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Conserved domains on  [gi|186478438|ref|NP_563927|]
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Endosomal targeting BRO1-like domain-containing protein [Arabidopsis thaliana]

Protein Classification

BRO1 domain-containing protein( domain architecture ID 10174145)

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_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 6-363 1.94e-138

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: 397.92  E-value: 1.94e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   6 YLIPEPKTKEILYEKTLQAAGPITLGEVKELTSKRKIIEESVNKTSKVIDSTTREMTrgltsaceQDLHKLGEYLPLLFN 85
Cdd:cd09247    1 YDFAKPKTKKIVFEKTFQARDSLTLEQLKELSLRRRAIIESINGSPFIALAIAREKA--------QYLPYLEGYLPALEN 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  86 LVHYTDKIKRVSNLKIRWSSGLISqtliqRTCPKFFQVDNIMFEFGMVLFIYAVKLRERAMELVST-DSKKAVAVYREAS 164
Cdd:cd09247   73 LVNHRDKVQLNEQLSFRWTSGLGS-----SKGPKAFQSDSLRFELGMVLFLYGAALRERASEVLPTeDFKEAATHLRRAA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 165 GVFHHLSHEILPLLQTCL-PPGKLPELTPPLCSALSLLCLAEGQAVTTEKAEESGKSASLLSKLHFGIFQFLSEAYALLS 243
Cdd:cd09247  148 GVFEFLAHDELPRLRGALsADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEAKNVLR 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 244 SRlTGEYKDLSTRFLEYVTTMGALHELKSQKYLAELLESEDRVGDAVGVLRRALAAAKKSTPSKDDKWIAIFKKEREDVA 323
Cdd:cd09247  228 SL-ATDLKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKLPGSDISSPVIFRDERAEVA 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 186478438 324 KNMAKYEKLNDSMMLQKIPIDREIPFPKGEKIVNLIPYTP 363
Cdd:cd09247  307 TLLQKYEKENEVIYFEKVPDIDELPLPEGKVIVKPVPYKP 346
 
Name Accession Description Interval E-value
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 6-363 1.94e-138

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: 397.92  E-value: 1.94e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   6 YLIPEPKTKEILYEKTLQAAGPITLGEVKELTSKRKIIEESVNKTSKVIDSTTREMTrgltsaceQDLHKLGEYLPLLFN 85
Cdd:cd09247    1 YDFAKPKTKKIVFEKTFQARDSLTLEQLKELSLRRRAIIESINGSPFIALAIAREKA--------QYLPYLEGYLPALEN 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  86 LVHYTDKIKRVSNLKIRWSSGLISqtliqRTCPKFFQVDNIMFEFGMVLFIYAVKLRERAMELVST-DSKKAVAVYREAS 164
Cdd:cd09247   73 LVNHRDKVQLNEQLSFRWTSGLGS-----SKGPKAFQSDSLRFELGMVLFLYGAALRERASEVLPTeDFKEAATHLRRAA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 165 GVFHHLSHEILPLLQTCL-PPGKLPELTPPLCSALSLLCLAEGQAVTTEKAEESGKSASLLSKLHFGIFQFLSEAYALLS 243
Cdd:cd09247  148 GVFEFLAHDELPRLRGALsADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEAKNVLR 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 244 SRlTGEYKDLSTRFLEYVTTMGALHELKSQKYLAELLESEDRVGDAVGVLRRALAAAKKSTPSKDDKWIAIFKKEREDVA 323
Cdd:cd09247  228 SL-ATDLKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKLPGSDISSPVIFRDERAEVA 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 186478438 324 KNMAKYEKLNDSMMLQKIPIDREIPFPKGEKIVNLIPYTP 363
Cdd:cd09247  307 TLLQKYEKENEVIYFEKVPDIDELPLPEGKVIVKPVPYKP 346
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 40-370 1.84e-17

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: 82.78  E-value: 1.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438    40 RKIIEESVNKTSKVIDSTTREMTRgLTSAC------EQDLHKLGEYLPLLFNLVHYTDKIKRVSNLKIRWSSGLISQTLI 113
Cdd:smart01041  19 KDYIKETYSEDSSSYEDEIAELNR-LRQAArtpsrdESGLELLLKYYGQLEALELRFPPPEGQLKLSFTWYDSLDTGVPS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   114 QRTcpkffqvdNIMFEFGMVLFIYAVKLRERA--MELVSTDS-KKAVAVYREASGVFHHLSHEILPLLqtclPPGKLPEL 190
Cdd:smart01041  98 TQS--------SLAFEKASVLFNLGALYSQIAaeQNRDTEEGlKEACKAFQQAAGVFNYLKENFLHAL----STEPSVDL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   191 TPPLCSALSLLCLAEGQAVTTEKAEESGKS--ASLLSKLHFGIFQFLSEAYALLSSrlTGEYKDLSTRFLEYVTTMGALH 268
Cdd:smart01041 166 SPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQT--SEPVKGYIPKSWIKLVQVKAHH 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   269 -ELKSQKYLAELLESEDRVGDAVGVLRRALAAAKKST-------PSKDDKWIAIFKKEREDVAKNMAKYEKLNDSMMLQK 340
Cdd:smart01041 244 fKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKkhlrckkLGKADKLQEDLSGLKDVVEEKLKEAEKDNDFIYHER 323

                          330       340       350
                   ....*....|....*....|....*....|
gi 186478438   341 IPIDREIPFPKGEKIVNLIPYTPTRVVREL 370
Cdd:smart01041 324 VPDIVSLPPIKKAPLVKPPPFSEVLKGPDL 353
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 145-360 3.50e-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: 51.43  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  145 AMELVSTDS--KKAVAVYREASGVFHHLSHEILpllqtcLPPGklPELTPPLCSALSLLCLAEGQAVTTEKAEESGKSAS 222
Cdd:pfam03097 124 ASQNRSTDEglKRACKYFQQAAGCFQYLKENFL------HAPS--PDLSPETLKALSNLMLAQAQECFWEKAINDNKKDS 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  223 LLSKLHFGIFQFLSEAYALLSSRltgeyKDLSTRFLEYVTTMGALHELKSQKYLAELLESEDRVGDAVGVLRRALAAAKK 302
Cdd:pfam03097 196 LIAKLAAQVSELYEEALEALKLS-----GLIDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKE 270

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 186478438  303 STPSKDDKWIAI-FKKEREDVAKNMAKYEKLNDSMMLQKIPIDREIPFPKGEKIVNLIP 360
Cdd:pfam03097 271 ALKSDRYKKVLEdLKGLLDVVEEKLKRAEKDNDFIYHERVPSESSLPPIKPASMVKPIP 329
 
Name Accession Description Interval E-value
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 6-363 1.94e-138

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: 397.92  E-value: 1.94e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   6 YLIPEPKTKEILYEKTLQAAGPITLGEVKELTSKRKIIEESVNKTSKVIDSTTREMTrgltsaceQDLHKLGEYLPLLFN 85
Cdd:cd09247    1 YDFAKPKTKKIVFEKTFQARDSLTLEQLKELSLRRRAIIESINGSPFIALAIAREKA--------QYLPYLEGYLPALEN 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  86 LVHYTDKIKRVSNLKIRWSSGLISqtliqRTCPKFFQVDNIMFEFGMVLFIYAVKLRERAMELVST-DSKKAVAVYREAS 164
Cdd:cd09247   73 LVNHRDKVQLNEQLSFRWTSGLGS-----SKGPKAFQSDSLRFELGMVLFLYGAALRERASEVLPTeDFKEAATHLRRAA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 165 GVFHHLSHEILPLLQTCL-PPGKLPELTPPLCSALSLLCLAEGQAVTTEKAEESGKSASLLSKLHFGIFQFLSEAYALLS 243
Cdd:cd09247  148 GVFEFLAHDELPRLRGALsADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEAKNVLR 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 244 SRlTGEYKDLSTRFLEYVTTMGALHELKSQKYLAELLESEDRVGDAVGVLRRALAAAKKSTPSKDDKWIAIFKKEREDVA 323
Cdd:cd09247  228 SL-ATDLKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKLPGSDISSPVIFRDERAEVA 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 186478438 324 KNMAKYEKLNDSMMLQKIPIDREIPFPKGEKIVNLIPYTP 363
Cdd:cd09247  307 TLLQKYEKENEVIYFEKVPDIDELPLPEGKVIVKPVPYKP 346
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 5-363 1.15e-28

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: 113.98  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   5 QYLIPEPKTKEILYEKTLQAAGPITLGEVKELTskrkiIEESVNKTSKVIDSTTREMTRGLTsaCEQDLHKLGEYLPLLF 84
Cdd:cd09034    1 FIGLPLKKTKEVDVKVPLSKFIPKNYGELEATA-----VEDLIEKLSKLRNNIVTEQNNDTT--CENLLEALKEYLPYLL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  85 NLVHYTDKIKRVSNLKIRWSSGLisqtliqrtCPKFFQVDNIMFEFGMVLFIYAVKLRERAMELVSTDS----KKAVAVY 160
Cdd:cd09034   74 GLEKKLPFQKLRDNVEFTWTDSF---------DTKKESATSLRYELLSILFNLAALASQLANEKLITGSeedlKQAIKSL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 161 REASGVFHHLSHEILPLLqtclPPGKLPELTPPLCSALSLLCLAEGQAVTTEKAEESGK-SASLLSKLHFGIFQFLSEAY 239
Cdd:cd09034  145 QKAAGYFEYLKEHVLPLP----PDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKaKLSLLARLACEAAKYYEEAL 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 240 ALLSSRLTGEYKDLSTRFLEYVTTMGALHELKSQKYLAELLESEDRVGDAVGVLRRALAAAKKSTPSKD----DKWIaIF 315
Cdd:cd09034  221 KCLSGVDLETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKsfllDVWG-NL 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 186478438 316 KKEREDVAKNMAKYEKLNDSMMLQKIPidREIPFPKGEKIVNLIPYTP 363
Cdd:cd09034  300 KKLKEKIEKELEKAERENDFIYFEEVP--PEDPLPEIKGALLVKPPPL 345
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 40-370 1.84e-17

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: 82.78  E-value: 1.84e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438    40 RKIIEESVNKTSKVIDSTTREMTRgLTSAC------EQDLHKLGEYLPLLFNLVHYTDKIKRVSNLKIRWSSGLISQTLI 113
Cdd:smart01041  19 KDYIKETYSEDSSSYEDEIAELNR-LRQAArtpsrdESGLELLLKYYGQLEALELRFPPPEGQLKLSFTWYDSLDTGVPS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   114 QRTcpkffqvdNIMFEFGMVLFIYAVKLRERA--MELVSTDS-KKAVAVYREASGVFHHLSHEILPLLqtclPPGKLPEL 190
Cdd:smart01041  98 TQS--------SLAFEKASVLFNLGALYSQIAaeQNRDTEEGlKEACKAFQQAAGVFNYLKENFLHAL----STEPSVDL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   191 TPPLCSALSLLCLAEGQAVTTEKAEESGKS--ASLLSKLHFGIFQFLSEAYALLSSrlTGEYKDLSTRFLEYVTTMGALH 268
Cdd:smart01041 166 SPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQT--SEPVKGYIPKSWIKLVQVKAHH 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438   269 -ELKSQKYLAELLESEDRVGDAVGVLRRALAAAKKST-------PSKDDKWIAIFKKEREDVAKNMAKYEKLNDSMMLQK 340
Cdd:smart01041 244 fKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKkhlrckkLGKADKLQEDLSGLKDVVEEKLKEAEKDNDFIYHER 323

                          330       340       350
                   ....*....|....*....|....*....|
gi 186478438   341 IPIDREIPFPKGEKIVNLIPYTPTRVVREL 370
Cdd:smart01041 324 VPDIVSLPPIKKAPLVKPPPFSEVLKGPDL 353
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
 76-363 1.11e-15

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: 77.83  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  76 LGEYLPLLFNLVH--YTDKIKRVSNLKIRWSSGLISQtlIQRTCPKFfQVDNIMFEFGMVLFIYAVKL------------ 141
Cdd:cd09245   63 LEEYLPYLLAIDAclSHDELILKSEPTFEWRTTLSST--SGRESPRL-PLPGLHYELAFVLLTYAYALsnlarsilaplg 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 142 ---RERAMELVSTDS-----KKAVAVYREASGVFHHLSHEILPLLQTCLPPGKLP-ELTPPLCSALSLLCLAEGQAVTTE 212
Cdd:cd09245  140 ayeTDRSISDASRKQrderlKAATKLLCKAAGIFDYLATRVLPQWESNRGGAPPPpDLSPEVLSALSSLALAEATLLAVR 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 213 K------------------AEESGKSASLLSKLHFGIFQFLSEAYALLSSRLTGEYK-DLSTRFLEYVTTMGALHELKSQ 273
Cdd:cd09245  220 KldpypaavdkdwmtpgppLPKVHPSAHLLARLCLAASEHAESARALLSTPGSKRGSgEVSEELLRYLSDLRRVARALAC 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 274 KYLAELLESEDRVGDAVGVLRRA---LAAAKKSTPSKDDKWIAIFKKE-RED--------VAK-----NM--AKYEKLND 334
Cdd:cd09245  300 KFLGIDAGENGKVGEAIGWLRAAkkeLEDLKSPSGVASKAKLKKSWKEkREDrkvekgagVEEelrtlEMllKKYKKMND 379

                        330       340       350
                 ....*....|....*....|....*....|.
gi 186478438 335 SMMLQKIPIDREIP--FPKGEKIVNLIPYTP 363
Cdd:cd09245  380 TVSFQPVPPSSELQssMPSGREAHTAKPYTP 410
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 125-348 6.13e-10

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: 60.10  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 125 NIMFEFGMVLFIYAVKLRERAmelVSTDS------KKAVAVYREASGVFHHLSHEILPLLQTCLPPgklpELTPPLCSAL 198
Cdd:cd09246  105 NVHFEKAAVLFNLGALSSQLG---LQQDRttaegiKQACHAFQAAAGAFAHLRDKVSGKTGGFRTP----DLTAECLGML 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 199 SLLCLAEGQAVTTEKAEESGKSASLLSKLHFGIFQFLSEAYALLSSRLTGEYKDLStrFLEYVTTMGALHELKSQKYLAE 278
Cdd:cd09246  178 ESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSPPLKGHFDKS--WVAHVQLKAAYFRAEALYRAAK 255

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186478438 279 LLESEDRVGDAVGVLRRA---LAAAKKSTPS-KDDKWIAIFKKEREDVAKNMAKYEKLNDSMMLQKIPIDREIP 348
Cdd:cd09246  256 DLHEKEDIGEEIARLRAAsdaLAEARKQAKGvNGDELIEAVSELEQVINELLERAEKENDCVYLDRVPAPSDLP 329
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 78-350 6.42e-08

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185766  Cd Length: 353  Bit Score: 53.88  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  78 EYLPLLFNLV---HYTDKIKRVSNL-KIRWSSGLISQTLIQRTcPKFFQVDNIMFEFGMVLFIYAVKLRERAmELVSTDS 153
Cdd:cd09243   60 AYLSLLQGFIlalDGKTQESKLRYLiNFKWTDSLLGNEPSVQQ-DAIFELASMLFNVALWYTKHASKLAGKE-DITEDEA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 154 KKAVAVYREASGVFHHLSHEILPLLQTCLPPGKlpELTPPLCSALSLLCLAEGQAVTTEKAEESGKSASLLSKLHFGIFQ 233
Cdd:cd09243  138 KDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGS--DLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAK 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 234 FLSEAYALLSSrLTGEYkdlSTRFLEYVttmgalhELKSQKYLA-------ELLESEDRVGDAVGVLR-------RALAA 299
Cdd:cd09243  216 LFQKADDSLSS-LDPEY---SGKWRKYL-------QLKSVFYLAyaycyhgETLLAKDKCGEAIRSLQeseklynKAEAL 284

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 186478438 300 AKK-------STPSKDDKWIaIFKKEREDVAKNMAKYEKLNDSMMLQKIPidREIPFP 350
Cdd:cd09243  285 CKEyaktkgpGTTAKPDQHL-FFRKLGPLVKRTLEKCERENGFIYHQKVP--DEVPQL 339
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 145-360 3.50e-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: 51.43  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  145 AMELVSTDS--KKAVAVYREASGVFHHLSHEILpllqtcLPPGklPELTPPLCSALSLLCLAEGQAVTTEKAEESGKSAS 222
Cdd:pfam03097 124 ASQNRSTDEglKRACKYFQQAAGCFQYLKENFL------HAPS--PDLSPETLKALSNLMLAQAQECFWEKAINDNKKDS 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438  223 LLSKLHFGIFQFLSEAYALLSSRltgeyKDLSTRFLEYVTTMGALHELKSQKYLAELLESEDRVGDAVGVLRRALAAAKK 302
Cdd:pfam03097 196 LIAKLAAQVSELYEEALEALKLS-----GLIDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKE 270

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 186478438  303 STPSKDDKWIAI-FKKEREDVAKNMAKYEKLNDSMMLQKIPIDREIPFPKGEKIVNLIP 360
Cdd:pfam03097 271 ALKSDRYKKVLEdLKGLLDVVEEKLKRAEKDNDFIYHERVPSESSLPPIKPASMVKPIP 329
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 125-360 4.39e-03

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: 38.79  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 125 NIMFEFGMVLFIYAVKLRERAMElvstDSKKAVAVYREASGVFHHLSHEILPllqtclPPGKLPELTPPLCSALSLLCLA 204
Cdd:cd09241  107 NILYNLGALYSQLALSENRYTDE----GLKRACSYFQASAGCFEYILQHLLP------TLSPPPDLDENTLKALESLMLA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 205 EGQAVTTEKAEESGKSASLLSKLHFGIFQFLSEAYALL-SSRLtgeykdLSTRFLEYVTTMGALHELKSQKYLAELLESE 283
Cdd:cd09241  177 QAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYAnKSDL------IRSDWINHLKVKKHHFKAAAHYRMALVALEK 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478438 284 DRVGDAVGVLRRALAAAKKStpSKDDKWIAIFKKE-----REDVAKNMAKYEKLNDSMMLQKIPIDREIPFPKGEKIVNL 358
Cdd:cd09241  251 SKYGEEVARLRVALAACKEA--LKEARYGNKAVLEdlqglKDIVKESLKRAERDNDLIYLQPVPPASELPPIKPASMVKA 328


                 ..
gi 186478438 359 IP 360
Cdd:cd09241  329 IV 330
 
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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