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Conserved domains on  [gi|274130232|emb|CAZ04931|]
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Rim23 protein [Mycosarcoma maydis]

Protein Classification

BRO1 domain-containing protein( domain architecture ID 10174124)

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_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
1-550 4.20e-164

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: 474.97  E-value: 4.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   1 MYMFELATTGSISFSDFLVTTELVSQVSEATQLRARLRGVLKQNRAGQSGSVgkhvgsyneqrgtssgsqaagdddcras 80
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQ---------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  81 atsvnAADWLTIVKTIEEYLPHLLGVFNCVQTDDLIVRYEPVFSWRTSISGTRFRGAQRIALGGLHYELASTLLTYALAL 160
Cdd:cd09245   53 -----ASNLLTVVKALEEYLPYLLAIDACLSHDELILKSEPTFEWRTTLSSTSGRESPRLPLPGLHYELAFVLLTYAYAL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 161 SNLSAATVASLGWYERDRSLSLDQRKRNDERLKWAADTLCRAAGILLYLSTQLIPKWSDHVGsLDGLPPDLTTEATLALS 240
Cdd:cd09245  128 SNLARSILAPLGAYETDRSISDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNRG-GAPPPPDLSPEVLSALS 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 241 NVCMAQAQALAIRKLVSPSIAKAVDTLTPGPPLDKNHPSASLLAKLHLNVVEQMESAVALLKTIADKRrrksanhagtqi 320
Cdd:cd09245  207 SLALAEATLLAVRKLDPYPAAVDKDWMTPGPPLPKVHPSAHLLARLCLAASEHAESARALLSTPGSKR------------ 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 321 glsanhehelasrlsasrdradhehdddmvetnrgagaqatskrnkllgrfklgssksspprsasvhsgphdvarssghl 400
Cdd:cd09245      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 401 sastagapvdCDVEISSSLLKYLGFGAAFHRSMAYKWLAIDHGEsSSRIGTAIAYLSLSSALLSSSTMRDGAPSHALIPS 480
Cdd:cd09245  275 ----------GSGEVSEELLRYLSDLRRVARALACKFLGIDAGE-NGKVGEAIGWLRAAKKELEDLKSPSGVASKAKLKK 343
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 481 SLLLNKSTKSGSAGGVVEQELATVTHWLVSYRKLNDTVAFQRVPASDEVTSNVPAGRPALGAKPYTLPSP 550
Cdd:cd09245  344 SWKEKREDRKVEKGAGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS 413
 
Name Accession Description Interval E-value
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
1-550 4.20e-164

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: 474.97  E-value: 4.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   1 MYMFELATTGSISFSDFLVTTELVSQVSEATQLRARLRGVLKQNRAGQSGSVgkhvgsyneqrgtssgsqaagdddcras 80
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQ---------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  81 atsvnAADWLTIVKTIEEYLPHLLGVFNCVQTDDLIVRYEPVFSWRTSISGTRFRGAQRIALGGLHYELASTLLTYALAL 160
Cdd:cd09245   53 -----ASNLLTVVKALEEYLPYLLAIDACLSHDELILKSEPTFEWRTTLSSTSGRESPRLPLPGLHYELAFVLLTYAYAL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 161 SNLSAATVASLGWYERDRSLSLDQRKRNDERLKWAADTLCRAAGILLYLSTQLIPKWSDHVGsLDGLPPDLTTEATLALS 240
Cdd:cd09245  128 SNLARSILAPLGAYETDRSISDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNRG-GAPPPPDLSPEVLSALS 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 241 NVCMAQAQALAIRKLVSPSIAKAVDTLTPGPPLDKNHPSASLLAKLHLNVVEQMESAVALLKTIADKRrrksanhagtqi 320
Cdd:cd09245  207 SLALAEATLLAVRKLDPYPAAVDKDWMTPGPPLPKVHPSAHLLARLCLAASEHAESARALLSTPGSKR------------ 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 321 glsanhehelasrlsasrdradhehdddmvetnrgagaqatskrnkllgrfklgssksspprsasvhsgphdvarssghl 400
Cdd:cd09245      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 401 sastagapvdCDVEISSSLLKYLGFGAAFHRSMAYKWLAIDHGEsSSRIGTAIAYLSLSSALLSSSTMRDGAPSHALIPS 480
Cdd:cd09245  275 ----------GSGEVSEELLRYLSDLRRVARALACKFLGIDAGE-NGKVGEAIGWLRAAKKELEDLKSPSGVASKAKLKK 343
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 481 SLLLNKSTKSGSAGGVVEQELATVTHWLVSYRKLNDTVAFQRVPASDEVTSNVPAGRPALGAKPYTLPSP 550
Cdd:cd09245  344 SWKEKREDRKVEKGAGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS 413
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
28-556 2.12e-27

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: 114.37  E-value: 2.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232    28 SEATQLRARLRGVLKQNRAGQSGSVGKHVGSYNEQRgtssgsQAAGDDDCRASATSVNAAdWLTIVKTIEEYLPHLLGVF 107
Cdd:smart01041   9 TKEVDFSKPLKDYIKETYSEDSSSYEDEIAELNRLR------QAARTPSRDESGLELLLK-YYGQLEALELRFPPPEGQL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   108 NcvqtddlivryePVFSWRTSisgtrFRGAQRIALGGLHYELASTLLTYALALSNLSAAtvaslgwyerdrslsldQRKR 187
Cdd:smart01041  82 K------------LSFTWYDS-----LDTGVPSTQSSLAFEKASVLFNLGALYSQIAAE-----------------QNRD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   188 NDERLKWAADTLCRAAGILLYLSTQLIPKWSdhvgslDGLPPDLTTEATLALSNVCMAQAQALAIRKLVSPSIAKavdtl 267
Cdd:smart01041 128 TEEGLKEACKAFQQAAGVFNYLKENFLHALS------TEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKN----- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   268 tpgppldknhpSASLLAKLHLNVVEQMESAVALLKTiadkrrrksanhagtqiglsanhehelasrlsasrdradhehdd 347
Cdd:smart01041 197 -----------KDSLIAKLAAQAAEYYEEALKALQT-------------------------------------------- 221
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   348 dmvetnrgagaqatskrnkllgrfklgssksspprSASVHSGphdvarssghlsastagapvdcdveISSSLLKYLGFGA 427
Cdd:smart01041 222 -----------------------------------SEPVKGY-------------------------IPKSWIKLVQVKA 241
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   428 AFHRSMAYKWLAIDHgESSSRIGTAIAYlslssallssstMRDGAPSHALIPSSLLLNKSTKSGSAGGVVEQELATVTHW 507
Cdd:smart01041 242 HHFKALAHYYQALDL-EEANKYGEAIAR------------LQEALERLKEAKKHLRCKKLGKADKLQEDLSGLKDVVEEK 308
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 274130232   508 LVSYRKLNDTVAFQRVPASD--EVTSNVPAGRPALGAKPYTLPSP--AWGPAS 556
Cdd:smart01041 309 LKEAEKDNDFIYHERVPDIVslPPIKKAPLVKPPPFSEVLKGPDLfaKLVPMA 361
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
123-309 9.07e-10

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: 60.67  E-value: 9.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  123 FSWRTSISGTRfrgaQRIALGGLHYELASTLltYalalsNLsAATVASLGwyerdrslsLDQRKRNDERLKWAADTLCRA 202
Cdd:pfam03097  86 FTWYDAFGTSS----KKVSQSSLAFEKASVL--F-----NI-AALYSQLA---------ASQNRSTDEGLKRACKYFQQA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  203 AGILLYLSTQLipkwsdhvgsLDGLPPDLTTEATLALSNVCMAQAQALAIRKLVspsiakavdtltpgppldKNHPSASL 282
Cdd:pfam03097 145 AGCFQYLKENF----------LHAPSPDLSPETLKALSNLMLAQAQECFWEKAI------------------NDNKKDSL 196
                         170       180
                  ....*....|....*....|....*..
gi 274130232  283 LAKLHLNVVEQMESAVALLKTIADKRR 309
Cdd:pfam03097 197 IAKLAAQVSELYEEALEALKLSGLIDK 223
 
Name Accession Description Interval E-value
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
1-550 4.20e-164

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: 474.97  E-value: 4.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   1 MYMFELATTGSISFSDFLVTTELVSQVSEATQLRARLRGVLKQNRAGQSGSVgkhvgsyneqrgtssgsqaagdddcras 80
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQ---------------------------- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  81 atsvnAADWLTIVKTIEEYLPHLLGVFNCVQTDDLIVRYEPVFSWRTSISGTRFRGAQRIALGGLHYELASTLLTYALAL 160
Cdd:cd09245   53 -----ASNLLTVVKALEEYLPYLLAIDACLSHDELILKSEPTFEWRTTLSSTSGRESPRLPLPGLHYELAFVLLTYAYAL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 161 SNLSAATVASLGWYERDRSLSLDQRKRNDERLKWAADTLCRAAGILLYLSTQLIPKWSDHVGsLDGLPPDLTTEATLALS 240
Cdd:cd09245  128 SNLARSILAPLGAYETDRSISDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNRG-GAPPPPDLSPEVLSALS 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 241 NVCMAQAQALAIRKLVSPSIAKAVDTLTPGPPLDKNHPSASLLAKLHLNVVEQMESAVALLKTIADKRrrksanhagtqi 320
Cdd:cd09245  207 SLALAEATLLAVRKLDPYPAAVDKDWMTPGPPLPKVHPSAHLLARLCLAASEHAESARALLSTPGSKR------------ 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 321 glsanhehelasrlsasrdradhehdddmvetnrgagaqatskrnkllgrfklgssksspprsasvhsgphdvarssghl 400
Cdd:cd09245      --------------------------------------------------------------------------------
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 401 sastagapvdCDVEISSSLLKYLGFGAAFHRSMAYKWLAIDHGEsSSRIGTAIAYLSLSSALLSSSTMRDGAPSHALIPS 480
Cdd:cd09245  275 ----------GSGEVSEELLRYLSDLRRVARALACKFLGIDAGE-NGKVGEAIGWLRAAKKELEDLKSPSGVASKAKLKK 343
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 481 SLLLNKSTKSGSAGGVVEQELATVTHWLVSYRKLNDTVAFQRVPASDEVTSNVPAGRPALGAKPYTLPSP 550
Cdd:cd09245  344 SWKEKREDRKVEKGAGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS 413
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
28-556 2.12e-27

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: 114.37  E-value: 2.12e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232    28 SEATQLRARLRGVLKQNRAGQSGSVGKHVGSYNEQRgtssgsQAAGDDDCRASATSVNAAdWLTIVKTIEEYLPHLLGVF 107
Cdd:smart01041   9 TKEVDFSKPLKDYIKETYSEDSSSYEDEIAELNRLR------QAARTPSRDESGLELLLK-YYGQLEALELRFPPPEGQL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   108 NcvqtddlivryePVFSWRTSisgtrFRGAQRIALGGLHYELASTLLTYALALSNLSAAtvaslgwyerdrslsldQRKR 187
Cdd:smart01041  82 K------------LSFTWYDS-----LDTGVPSTQSSLAFEKASVLFNLGALYSQIAAE-----------------QNRD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   188 NDERLKWAADTLCRAAGILLYLSTQLIPKWSdhvgslDGLPPDLTTEATLALSNVCMAQAQALAIRKLVSPSIAKavdtl 267
Cdd:smart01041 128 TEEGLKEACKAFQQAAGVFNYLKENFLHALS------TEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKN----- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   268 tpgppldknhpSASLLAKLHLNVVEQMESAVALLKTiadkrrrksanhagtqiglsanhehelasrlsasrdradhehdd 347
Cdd:smart01041 197 -----------KDSLIAKLAAQAAEYYEEALKALQT-------------------------------------------- 221
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   348 dmvetnrgagaqatskrnkllgrfklgssksspprSASVHSGphdvarssghlsastagapvdcdveISSSLLKYLGFGA 427
Cdd:smart01041 222 -----------------------------------SEPVKGY-------------------------IPKSWIKLVQVKA 241
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232   428 AFHRSMAYKWLAIDHgESSSRIGTAIAYlslssallssstMRDGAPSHALIPSSLLLNKSTKSGSAGGVVEQELATVTHW 507
Cdd:smart01041 242 HHFKALAHYYQALDL-EEANKYGEAIAR------------LQEALERLKEAKKHLRCKKLGKADKLQEDLSGLKDVVEEK 308
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 274130232   508 LVSYRKLNDTVAFQRVPASD--EVTSNVPAGRPALGAKPYTLPSP--AWGPAS 556
Cdd:smart01041 309 LKEAEKDNDFIYHERVPDIVslPPIKKAPLVKPPPFSEVLKGPDLfaKLVPMA 361
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
78-302 7.01e-19

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: 88.22  E-value: 7.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  78 RASATSVNAADWLTIVKTIE--EYLPHLLG----VFNCVQTDDLIVRYEP-VFSWrTSISGTRfRGAQRIALGGLHYELA 150
Cdd:cd09247   36 RAIIESINGSPFIALAIAREkaQYLPYLEGylpaLENLVNHRDKVQLNEQlSFRW-TSGLGSS-KGPKAFQSDSLRFELG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 151 STLLTYALALsnlsaatvaslgwyeRDRSLsldqRKRNDERLKWAADTLCRAAGILLYLSTQLIPKWSDHvGSLDGLPPD 230
Cdd:cd09247  114 MVLFLYGAAL---------------RERAS----EVLPTEDFKEAATHLRRAAGVFEFLAHDELPRLRGA-LSADERPPE 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 274130232 231 LTTEATLALSNVCMAQAQALAIRK-LVSPsiakavdtltpgppldknhPSASLLAKLHLNVVEQMESAVALLK 302
Cdd:cd09247  174 CTPSLALAMSLLCLAEAQAVTARKaEEKG-------------------TSPSLLAKLHYGATQFLEEAKNVLR 227
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
77-305 4.22e-15

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: 77.00  E-value: 4.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  77 CRASATSVNAADWLTIVKTIEEYLPHLLGV---FNCVQtddliVRYEPVFSWRTSISGTRFRGAQrialggLHYELASTL 153
Cdd:cd09034   46 NNIVTEQNNDTTCENLLEALKEYLPYLLGLekkLPFQK-----LRDNVEFTWTDSFDTKKESATS------LRYELLSIL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 154 LTYALALSNLsAATVAslgwyerdrslsldqRKRNDERLKWAADTLCRAAGILLYLSTQLIPKwsdhvgSLDGLPPDLTT 233
Cdd:cd09034  115 FNLAALASQL-ANEKL---------------ITGSEEDLKQAIKSLQKAAGYFEYLKEHVLPL------PPDELPVDLTE 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 274130232 234 EATLALSNVCMAQAQALAIRKLVSPSIAKavdtltpgppldknhpsASLLAKLHLNVVEQMESAVALLKTIA 305
Cdd:cd09034  173 AVLSALSLIMLAQAQECFLLKAEEDKKAK-----------------LSLLARLACEAAKYYEEALKCLSGVD 227
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
123-309 9.07e-10

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: 60.67  E-value: 9.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  123 FSWRTSISGTRfrgaQRIALGGLHYELASTLltYalalsNLsAATVASLGwyerdrslsLDQRKRNDERLKWAADTLCRA 202
Cdd:pfam03097  86 FTWYDAFGTSS----KKVSQSSLAFEKASVL--F-----NI-AALYSQLA---------ASQNRSTDEGLKRACKYFQQA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232  203 AGILLYLSTQLipkwsdhvgsLDGLPPDLTTEATLALSNVCMAQAQALAIRKLVspsiakavdtltpgppldKNHPSASL 282
Cdd:pfam03097 145 AGCFQYLKENF----------LHAPSPDLSPETLKALSNLMLAQAQECFWEKAI------------------NDNKKDSL 196
                         170       180
                  ....*....|....*....|....*..
gi 274130232  283 LAKLHLNVVEQMESAVALLKTIADKRR 309
Cdd:pfam03097 197 IAKLAAQVSELYEEALEALKLSGLIDK 223
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
123-340 1.86e-06

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: 50.47  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 123 FSWRTSisgtrFRGAQRIALGGLHYELASTLLTYALALSNLSAATvaslgwyerDRSlsldqrkrNDERLKWAADTLCRA 202
Cdd:cd09246   89 FSWYDA-----FRPHRKATQANVHFEKAAVLFNLGALSSQLGLQQ---------DRT--------TAEGIKQACHAFQAA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 203 AGILLYLSTQLIPKwsdhvgSLDGLPPDLTTEATLALSNVCMAQAQAL----AIRKLVSPSIA-----------KAVDTL 267
Cdd:cd09246  147 AGAFAHLRDKVSGK------TGGFRTPDLTAECLGMLESLMLAQAQECfyekAVADGKSPAVCsklakqarsyyEEALEA 220
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 274130232 268 TPGPPLdKNHPSASLLAklHLNVVEQMESAVALlktiadkrrRKSAN--HAGTQIGlsanhehELASRLSASRDR 340
Cdd:cd09246  221 LDSPPL-KGHFDKSWVA--HVQLKAAYFRAEAL---------YRAAKdlHEKEDIG-------EEIARLRAASDA 276
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
123-297 2.07e-06

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: 50.34  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 123 FSWRTSISGTRFRgaqRIALGGLHYELASTLLtyalalsNLsAATVASLGWYERDRSlsldqrkrnDERLKWAADTLCRA 202
Cdd:cd09241   82 FTWYPTLGYKSSG---PVSLSSLKFERANILY-------NL-GALYSQLALSENRYT---------DEGLKRACSYFQAS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 203 AGILLYLSTQLIPKWSDhvgsldglPPDLTTEATLALSNVCMAQAQALairklvspSIAKAVdtltpgppldKNHPSASL 282
Cdd:cd09241  142 AGCFEYILQHLLPTLSP--------PPDLDENTLKALESLMLAQAQEC--------FWQKAI----------SDGTKDSL 195
                        170
                 ....*....|....*
gi 274130232 283 LAKLHLNVVEQMESA 297
Cdd:cd09241  196 IAKLAAQVSDYYQEA 210
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
123-307 3.13e-04

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: 43.42  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 123 FSWRTSisgtrFRGAQRIALGGLHYELASTLLTYALALSNLSAatvaslgwyerdrslslDQRKRNDERLKWAADTLCRA 202
Cdd:cd09242   85 FTWYDA-----FYKSKKVKQHSLAFEKASVLFNIGALLSQLAA-----------------EKYREDEDDLKEAITNLQQA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 203 AGILLYLSTQLIpkwsdHVGSldglpPDLTTEATLALSNVCMAQAQALAIRKLVSpsiakavdtltpGPPLDKNhpsASL 282
Cdd:cd09242  143 AGCFQYINENFL-----HAPS-----VDLQQENVKFLVKLMLAQAQEIFLLKLIN------------GDDAQKK---ASL 197
                        170       180
                 ....*....|....*....|....*
gi 274130232 283 LAKLHLNVVEQMESAVALLKTIADK 307
Cdd:cd09242  198 ISKLASATANLYESCVEFLKEIQEK 222
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
123-254 7.14e-03

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: 38.82  E-value: 7.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 274130232 123 FSWRTSIS-GTRFRGAQRIALGGLHYELASTLLTYALALSNLSAAtvaslgwyerdrslsldQRKRNDERLKWAADTLCR 201
Cdd:cd09240   91 FTWKDAFDkGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAE-----------------QNLDTDEGLKLAAKLFQQ 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 274130232 202 AAGILLYLStqlipkwsDHVGSL--DGLPPDLTTEATLALSNVCMAQAQALAIRK 254
Cdd:cd09240  154 AAGIFNHLK--------ETVLSAlqQEPTPDLSPDTLSALSALMLAQAQEVFYLK 200
 
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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