIHA---------PGRDLDSNFLLGIYNLFLGQAQE-CVLGHMSFSA--SDSNMNY-----------SLA 207
Cdd:cd09245 170 AGIFDYLATRVLPQwesnrggapPPPDLSPEVLSALSSLALAEATLlAVRKLDPYPAavDKDWMTPgpplpkvhpsaHLL 249

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115164 208 AKIASSAATLYDSCV-----HAFESMEPACNPNFIRLASAKKAALEGFSSYFMARAQLEKSKQGLAIGYLQQAKSILS-- 280
Cdd:cd09245 250 ARLCLAASEHAESARallstPGSKRGSGEVSEELLRYLSDLRRVARALACKFLGIDAGENGKVGEAIGWLRAAKKELEdl 329

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 19115164 281 -SAQKLFNGIKLSTDFIHKPSL-SDYPQTISTFIKSSLSHLLKTAEKDNDFV 330
Cdd:cd09245 330 kSPSGVASKAKLKKSWKEKREDrKVEKGAGVEEELRTLEMLLKKYKKMNDTV 381
 
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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