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Conserved domains on  [gi|189204001|ref|XP_001938336|]
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pH-response regulator protein palC [Pyrenophora tritici-repentis Pt-1C-BFP]

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; ...
2-420 0e+00

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: 547.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   2 PFPFVLPTTSSISFIDYFNSSTHPSLPNCATTARGVLRDVLKRHKRIPPPSQASNLSTVLSALNDYIPYLFALDAGLSGT 81
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQASNLLTVVKALEEYLPYLLAIDACLSHD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  82 scageevDLVLVKELEIEWRSTLGSSiPGREPARVKLKGLESELCFTLSTLAYVYSLQARAQLHTLYNATV------PSP 155
Cdd:cd09245   81 -------ELILKSEPTFEWRTTLSST-SGRESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGAYETdrsisdASR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 156 EQRATAIGAAMKHFLEADSIHTYLANRAGQHNAQ-----PAAVDISAPMLGALAELTMAEATLITVLKDDPYPAVViedr 230
Cdd:cd09245  153 KQRDERLKAATKLLCKAAGIFDYLATRVLPQWESnrggaPPPPDLSPEVLSALSSLALAEATLLAVRKLDPYPAAV---- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 231 nkqSKDWMFRGVEIPKVRA--HLFARLCLASSEHAAKAQAMLGRSP------KINDDLLKYVDDLRRTAKGKACRFLACD 302
Cdd:cd09245  229 ---DKDWMTPGPPLPKVHPsaHLLARLCLAASEHAESARALLSTPGskrgsgEVSEELLRYLSDLRRVARALACKFLGID 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 303 AEASAKTGEGIAWLRGAKKELGFASLGVESDKKAsgfsKLKKDWQEKREDRKIEKGvdwgtdAGKFEEGRIVDMLLKKWE 382
Cdd:cd09245  306 AGENGKVGEAIGWLRAAKKELEDLKSPSGVASKA----KLKKSWKEKREDRKVEKG------AGVEEELRTLEMLLKKYK 375
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 189204001 383 KQNDTVGVQVIPPSEPLLASMPSGREYHTTKMFVVPAL 420
Cdd:cd09245  376 KMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS 413
 
Name Accession Description Interval E-value
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
2-420 0e+00

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: 547.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   2 PFPFVLPTTSSISFIDYFNSSTHPSLPNCATTARGVLRDVLKRHKRIPPPSQASNLSTVLSALNDYIPYLFALDAGLSGT 81
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQASNLLTVVKALEEYLPYLLAIDACLSHD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  82 scageevDLVLVKELEIEWRSTLGSSiPGREPARVKLKGLESELCFTLSTLAYVYSLQARAQLHTLYNATV------PSP 155
Cdd:cd09245   81 -------ELILKSEPTFEWRTTLSST-SGRESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGAYETdrsisdASR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 156 EQRATAIGAAMKHFLEADSIHTYLANRAGQHNAQ-----PAAVDISAPMLGALAELTMAEATLITVLKDDPYPAVViedr 230
Cdd:cd09245  153 KQRDERLKAATKLLCKAAGIFDYLATRVLPQWESnrggaPPPPDLSPEVLSALSSLALAEATLLAVRKLDPYPAAV---- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 231 nkqSKDWMFRGVEIPKVRA--HLFARLCLASSEHAAKAQAMLGRSP------KINDDLLKYVDDLRRTAKGKACRFLACD 302
Cdd:cd09245  229 ---DKDWMTPGPPLPKVHPsaHLLARLCLAASEHAESARALLSTPGskrgsgEVSEELLRYLSDLRRVARALACKFLGID 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 303 AEASAKTGEGIAWLRGAKKELGFASLGVESDKKAsgfsKLKKDWQEKREDRKIEKGvdwgtdAGKFEEGRIVDMLLKKWE 382
Cdd:cd09245  306 AGENGKVGEAIGWLRAAKKELEDLKSPSGVASKA----KLKKSWKEKREDRKVEKG------AGVEEELRTLEMLLKKYK 375
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 189204001 383 KQNDTVGVQVIPPSEPLLASMPSGREYHTTKMFVVPAL 420
Cdd:cd09245  376 KMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS 413
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
3-401 5.79e-33

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: 128.62  E-value: 5.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001     3 FPFVLPTTSSISFIDYFNSSTHPSLPncatTARGVLRDVLKRHKRIPppSQASNLS---TVLSALNDYIPYLFALDAGLS 79
Cdd:smart01041   2 IPLPLKETKEVDFSKPLKDYIKETYS----EDSSSYEDEIAELNRLR--QAARTPSrdeSGLELLLKYYGQLEALELRFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001    80 GTScageevdlvLVKELEIEWRSTLGSSipgrepARVKLKGLESELCFTLSTLAYVYSLQARAQLHTlynatvpSPEQRA 159
Cdd:smart01041  76 PPE---------GQLKLSFTWYDSLDTG------VPSTQSSLAFEKASVLFNLGALYSQIAAEQNRD-------TEEGLK 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   160 TAIgaamKHFLEADSIHTYLANRAGQHNAQPAAVDISAPMLGALAELTMAEATLITVLKddpypavVIEDrnkqskdwmf 239
Cdd:smart01041 134 EAC----KAFQQAAGVFNYLKENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEK-------AILD---------- 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   240 rgveIPKVRAHLFARLCLASSEHAAKAQAMLGRSP----KINDDLLKYVDDLRRTAKGKACRFLACDAEASAKTGEGIAW 315
Cdd:smart01041 193 ----GMKNKDSLIAKLAAQAAEYYEEALKALQTSEpvkgYIPKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIAR 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   316 LRGAKKELgfaslgvesdKKAsgfsklkkdwQEKREDRKIEKGVDWGTDAGKFEEgrIVDMLLKKWEKQNDTVGVQVIPP 395
Cdd:smart01041 269 LQEALERL----------KEA----------KKHLRCKKLGKADKLQEDLSGLKD--VVEEKLKEAEKDNDFIYHERVPD 326

                   ....*.
gi 189204001   396 SEPLLA 401
Cdd:smart01041 327 IVSLPP 332
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
96-399 9.82e-07

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: 50.66  E-value: 9.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   96 LEIEWRSTLGSSIPgrepaRVKLKGLESELCFTLSTLAYVYSLQARAQlhtlynatvpspeQRATAIG--AAMKHFLEAD 173
Cdd:pfam03097  84 IEFTWYDAFGTSSK-----KVSQSSLAFEKASVLFNIAALYSQLAASQ-------------NRSTDEGlkRACKYFQQAA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  174 SIHTYLANragqHNAQPAAVDISAPMLGALAELTMAEATLITVLKddpypavVIEDRNKQSkdwmfrgveipkvrahLFA 253
Cdd:pfam03097 146 GCFQYLKE----NFLHAPSPDLSPETLKALSNLMLAQAQECFWEK-------AINDNKKDS----------------LIA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  254 RLCLASSEHAAKAQAMLGRSPKINDDLLKYVddlrrTAK-----GKACRFLACDAEASAKTGEGIAWLRGAKKELgfasl 328
Cdd:pfam03097 199 KLAAQVSELYEEALEALKLSGLIDKEWISHV-----QAKahhfkALAQYRQALDDEEAKKYGEEIARLQLALSLL----- 268
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189204001  329 gvESDKKASGFSKLKKDWQEKREdrKIEKgvdwgtdagkfeegrivdmLLKKWEKQNDTVGVQVIPPSEPL 399
Cdd:pfam03097 269 --KEALKSDRYKKVLEDLKGLLD--VVEE-------------------KLKRAEKDNDFIYHERVPSESSL 316
 
Name Accession Description Interval E-value
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
2-420 0e+00

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: 547.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   2 PFPFVLPTTSSISFIDYFNSSTHPSLPNCATTARGVLRDVLKRHKRIPPPSQASNLSTVLSALNDYIPYLFALDAGLSGT 81
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQASNLLTVVKALEEYLPYLLAIDACLSHD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  82 scageevDLVLVKELEIEWRSTLGSSiPGREPARVKLKGLESELCFTLSTLAYVYSLQARAQLHTLYNATV------PSP 155
Cdd:cd09245   81 -------ELILKSEPTFEWRTTLSST-SGRESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGAYETdrsisdASR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 156 EQRATAIGAAMKHFLEADSIHTYLANRAGQHNAQ-----PAAVDISAPMLGALAELTMAEATLITVLKDDPYPAVViedr 230
Cdd:cd09245  153 KQRDERLKAATKLLCKAAGIFDYLATRVLPQWESnrggaPPPPDLSPEVLSALSSLALAEATLLAVRKLDPYPAAV---- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 231 nkqSKDWMFRGVEIPKVRA--HLFARLCLASSEHAAKAQAMLGRSP------KINDDLLKYVDDLRRTAKGKACRFLACD 302
Cdd:cd09245  229 ---DKDWMTPGPPLPKVHPsaHLLARLCLAASEHAESARALLSTPGskrgsgEVSEELLRYLSDLRRVARALACKFLGID 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 303 AEASAKTGEGIAWLRGAKKELGFASLGVESDKKAsgfsKLKKDWQEKREDRKIEKGvdwgtdAGKFEEGRIVDMLLKKWE 382
Cdd:cd09245  306 AGENGKVGEAIGWLRAAKKELEDLKSPSGVASKA----KLKKSWKEKREDRKVEKG------AGVEEELRTLEMLLKKYK 375
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 189204001 383 KQNDTVGVQVIPPSEPLLASMPSGREYHTTKMFVVPAL 420
Cdd:cd09245  376 KMNDTVSFQPVPPSSELQSSMPSGREAHTAKPYTPPPS 413
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
3-401 5.79e-33

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: 128.62  E-value: 5.79e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001     3 FPFVLPTTSSISFIDYFNSSTHPSLPncatTARGVLRDVLKRHKRIPppSQASNLS---TVLSALNDYIPYLFALDAGLS 79
Cdd:smart01041   2 IPLPLKETKEVDFSKPLKDYIKETYS----EDSSSYEDEIAELNRLR--QAARTPSrdeSGLELLLKYYGQLEALELRFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001    80 GTScageevdlvLVKELEIEWRSTLGSSipgrepARVKLKGLESELCFTLSTLAYVYSLQARAQLHTlynatvpSPEQRA 159
Cdd:smart01041  76 PPE---------GQLKLSFTWYDSLDTG------VPSTQSSLAFEKASVLFNLGALYSQIAAEQNRD-------TEEGLK 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   160 TAIgaamKHFLEADSIHTYLANRAGQHNAQPAAVDISAPMLGALAELTMAEATLITVLKddpypavVIEDrnkqskdwmf 239
Cdd:smart01041 134 EAC----KAFQQAAGVFNYLKENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEK-------AILD---------- 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   240 rgveIPKVRAHLFARLCLASSEHAAKAQAMLGRSP----KINDDLLKYVDDLRRTAKGKACRFLACDAEASAKTGEGIAW 315
Cdd:smart01041 193 ----GMKNKDSLIAKLAAQAAEYYEEALKALQTSEpvkgYIPKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIAR 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   316 LRGAKKELgfaslgvesdKKAsgfsklkkdwQEKREDRKIEKGVDWGTDAGKFEEgrIVDMLLKKWEKQNDTVGVQVIPP 395
Cdd:smart01041 269 LQEALERL----------KEA----------KKHLRCKKLGKADKLQEDLSGLKD--VVEEKLKEAEKDNDFIYHERVPD 326

                   ....*.
gi 189204001   396 SEPLLA 401
Cdd:smart01041 327 IVSLPP 332
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
3-399 2.00e-23

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: 100.89  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   3 FPFVLPTTSSISFIDYFNSSTHPSLP-NCATTARGVLRDVLKRHKRIP-PPSQASNLSTVLSALNDYIPYLFALDAGLSG 80
Cdd:cd09034    2 IGLPLKKTKEVDVKVPLSKFIPKNYGeLEATAVEDLIEKLSKLRNNIVtEQNNDTTCENLLEALKEYLPYLLGLEKKLPF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  81 TscageevdlVLVKELEIEWRSTLgssipgrEPARVKLKGLESELCFTLSTLAYVYSLQARAQLHTlynatvPSPEQRAT 160
Cdd:cd09034   82 Q---------KLRDNVEFTWTDSF-------DTKKESATSLRYELLSILFNLAALASQLANEKLIT------GSEEDLKQ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 161 AIgaamKHFLEADSIHTYLANRAGQHNAQPAAVDISAPMLGALAELTMAEATLITVLKDdpypavviedrnkqskdwmfr 240
Cdd:cd09034  140 AI----KSLQKAAGYFEYLKEHVLPLPPDELPVDLTEAVLSALSLIMLAQAQECFLLKA--------------------- 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 241 gVEIPKVRAHLFARLCLASSEHAAKAQAMLGRSPK-----INDDLLKYVDDLRRTAKGKACRFLACDAEASAKTGEGIAW 315
Cdd:cd09034  195 -EEDKKAKLSLLARLACEAAKYYEEALKCLSGVDLetiknIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIAR 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 316 LRGAKKELGfaslgvESDKKASGFSKLKKDWQeKREDRKIEKgvdwgtdagkfeegrivdmLLKKWEKQNDTVGVQVIPP 395
Cdd:cd09034  274 LQAALELLK------ESERLCKSFLLDVWGNL-KKLKEKIEK-------------------ELEKAERENDFIYFEEVPP 327

                 ....
gi 189204001 396 SEPL 399
Cdd:cd09034  328 EDPL 331
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
42-395 8.03e-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: 66.26  E-value: 8.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  42 LKRHKRIPPPSQASNLSTVLSAL-NDYIPYLFALDAGLSgtSCAGEEVDLVLVKELEIEWRSTLGSSipgREPARVKLKG 120
Cdd:cd09247   33 LRRRAIIESINGSPFIALAIAREkAQYLPYLEGYLPALE--NLVNHRDKVQLNEQLSFRWTSGLGSS---KGPKAFQSDS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 121 LESELCFTLSTlaYVYSLQARAqlhtlynatvpSPEQRATAIGAAMKHFLEADSIHTYLANRA-----GQHNAQPAAVDI 195
Cdd:cd09247  108 LRFELGMVLFL--YGAALRERA-----------SEVLPTEDFKEAATHLRRAAGVFEFLAHDElprlrGALSADERPPEC 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 196 SAPMLGALAELTMAEATLITVLKddpypavviedrnkqskdwmfrgVEIPKVRAHLFARLCLASSEHAAKAQAML----G 271
Cdd:cd09247  175 TPSLALAMSLLCLAEAQAVTARK-----------------------AEEKGTSPSLLAKLHYGATQFLEEAKNVLrslaT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 272 RSPKINDDLLKYVDDLRRTAKGKACRFLACDAEASAKTGEGIAWLRGAKKELGFASLGvESDKKASGFSKLKKDwqekre 351
Cdd:cd09247  232 DLKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKLPG-SDISSPVIFRDERAE------ 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 189204001 352 drkiekgvdwgtdagkfeegriVDMLLKKWEKQNDTVGVQVIPP 395
Cdd:cd09247  305 ----------------------VATLLQKYEKENEVIYFEKVPD 326
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
96-399 9.82e-07

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: 50.66  E-value: 9.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001   96 LEIEWRSTLGSSIPgrepaRVKLKGLESELCFTLSTLAYVYSLQARAQlhtlynatvpspeQRATAIG--AAMKHFLEAD 173
Cdd:pfam03097  84 IEFTWYDAFGTSSK-----KVSQSSLAFEKASVLFNIAALYSQLAASQ-------------NRSTDEGlkRACKYFQQAA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  174 SIHTYLANragqHNAQPAAVDISAPMLGALAELTMAEATLITVLKddpypavVIEDRNKQSkdwmfrgveipkvrahLFA 253
Cdd:pfam03097 146 GCFQYLKE----NFLHAPSPDLSPETLKALSNLMLAQAQECFWEK-------AINDNKKDS----------------LIA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001  254 RLCLASSEHAAKAQAMLGRSPKINDDLLKYVddlrrTAK-----GKACRFLACDAEASAKTGEGIAWLRGAKKELgfasl 328
Cdd:pfam03097 199 KLAAQVSELYEEALEALKLSGLIDKEWISHV-----QAKahhfkALAQYRQALDDEEAKKYGEEIARLQLALSLL----- 268
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189204001  329 gvESDKKASGFSKLKKDWQEKREdrKIEKgvdwgtdagkfeegrivdmLLKKWEKQNDTVGVQVIPPSEPL 399
Cdd:pfam03097 269 --KEALKSDRYKKVLEDLKGLLD--VVEE-------------------KLKRAEKDNDFIYHERVPSESSL 316
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
193-399 2.21e-03

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: 39.96  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 193 VDISAPMLGALAELTMAEATLITVLKddpypavVIEDRNKQSKdwmfrgveipkvrAHLFARLCLASSEHAAKAQAMLGr 272
Cdd:cd09242  159 VDLQQENVKFLVKLMLAQAQEIFLLK-------LINGDDAQKK-------------ASLISKLASATANLYESCVEFLK- 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189204001 273 spKINDDLLKYVD-DLRRTAKGKACRFLACDA-------EASAKTGEGIAWLRGAKKELgfaslgVESDKKASGFSKLKK 344
Cdd:cd09242  218 --EIQEKGISYGDpKWISLVQCKAHYYKSLAAyyhalalEAAGKYGEAIAYLTQAESIL------KEANPQKLSLKASAG 289
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189204001 345 DwqEKREDRKIEKGvdwgtdagkFEEgrIVDMLLKKWEKQNDTVGVQVIPPSEPL 399
Cdd:cd09242  290 D--AAYALNDDFKG---------QKD--TVEEKLKELEKDNDFIYHDIVPSEVTL 331
 
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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