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Conserved domains on  [gi|357528827|sp|Q9P905|]
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RecName: Full=pH-response regulator protein palC

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; ...
2-445 1.36e-160

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: 461.87  E-value: 1.36e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   2 VYPFELPTTSHLSFQSALSSHTHPSLPQSATTARHALRLALKAHNRLPRGFQrDSHLTSVLSAINDYLPYVVALAQGLNN 81
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQ-ASNLLTVVKALEEYLPYLLAIDACLSH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  82 GkpidtttpsttthleeiRVAQRAELEPEWRATLASSSLRrpSTNRTRGTGVQYELAFILTTLGYILSSLARSGVTRTLY 161
Cdd:cd09245   80 D-----------------ELILKSEPTFEWRTTLSSTSGR--ESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 162 AST-----TPSAEQRTAAVQTATKHLLQASTIHSFLSSSPYFATVSE---AATLPDLAPATQAALSSLALAEATLLTVLK 233
Cdd:cd09245  141 YETdrsisDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNrggAPPPPDLSPEVLSALSSLALAEATLLAVRK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 234 DDSYVVACiqarnpnDKDWMVRAPEIPKVRA--HLFARLCIRAAEYAEQAATGLSSVAAEGRKAGVDEDVARYAHVLGLV 311
Cdd:cd09245  221 LDPYPAAV-------DKDWMTPGPPLPKVHPsaHLLARLCLAASEHAESARALLSTPGSKRGSGEVSEELLRYLSDLRRV 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 312 ARARACRFFGVDAELAGKVGEGIAWLRAAKGALGLRNTGSASAEEVttksrglsKLKLGFrerreerkleKGAGGERVDK 391
Cdd:cd09245  294 ARALACKFLGIDAGENGKVGEAIGWLRAAKKELEDLKSPSGVASKA--------KLKKSW----------KEKREDRKVE 355
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 357528827 392 GGlgpgdnAGREEEGRVLEMLETKWVRANDTLNTQLIPSSADYVANLPSGRDVL 445
Cdd:cd09245  356 KG------AGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAH 403
 
Name Accession Description Interval E-value
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
2-445 1.36e-160

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: 461.87  E-value: 1.36e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   2 VYPFELPTTSHLSFQSALSSHTHPSLPQSATTARHALRLALKAHNRLPRGFQrDSHLTSVLSAINDYLPYVVALAQGLNN 81
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQ-ASNLLTVVKALEEYLPYLLAIDACLSH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  82 GkpidtttpsttthleeiRVAQRAELEPEWRATLASSSLRrpSTNRTRGTGVQYELAFILTTLGYILSSLARSGVTRTLY 161
Cdd:cd09245   80 D-----------------ELILKSEPTFEWRTTLSSTSGR--ESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 162 AST-----TPSAEQRTAAVQTATKHLLQASTIHSFLSSSPYFATVSE---AATLPDLAPATQAALSSLALAEATLLTVLK 233
Cdd:cd09245  141 YETdrsisDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNrggAPPPPDLSPEVLSALSSLALAEATLLAVRK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 234 DDSYVVACiqarnpnDKDWMVRAPEIPKVRA--HLFARLCIRAAEYAEQAATGLSSVAAEGRKAGVDEDVARYAHVLGLV 311
Cdd:cd09245  221 LDPYPAAV-------DKDWMTPGPPLPKVHPsaHLLARLCLAASEHAESARALLSTPGSKRGSGEVSEELLRYLSDLRRV 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 312 ARARACRFFGVDAELAGKVGEGIAWLRAAKGALGLRNTGSASAEEVttksrglsKLKLGFrerreerkleKGAGGERVDK 391
Cdd:cd09245  294 ARALACKFLGIDAGENGKVGEAIGWLRAAKKELEDLKSPSGVASKA--------KLKKSW----------KEKREDRKVE 355
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 357528827 392 GGlgpgdnAGREEEGRVLEMLETKWVRANDTLNTQLIPSSADYVANLPSGRDVL 445
Cdd:cd09245  356 KG------AGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAH 403
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
2-433 8.66e-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: 8.66e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827     2 VYPFELPTTSHLSFQSALSSHTHPSLPQsattARHALRLALKAHNRLPRGFQRDSHLTSVLSAINDYLPYVVALAQGLNN 81
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSE----DSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827    82 GkpidtttpsttthleeirvAQRAELEPEWRATLASSSlrrPSTNRTrgtgVQYELAFILTTLGYILSSLARSgvtrtly 161
Cdd:smart01041  77 P-------------------EGQLKLSFTWYDSLDTGV---PSTQSS----LAFEKASVLFNLGALYSQIAAE------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   162 asttpSAEQRTAAVQTATKHLLQASTIHSFLSSspyfaTVSEAA---TLPDLAPATQAALSSLALAEATLLTVLKddsyv 238
Cdd:smart01041 124 -----QNRDTEEGLKEACKAFQQAAGVFNYLKE-----NFLHALstePSVDLSPETLSALSSLMLAQAQECFFEK----- 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   239 vACIQARnpndkdwmvrapeipKVRAHLFARLCIRAAEYAEQAATGLSSVAAEgrKAGVDEDVARYAHVLGLVARARACR 318
Cdd:smart01041 189 -AILDGM---------------KNKDSLIAKLAAQAAEYYEEALKALQTSEPV--KGYIPKSWIKLVQVKAHHFKALAHY 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   319 FFGVDAELAGKVGEGIAWLRAAKGALGLrntgsASAEEVTTKSRGLSKLklgfrerreerklekgaggervdkgglgpGD 398
Cdd:smart01041 251 YQALDLEEANKYGEAIARLQEALERLKE-----AKKHLRCKKLGKADKL-----------------------------QE 296
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 357528827   399 NAGREEEgRVLEMLEtKWVRANDTLNTQLIPSSAD 433
Cdd:smart01041 297 DLSGLKD-VVEEKLK-EAEKDNDFIYHERVPDIVS 329
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
111-344 1.05e-05

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: 47.58  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  111 WRATLASSSlrRPSTNRTrgtgVQYELAFILTTLGYILSSLArsgvtrtlyasttpSAEQRTAA--VQTATKHLLQASTI 188
Cdd:pfam03097  88 WYDAFGTSS--KKVSQSS----LAFEKASVLFNIAALYSQLA--------------ASQNRSTDegLKRACKYFQQAAGC 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  189 HSFLSSspyfaTVSEAATlPDLAPATQAALSSLALAEATLLTVLKddsyvvaciqARNPNDKDwmvrapeipkvraHLFA 268
Cdd:pfam03097 148 FQYLKE-----NFLHAPS-PDLSPETLKALSNLMLAQAQECFWEK----------AINDNKKD-------------SLIA 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357528827  269 RLCIRAAEYAEQAATGLSSVAAegrkagVDEDVARYAHVLGLVARARACRFFGVDAELAGKVGEGIAWLRAAKGAL 344
Cdd:pfam03097 199 KLAAQVSELYEEALEALKLSGL------IDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLL 268
 
Name Accession Description Interval E-value
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
2-445 1.36e-160

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: 461.87  E-value: 1.36e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   2 VYPFELPTTSHLSFQSALSSHTHPSLPQSATTARHALRLALKAHNRLPRGFQrDSHLTSVLSAINDYLPYVVALAQGLNN 81
Cdd:cd09245    1 PYPFELPTTSSISFSDFFNSDSYPSLPLNATTARAVLRAALKAHKRTPPGSQ-ASNLLTVVKALEEYLPYLLAIDACLSH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  82 GkpidtttpsttthleeiRVAQRAELEPEWRATLASSSLRrpSTNRTRGTGVQYELAFILTTLGYILSSLARSGVTRTLY 161
Cdd:cd09245   80 D-----------------ELILKSEPTFEWRTTLSSTSGR--ESPRLPLPGLHYELAFVLLTYAYALSNLARSILAPLGA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 162 AST-----TPSAEQRTAAVQTATKHLLQASTIHSFLSSSPYFATVSE---AATLPDLAPATQAALSSLALAEATLLTVLK 233
Cdd:cd09245  141 YETdrsisDASRKQRDERLKAATKLLCKAAGIFDYLATRVLPQWESNrggAPPPPDLSPEVLSALSSLALAEATLLAVRK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 234 DDSYVVACiqarnpnDKDWMVRAPEIPKVRA--HLFARLCIRAAEYAEQAATGLSSVAAEGRKAGVDEDVARYAHVLGLV 311
Cdd:cd09245  221 LDPYPAAV-------DKDWMTPGPPLPKVHPsaHLLARLCLAASEHAESARALLSTPGSKRGSGEVSEELLRYLSDLRRV 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 312 ARARACRFFGVDAELAGKVGEGIAWLRAAKGALGLRNTGSASAEEVttksrglsKLKLGFrerreerkleKGAGGERVDK 391
Cdd:cd09245  294 ARALACKFLGIDAGENGKVGEAIGWLRAAKKELEDLKSPSGVASKA--------KLKKSW----------KEKREDRKVE 355
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 357528827 392 GGlgpgdnAGREEEGRVLEMLETKWVRANDTLNTQLIPSSADYVANLPSGRDVL 445
Cdd:cd09245  356 KG------AGVEEELRTLEMLLKKYKKMNDTVSFQPVPPSSELQSSMPSGREAH 403
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
2-445 2.29e-62

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: 207.20  E-value: 2.29e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   2 VYPFELPTTSHLSFQSALSSHTHPSLPQS-ATTARHALRLALKAHNRLPRGFQRDSHLTSVLSAINDYLPYVVALAQGLN 80
Cdd:cd09034    1 FIGLPLKKTKEVDVKVPLSKFIPKNYGELeATAVEDLIEKLSKLRNNIVTEQNNDTTCENLLEALKEYLPYLLGLEKKLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  81 NGKpidtttpsttthleeirvaQRAELEPEWRATLassslrrpSTNRTRGTGVQYELAFILTTLGYILSSLARSGVTRTl 160
Cdd:cd09034   81 FQK-------------------LRDNVEFTWTDSF--------DTKKESATSLRYELLSILFNLAALASQLANEKLITG- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 161 yasttpsaeqRTAAVQTATKHLLQASTIHSFLSSSPYFATVSEaaTLPDLAPATQAALSSLALAEATLLTVLKDDsyvva 240
Cdd:cd09034  133 ----------SEEDLKQAIKSLQKAAGYFEYLKEHVLPLPPDE--LPVDLTEAVLSALSLIMLAQAQECFLLKAE----- 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 241 ciqarnpNDKdwmvrapeipKVRAHLFARLCIRAAEYAEQAATGLSSVAAEGRKaGVDEDVARYAHVLGLVARARACRFF 320
Cdd:cd09034  196 -------EDK----------KAKLSLLARLACEAAKYYEEALKCLSGVDLETIK-NIPKKWLLFLKWKKCIFKALAYYYH 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 321 GVDAELAGKVGEGIAWLRAAKGALGLRNTGSASAEEvttksrglsklklgfrerreerklekgaggervdkgglgpGDNA 400
Cdd:cd09034  258 GLKLDEANKIGEAIARLQAALELLKESERLCKSFLL----------------------------------------DVWG 297
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 357528827 401 GREEEGRVLEMLETKWVRANDTLNTQLIPSSadyvANLPSGRDVL 445
Cdd:cd09034  298 NLKKLKEKIEKELEKAERENDFIYFEEVPPE----DPLPEIKGAL 338
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
2-433 8.66e-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: 8.66e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827     2 VYPFELPTTSHLSFQSALSSHTHPSLPQsattARHALRLALKAHNRLPRGFQRDSHLTSVLSAINDYLPYVVALAQGLNN 81
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYSE----DSSSYEDEIAELNRLRQAARTPSRDESGLELLLKYYGQLEALELRFPP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827    82 GkpidtttpsttthleeirvAQRAELEPEWRATLASSSlrrPSTNRTrgtgVQYELAFILTTLGYILSSLARSgvtrtly 161
Cdd:smart01041  77 P-------------------EGQLKLSFTWYDSLDTGV---PSTQSS----LAFEKASVLFNLGALYSQIAAE------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   162 asttpSAEQRTAAVQTATKHLLQASTIHSFLSSspyfaTVSEAA---TLPDLAPATQAALSSLALAEATLLTVLKddsyv 238
Cdd:smart01041 124 -----QNRDTEEGLKEACKAFQQAAGVFNYLKE-----NFLHALstePSVDLSPETLSALSSLMLAQAQECFFEK----- 188
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   239 vACIQARnpndkdwmvrapeipKVRAHLFARLCIRAAEYAEQAATGLSSVAAEgrKAGVDEDVARYAHVLGLVARARACR 318
Cdd:smart01041 189 -AILDGM---------------KNKDSLIAKLAAQAAEYYEEALKALQTSEPV--KGYIPKSWIKLVQVKAHHFKALAHY 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   319 FFGVDAELAGKVGEGIAWLRAAKGALGLrntgsASAEEVTTKSRGLSKLklgfrerreerklekgaggervdkgglgpGD 398
Cdd:smart01041 251 YQALDLEEANKYGEAIARLQEALERLKE-----AKKHLRCKKLGKADKL-----------------------------QE 296
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 357528827   399 NAGREEEgRVLEMLEtKWVRANDTLNTQLIPSSAD 433
Cdd:smart01041 297 DLSGLKD-VVEEKLK-EAEKDNDFIYHERVPDIVS 329
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
3-344 2.48e-09

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: 58.94  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827   3 YPFELPTTSHLSFQS---ALSSHTHPSLpQSATTARHALrlaLKAHNRLPRGFQRdshltsVLSAINDYLPYVVALAQGL 79
Cdd:cd09247    1 YDFAKPKTKKIVFEKtfqARDSLTLEQL-KELSLRRRAI---IESINGSPFIALA------IAREKAQYLPYLEGYLPAL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  80 NNgkpidTTTPSTTTHLEEirvaqraELEPEWRATLASSSLRRPSTNrtrgTGVQYELAFILTTLGYILSSLArsgvtrt 159
Cdd:cd09247   71 EN-----LVNHRDKVQLNE-------QLSFRWTSGLGSSKGPKAFQS----DSLRFELGMVLFLYGAALRERA------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 160 lyasttpSAEQRTAAVQTATKHLLQASTIHSFLSSS---PYFATVSEAATLPDLAPATQAALSSLALAEATLLTVLKdds 236
Cdd:cd09247  128 -------SEVLPTEDFKEAATHLRRAAGVFEFLAHDelpRLRGALSADERPPECTPSLALAMSLLCLAEAQAVTARK--- 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 237 yvvACIQARNPNdkdwmvrapeipkvrahLFARLCIRAAEYAEQAATGLSSVAAEGRKagVDEDVARYAHVLGLVARARA 316
Cdd:cd09247  198 ---AEEKGTSPS-----------------LLAKLHYGATQFLEEAKNVLRSLATDLKD--LDPRFLRFISSCIALHEARS 255
                        330       340
                 ....*....|....*....|....*...
gi 357528827 317 CRFFGVDAELAGKVGEGIAWLRAAKGAL 344
Cdd:cd09247  256 QLYLARRLKEAGHIGVAVGVLREALRNL 283
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
111-344 1.05e-05

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: 47.58  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  111 WRATLASSSlrRPSTNRTrgtgVQYELAFILTTLGYILSSLArsgvtrtlyasttpSAEQRTAA--VQTATKHLLQASTI 188
Cdd:pfam03097  88 WYDAFGTSS--KKVSQSS----LAFEKASVLFNIAALYSQLA--------------ASQNRSTDegLKRACKYFQQAAGC 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827  189 HSFLSSspyfaTVSEAATlPDLAPATQAALSSLALAEATLLTVLKddsyvvaciqARNPNDKDwmvrapeipkvraHLFA 268
Cdd:pfam03097 148 FQYLKE-----NFLHAPS-PDLSPETLKALSNLMLAQAQECFWEK----------AINDNKKD-------------SLIA 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357528827  269 RLCIRAAEYAEQAATGLSSVAAegrkagVDEDVARYAHVLGLVARARACRFFGVDAELAGKVGEGIAWLRAAKGAL 344
Cdd:pfam03097 199 KLAAQVSELYEEALEALKLSGL------IDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLL 268
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
134-344 3.83e-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: 42.65  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 134 QYELAF----ILTTLGYILSSLARSgvtrtlyasttpSAEQRTAAVQTATKHLLQASTIHSFLSSspYFATvseaATLPD 209
Cdd:cd09242   99 QHSLAFekasVLFNIGALLSQLAAE------------KYREDEDDLKEAITNLQQAAGCFQYINE--NFLH----APSVD 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 210 LAPATQAALSSLALAEATLLTVLKddsyvvaCIqarnpNDKDwmvrapeiPKVRAHLFARLCIRAAEYAEQAATGLSSVA 289
Cdd:cd09242  161 LQQENVKFLVKLMLAQAQEIFLLK-------LI-----NGDD--------AQKKASLISKLASATANLYESCVEFLKEIQ 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 357528827 290 AEGRKAGVD---EDVARYAHVLglvaRARACRFFGVDAELAGKVGEGIAWLRAAKGAL 344
Cdd:cd09242  221 EKGISYGDPkwiSLVQCKAHYY----KSLAAYYHALALEAAGKYGEAIAYLTQAESIL 274
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
177-330 4.19e-04

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: 42.67  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 177 TATKHLLQASTIHSFLSSSPYfATVSEAATlPDLAPATQAALSSLALAEATLLTVLK------------------DDSYV 238
Cdd:cd09240  146 LAAKLFQQAAGIFNHLKETVL-SALQQEPT-PDLSPDTLSALSALMLAQAQEVFYLKatrdkmkdaiiaklaaqaADYYG 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357528827 239 VACIQARNPN-----DKDWmvrapeipkvrahlFARLCIRAAEYAEQAATGLSSVAAEGRKAGvdEDVARYAHVLGLV-- 311
Cdd:cd09240  224 DAFKQCQREDvrsllPKDW--------------IPVLAGKQAYFHALAEYHQSLVAKAQKKFG--EEIARLQHALELIkt 287
                        170
                 ....*....|....*....
gi 357528827 312 ARARACRFFGVDaELAGKV 330
Cdd:cd09240  288 AQSRAGEYVDVK-DFAAKI 305
 
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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