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Conserved domains on  [gi|6324849|ref|NP_014918|]
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Rim20p [Saccharomyces cerevisiae S288C]

Protein Classification

BRO1 domain-containing protein( domain architecture ID 10174072)

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_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
3-343 1.72e-159

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: 462.51  E-value: 1.72e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    3 ELLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFPNNQI 82
Cdd:cd09241   1 NLLSIPFKRTLPVDLKDALRNYISNHYFQTPSSFEDDLAEIDKLRNDAINPEPSVNGLSLLKEYYAQLVVLSKKFPDDQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   83 EFTWFQTLSQKSRGTSQY-SLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLETIP- 160
Cdd:cd09241  81 EFTWYPTLGYKSSGPVSLsSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYILQHLLPTLSPPp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  161 VVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRSDWINHLKAKKAYFSAVTY 240
Cdd:cd09241 161 DLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSDLIRSDWINHLKVKKHHFKAAAH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  241 YRIALSFNEKKQFGNVVKALQMGLQFINEST----------LSSQAKFKTVVESSLKEAQRDNEFIYLQEVP--SELPSI 308
Cdd:cd09241 241 YRMALVALEKSKYGEEVARLRVALAACKEALkearygnkavLEDLQGLKDIVKESLKRAERDNDLIYLQPVPpaSELPPI 320
                       330       340       350
                ....*....|....*....|....*....|....*
gi 6324849  309 KPALMVKPSSSATLLPSIKKDETLFKDLIPIEVME 343
Cdd:cd09241 321 KPASMVKAIVPPELEEGSKLGKPLFKDLLPYGVHE 355
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
338-645 5.58e-98

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: 304.26  E-value: 5.58e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  338 PIEVMEYCTAYNERQDEYVEQRVTNPLASLNKLLKESLTTFQIPQGLTKV-----------------SEAELSHYQASLN 400
Cdd:cd08915   1 PYDVIESASAYNERQDDYVREHIVEPIEALNKLLNSFLAERNLPASIDDLqkpenlpdsiqhsqeiiEEGGLDNIEQSFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  401 NLLINNKNVQVQLDNIEQILNEEAFTDNQLRLKHGTLNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSID 480
Cdd:cd08915  81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  481 KNLI---------------------GSEIRLPESNDPLTNKIKMIIQERNDYIDRTRRKSSEYRILPKIITSYKKNGTVD 539
Cdd:cd08915 161 PNLVllcggykelkafipspypaldPEVSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDILPKLITEYKKNGTTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  540 FEPIFIGHLKYFDEDLRYVNSTKEENIKLIEEVNLSKKNNPGRSGIEpkkmVRIDPRELYIEDLRYSFKLLDEVKENLSA 619
Cdd:cd08915 241 FEDLFEEHLKKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSN----DSLDPREEALQDLEASYKKYLELKENLNE 316
                       330       340
                ....*....|....*....|....*.
gi 6324849  620 GTAFYENLITSTSNLYNEVQEYDTAR 645
Cdd:cd08915 317 GSKFYNDLIEKVNRLLEECEDFVNAR 342
 
Name Accession Description Interval E-value
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
3-343 1.72e-159

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: 462.51  E-value: 1.72e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    3 ELLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFPNNQI 82
Cdd:cd09241   1 NLLSIPFKRTLPVDLKDALRNYISNHYFQTPSSFEDDLAEIDKLRNDAINPEPSVNGLSLLKEYYAQLVVLSKKFPDDQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   83 EFTWFQTLSQKSRGTSQY-SLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLETIP- 160
Cdd:cd09241  81 EFTWYPTLGYKSSGPVSLsSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYILQHLLPTLSPPp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  161 VVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRSDWINHLKAKKAYFSAVTY 240
Cdd:cd09241 161 DLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSDLIRSDWINHLKVKKHHFKAAAH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  241 YRIALSFNEKKQFGNVVKALQMGLQFINEST----------LSSQAKFKTVVESSLKEAQRDNEFIYLQEVP--SELPSI 308
Cdd:cd09241 241 YRMALVALEKSKYGEEVARLRVALAACKEALkearygnkavLEDLQGLKDIVKESLKRAERDNDLIYLQPVPpaSELPPI 320
                       330       340       350
                ....*....|....*....|....*....|....*
gi 6324849  309 KPALMVKPSSSATLLPSIKKDETLFKDLIPIEVME 343
Cdd:cd09241 321 KPASMVKAIVPPELEEGSKLGKPLFKDLLPYGVHE 355
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-356 2.39e-129

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: 385.78  E-value: 2.39e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849      4 LLAIPLKRTLEVDFATELSKLIDTT-SFQTASFFQSDILKVVDARNNAIAP-DISIDGLSALKEYYVILLQLEKKFPNN- 80
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTyGSQDPSSFEDDLAELNKLRQDAVRGaNEDESGLDLLYKYYAQLELLELRFPIDi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849     81 --QIEFTWFQTLSQKSRGTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLET 158
Cdd:pfam03097  81 qiGIEFTWYDAFGTSSKKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYLKENFLHAPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    159 iPVVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRSDWINHLKAKKAYFSAV 238
Cdd:pfam03097 161 -PDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDKEWISHVQAKAHHFKAL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    239 TYYRIALSFNEKKQFGNVVKALQMGLQFINE--------STLSSQAKFKTVVESSLKEAQRDNEFIYLQEVPSE--LPSI 308
Cdd:pfam03097 240 AQYRQALDDEEAKKYGEEIARLQLALSLLKEalksdrykKVLEDLKGLLDVVEEKLKRAEKDNDFIYHERVPSEssLPPI 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 6324849    309 KPALMVKPSSSATLLPSIKKdETLFKDLIPIEVMEYCTAYNERQDEYV 356
Cdd:pfam03097 320 KPASMVKPIPPLELYPFQIG-PDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-360 2.27e-108

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: 332.39  E-value: 2.27e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849       4 LLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFP----N 79
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSEDSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPppegQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849      80 NQIEFTWFQTLSQKSRgTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDH-QKNLET 158
Cdd:smart01041  81 LKLSFTWYDSLDTGVP-STQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYLKENfLHALST 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849     159 IPVVD--DATLNALTSLMLAQAQECFWFKAVQD--KHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRS----DWINHLKA 230
Cdd:smart01041 160 EPSVDlsPETLSALSSLMLAQAQECFFEKAILDgmKNKDSLIAKLAAQAAEYYEEALKALQTSEPVKGyipkSWIKLVQV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849     231 KKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINESTLSSQAK--------------FKTVVESSLKEAQRDNEFI 296
Cdd:smart01041 240 KAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLRCKklgkadklqedlsgLKDVVEEKLKEAEKDNDFI 319
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324849     297 YLQEVPSE--LPSIKPALMVKPsssaTLLPSIKKDETLFKDLIPIEVMEYCTAYNERQDEYVEQRV 360
Cdd:smart01041 320 YHERVPDIvsLPPIKKAPLVKP----PPFSEVLKGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
338-645 5.58e-98

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: 304.26  E-value: 5.58e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  338 PIEVMEYCTAYNERQDEYVEQRVTNPLASLNKLLKESLTTFQIPQGLTKV-----------------SEAELSHYQASLN 400
Cdd:cd08915   1 PYDVIESASAYNERQDDYVREHIVEPIEALNKLLNSFLAERNLPASIDDLqkpenlpdsiqhsqeiiEEGGLDNIEQSFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  401 NLLINNKNVQVQLDNIEQILNEEAFTDNQLRLKHGTLNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSID 480
Cdd:cd08915  81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  481 KNLI---------------------GSEIRLPESNDPLTNKIKMIIQERNDYIDRTRRKSSEYRILPKIITSYKKNGTVD 539
Cdd:cd08915 161 PNLVllcggykelkafipspypaldPEVSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDILPKLITEYKKNGTTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  540 FEPIFIGHLKYFDEDLRYVNSTKEENIKLIEEVNLSKKNNPGRSGIEpkkmVRIDPRELYIEDLRYSFKLLDEVKENLSA 619
Cdd:cd08915 241 FEDLFEEHLKKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSN----DSLDPREEALQDLEASYKKYLELKENLNE 316
                       330       340
                ....*....|....*....|....*.
gi 6324849  620 GTAFYENLITSTSNLYNEVQEYDTAR 645
Cdd:cd08915 317 GSKFYNDLIEKVNRLLEECEDFVNAR 342
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
409-648 2.21e-26

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: 109.63  E-value: 2.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    409 VQVQLDNIEQILNEEAFTDNQLRLKHGTlNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSIDKNLI---- 484
Cdd:pfam13949  36 NREILDEAEKLLDEEESEDEQLRAKYGT-RWTRPPSSELTATLRAEIRKYREILEQASESDSQVRSKFREHEEDLEllsg 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    485 -----------GSEIRLPESNDPLTNKIKMII-------QERNDYIDRTRRKSSEYRILPKIITSYKKNGTVD-FEPIFI 545
Cdd:pfam13949 115 pdedleaflpsSRRAKNSPSVEEQVAKLRELLnklnelkREREQLLKDLKEKARNDDISPKLLLEKARLIAPNqEEQLFE 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    546 GHLKYFDEDLRYVNSTKEENIKL---IEEVNLSKKNNPGRSGIEPKKmvridpRELYIEDLRYSFKLLDEVKENLSAGTA 622
Cdd:pfam13949 195 EELEKYDPLQNRLEQNLHKQEELlkeITEANNEFLQDKRVDSEKQRQ------REEALQKLENAYDKYKELVSNLQEGLK 268
                         250       260
                  ....*....|....*....|....*.
gi 6324849    623 FYENLITSTSNLYNEVQEYDTARRAE 648
Cdd:pfam13949 269 FYNDLTEILEKLLKKVKDFVNARRSE 294
 
Name Accession Description Interval E-value
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
3-343 1.72e-159

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: 462.51  E-value: 1.72e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    3 ELLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFPNNQI 82
Cdd:cd09241   1 NLLSIPFKRTLPVDLKDALRNYISNHYFQTPSSFEDDLAEIDKLRNDAINPEPSVNGLSLLKEYYAQLVVLSKKFPDDQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   83 EFTWFQTLSQKSRGTSQY-SLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLETIP- 160
Cdd:cd09241  81 EFTWYPTLGYKSSGPVSLsSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYILQHLLPTLSPPp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  161 VVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRSDWINHLKAKKAYFSAVTY 240
Cdd:cd09241 161 DLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSDLIRSDWINHLKVKKHHFKAAAH 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  241 YRIALSFNEKKQFGNVVKALQMGLQFINEST----------LSSQAKFKTVVESSLKEAQRDNEFIYLQEVP--SELPSI 308
Cdd:cd09241 241 YRMALVALEKSKYGEEVARLRVALAACKEALkearygnkavLEDLQGLKDIVKESLKRAERDNDLIYLQPVPpaSELPPI 320
                       330       340       350
                ....*....|....*....|....*....|....*
gi 6324849  309 KPALMVKPSSSATLLPSIKKDETLFKDLIPIEVME 343
Cdd:cd09241 321 KPASMVKAIVPPELEEGSKLGKPLFKDLLPYGVHE 355
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-356 2.39e-129

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: 385.78  E-value: 2.39e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849      4 LLAIPLKRTLEVDFATELSKLIDTT-SFQTASFFQSDILKVVDARNNAIAP-DISIDGLSALKEYYVILLQLEKKFPNN- 80
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTyGSQDPSSFEDDLAELNKLRQDAVRGaNEDESGLDLLYKYYAQLELLELRFPIDi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849     81 --QIEFTWFQTLSQKSRGTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLET 158
Cdd:pfam03097  81 qiGIEFTWYDAFGTSSKKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYLKENFLHAPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    159 iPVVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRSDWINHLKAKKAYFSAV 238
Cdd:pfam03097 161 -PDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDKEWISHVQAKAHHFKAL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    239 TYYRIALSFNEKKQFGNVVKALQMGLQFINE--------STLSSQAKFKTVVESSLKEAQRDNEFIYLQEVPSE--LPSI 308
Cdd:pfam03097 240 AQYRQALDDEEAKKYGEEIARLQLALSLLKEalksdrykKVLEDLKGLLDVVEEKLKRAEKDNDFIYHERVPSEssLPPI 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 6324849    309 KPALMVKPSSSATLLPSIKKdETLFKDLIPIEVMEYCTAYNERQDEYV 356
Cdd:pfam03097 320 KPASMVKPIPPLELYPFQIG-PDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-360 2.27e-108

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: 332.39  E-value: 2.27e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849       4 LLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFP----N 79
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSEDSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPppegQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849      80 NQIEFTWFQTLSQKSRgTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDH-QKNLET 158
Cdd:smart01041  81 LKLSFTWYDSLDTGVP-STQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYLKENfLHALST 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849     159 IPVVD--DATLNALTSLMLAQAQECFWFKAVQD--KHKDSLIAKLSQQIVDFYCEAINDAQRGKLIRS----DWINHLKA 230
Cdd:smart01041 160 EPSVDlsPETLSALSSLMLAQAQECFFEKAILDgmKNKDSLIAKLAAQAAEYYEEALKALQTSEPVKGyipkSWIKLVQV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849     231 KKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINESTLSSQAK--------------FKTVVESSLKEAQRDNEFI 296
Cdd:smart01041 240 KAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLRCKklgkadklqedlsgLKDVVEEKLKEAEKDNDFI 319
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324849     297 YLQEVPSE--LPSIKPALMVKPsssaTLLPSIKKDETLFKDLIPIEVMEYCTAYNERQDEYVEQRV 360
Cdd:smart01041 320 YHERVPDIvsLPPIKKAPLVKP----PPFSEVLKGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
338-645 5.58e-98

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: 304.26  E-value: 5.58e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  338 PIEVMEYCTAYNERQDEYVEQRVTNPLASLNKLLKESLTTFQIPQGLTKV-----------------SEAELSHYQASLN 400
Cdd:cd08915   1 PYDVIESASAYNERQDDYVREHIVEPIEALNKLLNSFLAERNLPASIDDLqkpenlpdsiqhsqeiiEEGGLDNIEQSFK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  401 NLLINNKNVQVQLDNIEQILNEEAFTDNQLRLKHGTLNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSID 480
Cdd:cd08915  81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  481 KNLI---------------------GSEIRLPESNDPLTNKIKMIIQERNDYIDRTRRKSSEYRILPKIITSYKKNGTVD 539
Cdd:cd08915 161 PNLVllcggykelkafipspypaldPEVSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDILPKLITEYKKNGTTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  540 FEPIFIGHLKYFDEDLRYVNSTKEENIKLIEEVNLSKKNNPGRSGIEpkkmVRIDPRELYIEDLRYSFKLLDEVKENLSA 619
Cdd:cd08915 241 FEDLFEEHLKKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSN----DSLDPREEALQDLEASYKKYLELKENLNE 316
                       330       340
                ....*....|....*....|....*.
gi 6324849  620 GTAFYENLITSTSNLYNEVQEYDTAR 645
Cdd:cd08915 317 GSKFYNDLIEKVNRLLEECEDFVNAR 342
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
4-316 1.89e-84

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: 269.22  E-value: 1.89e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    4 LLAIPLKRTLEVDFATELSKLIDTTSFQ-TASFFQSDILKVVDARNNAIAPDISI----DGLSALKEYYVILLQLEKKFP 78
Cdd:cd09034   1 FIGLPLKKTKEVDVKVPLSKFIPKNYGElEATAVEDLIEKLSKLRNNIVTEQNNDttceNLLEALKEYLPYLLGLEKKLP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   79 NN----QIEFTWFQTLSQKSrgTSQYSLQWEKLTIIYNIGCMYSLLALNSNND-AAESLKTSCLYFQNAAGCFKHVLDHQ 153
Cdd:cd09034  81 FQklrdNVEFTWTDSFDTKK--ESATSLRYELLSILFNLAALASQLANEKLITgSEEDLKQAIKSLQKAAGYFEYLKEHV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  154 KNL---ETIPVVDDATLNALTSLMLAQAQECFWFKAVQD-KHKDSLIAKLSQQIVDFYCEAIN-----DAQRGKLIRSDW 224
Cdd:cd09034 159 LPLppdELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDkKAKLSLLARLACEAAKYYEEALKclsgvDLETIKNIPKKW 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  225 INHLKAKKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINESTLSS----------QAKFKTVVESSLKEAQRDNE 294
Cdd:cd09034 239 LLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCksflldvwgnLKKLKEKIEKELEKAEREND 318
                       330       340
                ....*....|....*....|....
gi 6324849  295 FIYLQEVPSE--LPSIKPALMVKP 316
Cdd:cd09034 319 FIYFEEVPPEdpLPEIKGALLVKP 342
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
2-321 2.47e-62

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: 211.00  E-value: 2.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    2 SELLAIPLKRTLEVDFATELSKLIDTTsFQTASFfQSDILKVVDA----RNNAI--APDISIDGLSALKEYYVILLQLEK 75
Cdd:cd09240   1 ASFISVPLKKSSEVDLVKPLEKFIKNT-YSSGEE-QADYKEAIKElnklRNNAVcrPLDKHESSLELLLRYYDQLCAIEP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   76 KFP----NNQIEFTWFQTLSQKS-----RGTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCF 146
Cdd:cd09240  79 KFPfsesQIQVTFTWKDAFDKGSlfggsKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  147 KHVLDH-QKNLETIPVVDDA--TLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQR---GKLI 220
Cdd:cd09240 159 NHLKETvLSALQQEPTPDLSpdTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQRedvRSLL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  221 RSDWINHLKAKKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINE-STLSSQAK-FKTVVES---SLKEAQRDNEF 295
Cdd:cd09240 239 PKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTaQSRAGEYVdVKDFAAKisrALTAAKKDNDF 318
                       330       340
                ....*....|....*....|....*...
gi 6324849  296 IYLQEVPS--ELPSIKPALMVKPSSSAT 321
Cdd:cd09240 319 IYHDRVPDvkSLPPIGKAALAKPTPVNV 346
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
4-316 1.30e-61

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: 209.18  E-value: 1.30e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    4 LLAIPLKRTLEVDFATELSKLIDTT-SFQTASFFQSDILKV----VDARNNAIAPDISIDglsALKEYYVILLQLEKKFP 78
Cdd:cd09246   1 MLSIHRKKTETVDLVSPLRAYISETySEREAQDAEDDLAELqqlrSEVRTLQEKHAASRE---LLLRYYRALCAVESRFP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   79 ------NNQIEFTWFQTLSQKSRGTsQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDH 152
Cdd:cd09246  78 iseesgHARVSFSWYDAFRPHRKAT-QANVHFEKAAVLFNLGALSSQLGLQQDRTTAEGIKQACHAFQAAAGAFAHLRDK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  153 QKNLETIPVVDDAT---LNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAINDAQRGKL---IRSDWIN 226
Cdd:cd09246 157 VSGKTGGFRTPDLTaecLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSPPLkghFDKSWVA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  227 HLKAKKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINE-----------STLSSQAKFKTVVESSLKEAQRDNEF 295
Cdd:cd09246 237 HVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEarkqakgvngdELIEAVSELEQVINELLERAEKENDC 316
                       330       340
                ....*....|....*....|...
gi 6324849  296 IYLQEVP--SELPSIKPALMVKP 316
Cdd:cd09246 317 VYLDRVPapSDLPPLGAASMVKP 339
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
4-316 4.61e-47

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: 169.92  E-value: 4.61e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    4 LLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKFPNNQIE 83
Cdd:cd09239   8 MLWLQLKSSGEFTFQPALKKYILENYGEDPELYSEELKSLEQLRQEAVNPPRDFEGCSVLKRYYGQLHLLQSRFPMGAGQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   84 -----FTWFQTLSQKSrgTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDHQKNLET 158
Cdd:cd09239  88 eaavpFTWTDIFSGSE--VTHEDIKFEEASVLYNIGALHSQLGASDKRDSEEGMKVACTHFQCAAWAFAYLREHYPQVYG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  159 IPVVDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAI--------NDAQRGKLIRSDWINHLKA 230
Cdd:cd09239 166 AVDMSSQLLSFNYSLMLAQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALralenwesNSKIILGKIQKEWRKLVQM 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  231 KKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINEstLSSQAK--------FKT------VVESSLKEAQRDNEFI 296
Cdd:cd09239 246 KIAYYASIAHLHMGKQSEEQQKMGERVAYYQLANDKLEE--AIKNAKgqpdtvnlQEAlsftmdVIGGKRNSAKKENDFI 323
                       330       340
                ....*....|....*....|..
gi 6324849  297 YLQEVP--SELPSIKPALMVKP 316
Cdd:cd09239 324 YHEAVPklDTLQAVKGANLVKG 345
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
4-316 5.28e-47

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: 169.38  E-value: 5.28e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    4 LLAIPLKRTLEVDFATELSKLIdTTSFQTASFFQSDILKVVDA-RNNAIAPDISIDGLSALKEYYVILLQLEKKFPNN-- 80
Cdd:cd09242   1 LISLPLKDTEEVDWKKPLSSYL-KRSYGSSTFYYEEEIAEFDRlRQDANGVLADETGRDLLYKYYGQLELLELRFPFNnk 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   81 --QIEFTWFQTLSqKSRGTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDhqkNLET 158
Cdd:cd09242  80 elKVDFTWYDAFY-KSKKVKQHSLAFEKASVLFNIGALLSQLAAEKYREDEDDLKEAITNLQQAAGCFQYINE---NFLH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  159 IPVVD--DATLNALTSLMLAQAQECFWFKAVQDKH---KDSLIAKLSQQ-------IVDFYCEaINDAQRGKLIRSdWIN 226
Cdd:cd09242 156 APSVDlqQENVKFLVKLMLAQAQEIFLLKLINGDDaqkKASLISKLASAtanlyesCVEFLKE-IQEKGISYGDPK-WIS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  227 HLKAKKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINES---TLSSQAK--------------FKTVVESSLKEA 289
Cdd:cd09242 234 LVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEAnpqKLSLKASagdaayalnddfkgQKDTVEEKLKEL 313
                       330       340
                ....*....|....*....|....*....
gi 6324849  290 QRDNEFIYLQEVPSE--LPSIKPALMVKP 316
Cdd:cd09242 314 EKDNDFIYHDIVPSEvtLPSIKPLDAAKP 342
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
7-247 3.45e-28

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: 116.29  E-value: 3.45e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    7 IP--LKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKF--PNNQ- 81
Cdd:cd09244   2 IPlgLKETKEIDFMEPFKDFILEHYSEDPSLYEDEIADFTDLRQAMRTPSRDEAGIELLFEYYNQLYFVERRFfpPDRSl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   82 -IEFTWFQTLSqksrG--TSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVLDhqkNLET 158
Cdd:cd09244  82 gIYFHWYDSLT----GvpSVQRSVAFEKASVLFNIGALYTQIGAKQDRTTEEGIEAAVDAFQRAAGAFNYLRE---NFSN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  159 IPVVD--DATLNALTSLMLAQAQECFWFKAV--QDKHKDSLI----AKLSQQIVDFYCEAIndaqrgKLIRSD------- 223
Cdd:cd09244 155 APSMDlsPEMLEALIKLMLAQAQECVFEKLVlpGEDSKDIQAcldlAQEAAQVSDCYSEVH------KLMNQEpvkdyip 228
                       250       260
                ....*....|....*....|....*.
gi 6324849  224 --WINHLKAKKAYFSAVTYYRIALSF 247
Cdd:cd09244 229 ysWISLVEVKSEHYKALAHYYAAMGL 254
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
409-648 2.21e-26

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: 109.63  E-value: 2.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    409 VQVQLDNIEQILNEEAFTDNQLRLKHGTlNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSIDKNLI---- 484
Cdd:pfam13949  36 NREILDEAEKLLDEEESEDEQLRAKYGT-RWTRPPSSELTATLRAEIRKYREILEQASESDSQVRSKFREHEEDLEllsg 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    485 -----------GSEIRLPESNDPLTNKIKMII-------QERNDYIDRTRRKSSEYRILPKIITSYKKNGTVD-FEPIFI 545
Cdd:pfam13949 115 pdedleaflpsSRRAKNSPSVEEQVAKLRELLnklnelkREREQLLKDLKEKARNDDISPKLLLEKARLIAPNqEEQLFE 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    546 GHLKYFDEDLRYVNSTKEENIKL---IEEVNLSKKNNPGRSGIEPKKmvridpRELYIEDLRYSFKLLDEVKENLSAGTA 622
Cdd:pfam13949 195 EELEKYDPLQNRLEQNLHKQEELlkeITEANNEFLQDKRVDSEKQRQ------REEALQKLENAYDKYKELVSNLQEGLK 268
                         250       260
                  ....*....|....*....|....*.
gi 6324849    623 FYENLITSTSNLYNEVQEYDTARRAE 648
Cdd:pfam13949 269 FYNDLTEILEKLLKKVKDFVNARRSE 294
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
7-246 4.34e-18

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: 86.86  E-value: 4.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    7 IP--LKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKF--PNNQI 82
Cdd:cd09248   2 IPlgLKETKELDLPTPLKELISEHFGEDGTSYEAEIRELEDLRQAMRTPSRSEAGLELLMAYYNQLCFLDARFfpPAKSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   83 E--FTWFQTLSQKSrgTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVldhQKNLETIP 160
Cdd:cd09248  82 GlfFHWYDSLTGVP--AQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLL---RENFSNAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  161 VVD--DATLNALTSLMLAQAQECFWFKAV-------QDKHKDSLIAKLSQQIVDFYC---EAINDAQRGKLIRSDWINHL 228
Cdd:cd09248 157 SPDmsTASLSMLEQLMVAQAQECIFEGLLlpllatpQDFFAQLQLAQEAAQVAAEYRlvhRTMAQPPVRDYVPFSWTALV 236
                       250
                ....*....|....*...
gi 6324849  229 KAKKAYFSAVTYYRIALS 246
Cdd:cd09248 237 HVKAEHFCALAHYHAAMA 254
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
4-252 6.25e-17

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: 83.36  E-value: 6.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    4 LLAIPLKRTLEVDFATELSKLIDTTSFQTASFFQSDILKVVDARNNAIAPDISIDGLSALKEYYVILLQLEKKF--PNNQ 81
Cdd:cd09249   1 LIPLGLKETKDVDFSVPLKDFILEHYSEDGSEYEDEIADLMDLRQACRTPSRDEAGVELLMSYFSQLGFLENRFfpPTRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   82 IE--FTWFQTLSQKSrgTSQYSLQWEKLTIIYNIGCMYSLLALNSNNDAAESLKTSCLYFQNAAGC---FKHVLDHQKNL 156
Cdd:cd09249  81 MGilFTWYDSFTGVP--VSQQNLLLEKASILFNIGALYTQIGTRCNRQTQAGLESAVDAFQRAAGVlnyLKETFTHTPSY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  157 ETIPvvddATLNALTSLMLAQAQECFWFKAVQDKHKDS--LIAKLSQQ---IVDFYCE---AINDAQRGKLIRSDW---- 224
Cdd:cd09249 159 DMSP----AMLSVLVKMMLAQAQECLFEKISLPGIRNEffTLVKMAQEaakVGEVYMQvhtAMNQAPVKENIPYSWsslv 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 6324849  225 ---INHLKAKKAYFSAVTY--YRIALSFNEKKQ 252
Cdd:cd09249 235 qvkAHHYNALAHYFVATLLidHQLNPSDDEDKQ 267
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
8-306 6.51e-17

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: 82.77  E-value: 6.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849    8 PLKRTLEVDFatELSKLIDTTSfqtASFFQSDiLKVVDARNNAIAPDISIDGLSALKEY--YVILLQ-----LEKKFPNN 80
Cdd:cd09243   6 PLKATAPVKF--DLKGVATTPA---ASKLCSD-LRTARARLLELLSDPSNDVDTVKTAFnaYLSLLQgfilaLDGKTQES 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   81 Q----IEFTWFQTLsQKSRGTSQYSLQWEKLTIIYNIGCMY----SLLALNSN---NDAAE---SLKTsclyfqnAAGCF 146
Cdd:cd09243  80 KlrylINFKWTDSL-LGNEPSVQQDAIFELASMLFNVALWYtkhaSKLAGKEDiteDEAKDvhkSLRT-------AAGIF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  147 KHVLD-HQKNLETIPV----VDDATLNALTSLMLAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEA------INDAQ 215
Cdd:cd09243 152 QFVKEnYIPKLIEPAEkgsdLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKAddslssLDPEY 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  216 RGKlirsdWINHLKAKKAYFSAVTYyrialSFNEKKQF-----GNVVKALQMGLQFIN--ESTLSSQAKFK--------- 279
Cdd:cd09243 232 SGK-----WRKYLQLKSVFYLAYAY-----CYHGETLLakdkcGEAIRSLQESEKLYNkaEALCKEYAKTKgpgttakpd 301
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 6324849  280 ---------TVVESSLKEAQRDNEFIYLQEVPSELP 306
Cdd:cd09243 302 qhlffrklgPLVKRTLEKCERENGFIYHQKVPDEVP 337
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
348-627 1.94e-12

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: 68.92  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  348 YNERQDEYVEQRVTNPLASLNKLLKESLTTFQIP---QGLTK--------VSEAE-------LSHYQASLNNLLINNKNV 409
Cdd:cd09236  11 YDDRKDRLVNESIIDELEELTNRAHSTLRSLNLPgslQALEKplglppslLRHAEeirqedgLERIRASLDDVARLAASD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  410 QVQLDNIEQILNEEAFTDNQLRLKHGTLNWTLPESSTTNTAYYEKLKKLRGYLDEGSAIDKQTNELFQSIDKN---LIGS 486
Cdd:cd09236  91 RAILEEAMDILDDEASEDESLRRKFGTDRWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRRKLDEWEDLiqiLTGD 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  487 EIRL----PESNDP---------------LTNKIKMIIQERNDYIDRTRRKSSEYRILPKII---------TSYKKNGTV 538
Cdd:cd09236 171 ERDLenfvPSSRRPsippelerhvralrvSLEELDRLESRRRRKVERARTKARADDIRPEILreaarlereYPATEVAPA 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  539 DFEPIFIGHLKYFDEDLRYVNSTKEENIKLIEEVNLSKKNNPGRSGIEPKkmvrIDPRELYIEDLRYSFKLLDEVKENLS 618
Cdd:cd09236 251 HFEDLFDKRLAKYDKDLDAVSEEAQEQEEILQQIEVANKAFLQSRKGDPA----TKERERALQSLDLAYFKYKEIVSNLD 326

                ....*....
gi 6324849  619 AGTAFYENL 627
Cdd:cd09236 327 EGRKFYNDL 335
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
23-316 4.60e-12

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: 67.80  E-value: 4.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   23 KLIDTTSFQTASFFQSDILKVVDARNNAIApdISIDGLSA---------------LKEYYVILLQLEKKFP----NNQIE 83
Cdd:cd09247  10 KIVFEKTFQARDSLTLEQLKELSLRRRAII--ESINGSPFialaiarekaqylpyLEGYLPALENLVNHRDkvqlNEQLS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849   84 FTWFQTL-SQKSRGTSQY-SLQWEKLTIIYNIGcmYSLLALNSNNDAAESLKTSCLYFQNAAGCFKHVL-DHQKNLETIP 160
Cdd:cd09247  88 FRWTSGLgSSKGPKAFQSdSLRFELGMVLFLYG--AALRERASEVLPTEDFKEAATHLRRAAGVFEFLAhDELPRLRGAL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  161 VVDDaTLNALTSLM--------LAQAQECFWFKAVQDKHKDSLIAKLSQQIVDFYCEAIN----DAQRGKLIRSDWINHL 228
Cdd:cd09247 166 SADE-RPPECTPSLalamsllcLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEAKNvlrsLATDLKDLDPRFLRFI 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  229 KAKKAYFSAVTYYRIALSFNEKKQFGNVVKALQMGLQFINEST----LSSQAKFKTVVESSLKEAQ---RDNEFIYLQEV 301
Cdd:cd09247 245 SSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKLpgsdISSPVIFRDERAEVATLLQkyeKENEVIYFEKV 324
                       330
                ....*....|....*..
gi 6324849  302 P--SELPSIKPALMVKP 316
Cdd:cd09247 325 PdiDELPLPEGKVIVKP 341
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
371-645 7.80e-05

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: 45.16  E-value: 7.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  371 LKESLTTFQIPQGLtkvseaelSHYQASLNNLLINNKNVQVQLDNIEQILNEEAFTDNQLRLKHGTlNWTLPESSTTNTA 450
Cdd:cd09238  61 LDEEVEAVQISGGL--------AALEGELPRLRELRRVCTELLAAAQESLEAEATEDSAARTQYGT-AWTRPPSATLTKN 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  451 YYEKLKKLRGYLDEGSAIDKQtneLFQSIDKNLIGSEI---RLPESNDPLTNKIKMIIQERNDYI--------------- 512
Cdd:cd09238 132 LWERLNRFRVNLEQAGDSDES---LRRRIEDAMDGMLIlddEPAAAAAPTLRAPMLSTDEDDASIvgtlrsnleelealg 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  513 -------DRTRRKSSEYRILPKIITSykkngTVDFEPIFIGHLKYFDEDLRYVNSTKEENIKLIEEVnlsKKNNPGRSGI 585
Cdd:cd09238 209 neragieDMMKALKRNDNILAKVMAT-----TGSYDALFKEELKKYDSVREAVSKNISSQDDLLSRL---RALNEKFSQI 280
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324849  586 EPKKMVRIDPRELYiEDLRYSFKLLDEVKENLSAGTAFYENLITSTSNLYNEVQEYDTAR 645
Cdd:cd09238 281 FDVEGWRAATESHA-TQIRAAVAKYRELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR 339
 
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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