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Conserved domains on  [gi|530366071|ref|XP_005273126|]
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BRO1 domain-containing protein BROX isoform X5 [Homo sapiens]

Protein Classification

BRO1_Brox_like domain-containing protein( domain architecture ID 10174120)

BRO1_Brox_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
1-301 0e+00

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: 596.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   1 MMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENI 80
Cdd:cd09243   53 TVKTAFNAYLSLLQGFILALDGKTQESKLRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  81 TEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYE 160
Cdd:cd09243  133 TEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYE 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 161 TANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETK 240
Cdd:cd09243  213 TAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTK 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530366071 241 GPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPF 301
Cdd:cd09243  293 GPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
1-301 0e+00

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: 596.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   1 MMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENI 80
Cdd:cd09243   53 TVKTAFNAYLSLLQGFILALDGKTQESKLRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  81 TEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYE 160
Cdd:cd09243  133 TEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYE 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 161 TANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETK 240
Cdd:cd09243  213 TAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTK 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530366071 241 GPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPF 301
Cdd:cd09243  293 GPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
9-306 1.06e-83

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: 258.82  E-value: 1.06e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071     9 YFSLLQGFINSLDESTQESKLryiqNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEV 88
Cdd:smart01041  63 YYGQLEALELRFPPPEGQLKL----SFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEA 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071    89 HRSLKIAAGIFKHLKESHLPKLITpaEKGRDLESRLIEAYVIQCQAEAQEVTIARAI--ELKHAPGLIAALAYETANFYQ 166
Cdd:smart01041 136 CKAFQQAAGVFNYLKENFLHALST--EPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYE 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   167 KADHTLSSLEPAYS---AKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKeygeTKGPG 243
Cdd:smart01041 214 EALKALQTSEPVKGyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLG 289
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530366071   244 PTVKPSGHLFFrkLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKAnYGLVEPIPFEFPPT 306
Cdd:smart01041 290 KADKLQEDLSG--LKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKK-APLVKPPPFSEVLK 349
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
34-308 1.67e-37

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: 138.10  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   34 NFKWTDTLQ-GQVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKli 111
Cdd:pfam03097  85 EFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENFLHA-- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  112 tpaeKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKAdHTLSSLEPAYSAKWRKYLHLKM 191
Cdd:pfam03097 159 ----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKA 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  192 CFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEAlCKEYGETKGpgptvkpsghlFFRKLGNLVKNTLEKCQRE 271
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKD 301
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 530366071  272 NGFIYFQKIPTEA--PQLElKANygLVEPIPFEFPPTSV 308
Cdd:pfam03097 302 NDFIYHERVPSESslPPIK-PAS--MVKPIPPLELYPFQ 337
 
Name Accession Description Interval E-value
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
1-301 0e+00

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: 596.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   1 MMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENI 80
Cdd:cd09243   53 TVKTAFNAYLSLLQGFILALDGKTQESKLRYLINFKWTDSLLGNEPSVQQDAIFELASMLFNVALWYTKHASKLAGKEDI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  81 TEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYE 160
Cdd:cd09243  133 TEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYE 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 161 TANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETK 240
Cdd:cd09243  213 TAKLFQKADDSLSSLDPEYSGKWRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKEYAKTK 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530366071 241 GPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPF 301
Cdd:cd09243  293 GPGTTAKPDQHLFFRKLGPLVKRTLEKCERENGFIYHQKVPDEVPQLELKATYGLVSPEEF 353
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
9-306 1.06e-83

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: 258.82  E-value: 1.06e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071     9 YFSLLQGFINSLDESTQESKLryiqNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAgkeNITEDEAKEV 88
Cdd:smart01041  63 YYGQLEALELRFPPPEGQLKL----SFTWYDSLDTGVPSTQSSLAFEKASVLFNLGALYSQIAAEQN---RDTEEGLKEA 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071    89 HRSLKIAAGIFKHLKESHLPKLITpaEKGRDLESRLIEAYVIQCQAEAQEVTIARAI--ELKHAPGLIAALAYETANFYQ 166
Cdd:smart01041 136 CKAFQQAAGVFNYLKENFLHALST--EPSVDLSPETLSALSSLMLAQAQECFFEKAIldGMKNKDSLIAKLAAQAAEYYE 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   167 KADHTLSSLEPAYS---AKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKeygeTKGPG 243
Cdd:smart01041 214 EALKALQTSEPVKGyipKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKHLR----CKKLG 289
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530366071   244 PTVKPSGHLFFrkLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKAnYGLVEPIPFEFPPT 306
Cdd:smart01041 290 KADKLQEDLSG--LKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKK-APLVKPPPFSEVLK 349
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
3-298 1.01e-67

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: 216.45  E-value: 1.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   3 KNAADSYFSLLQGFINSLDEStqesKLRYIQNFKWTDTLQGQVPSAQqDAVFELISMGFNVALWYtkyaSRLAGKENIT- 81
Cdd:cd09034   62 LEALKEYLPYLLGLEKKLPFQ----KLRDNVEFTWTDSFDTKKESAT-SLRYELLSILFNLAALA----SQLANEKLITg 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  82 -EDEAKEVHRSLKIAAGIFKHLKESHLPKliTPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHA-PGLIAALAY 159
Cdd:cd09034  133 sEEDLKQAIKSLQKAAGYFEYLKEHVLPL--PPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKAkLSLLARLAC 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 160 ETANFYQKADHTLSSLEPAYS----AKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKE 235
Cdd:cd09034  211 EAAKYYEEALKCLSGVDLETIknipKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKS 290
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530366071 236 YGEtkgpgptvkpSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEP 298
Cdd:cd09034  291 FLL----------DVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPEDPLPEIKGALLVKPP 343
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
34-308 1.67e-37

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: 138.10  E-value: 1.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   34 NFKWTDTLQ-GQVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKli 111
Cdd:pfam03097  85 EFTWYDAFGtSSKKVSQSSLAFEKASVLFNIAALY----SQLAASQNRSTDEGlKRACKYFQQAAGCFQYLKENFLHA-- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  112 tpaeKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKAdHTLSSLEPAYSAKWRKYLHLKM 191
Cdd:pfam03097 159 ----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEA-LEALKLSGLIDKEWISHVQAKA 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  192 CFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEAlCKEYGETKGpgptvkpsghlFFRKLGNLVKNTLEKCQRE 271
Cdd:pfam03097 234 HHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALK-SDRYKKVLE-----------DLKGLLDVVEEKLKRAEKD 301
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 530366071  272 NGFIYFQKIPTEA--PQLElKANygLVEPIPFEFPPTSV 308
Cdd:pfam03097 302 NDFIYHERVPSESslPPIK-PAS--MVKPIPPLELYPFQ 337
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
8-302 1.71e-29

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: 115.95  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   8 SYFSLLQGFINSLDESTQESKLRyiqnFKWTDTLQGQVP--SAQQDAV-FELISMGFNVALWYTKYASRLagkeNITEDe 84
Cdd:cd09247   65 GYLPALENLVNHRDKVQLNEQLS----FRWTSGLGSSKGpkAFQSDSLrFELGMVLFLYGAALRERASEV----LPTED- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  85 AKEVHRSLKIAAGIFKHLKESHLPKLIT---PAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYET 161
Cdd:cd09247  136 FKEAATHLRRAAGVFEFLAHDELPRLRGalsADERPPECTPSLALAMSLLCLAEAQAVTARKAEEKGTSPSLLAKLHYGA 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 162 ANFYQKADHTLSSLEPAYSA---KWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEalckeyge 238
Cdd:cd09247  216 TQFLEEAKNVLRSLATDLKDldpRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLREALRNLKKKL-------- 287
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530366071 239 tkgpgPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIP--TEAPQLELKAnygLVEPIPFE 302
Cdd:cd09247  288 -----PGSDISSPVIFRDERAEVATLLQKYEKENEVIYFEKVPdiDELPLPEGKV---IVKPVPYK 345
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
35-303 5.51e-29

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: 114.67  E-value: 5.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  35 FKWTDTL--QGQVPSAQQDAVFELISMGFNVALWYtkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKLI 111
Cdd:cd09241   82 FTWYPTLgyKSSGPVSLSSLKFERANILYNLGALY----SQLALSENRYTDEGlKRACSYFQASAGCFEYILQHLLPTLS 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 112 TPaekgRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKAdHTLSSLEPAYSAKWRKYLHLKM 191
Cdd:cd09241  158 PP----PDLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEA-LKYANKSDLIRSDWINHLKVKK 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 192 CFYTAYAYCYHGETLLASDKCGEAIRSLQEaeklyakAEALCKE-YGETKGPGPTVKPSghlfFRKLGNLVKNTLEKCQR 270
Cdd:cd09241  233 HHFKAAAHYRMALVALEKSKYGEEVARLRV-------ALAACKEaLKEARYGNKAVLED----LQGLKDIVKESLKRAER 301
                        250       260       270
                 ....*....|....*....|....*....|...
gi 530366071 271 ENGFIYFQKIPTEApQLELKANYGLVEPIPFEF 303
Cdd:cd09241  302 DNDLIYLQPVPPAS-ELPPIKPASMVKAIVPPE 333
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
34-302 5.98e-24

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: 100.82  E-value: 5.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  34 NFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYAsrlagKENITEDEA--KEVHRSLKIAAGIFKHLKES--HLPk 109
Cdd:cd09242   84 DFTWYDAFYKSKKVKQHSLAFEKASVLFNIGALLSQLA-----AEKYREDEDdlKEAITNLQQAAGCFQYINENflHAP- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 110 litpaekGRDLESRLIEAYVIQCQAEAQEV----TIARAIELKHApGLIAALAYETANFYQKADHTLSSLEPA----YSA 181
Cdd:cd09242  158 -------SVDLQQENVKFLVKLMLAQAQEIfllkLINGDDAQKKA-SLISKLASATANLYESCVEFLKEIQEKgisyGDP 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 182 KWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALckeygeTKGPGPTVKPSGHL---FFRKLG 258
Cdd:cd09242  230 KWISLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPQ------KLSLKASAGDAAYAlndDFKGQK 303
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 530366071 259 NLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGlVEPIPFE 302
Cdd:cd09242  304 DTVEEKLKELEKDNDFIYHDIVPSEVTLPSIKPLDA-AKPIPIE 346
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
34-301 3.63e-20

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: 90.05  E-value: 3.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  34 NFKWTDTLQ------GQVPSAQQDAVFELISMGFNVAlwytKYASRLAGKENI-TEDEAKEVHRSLKIAAGIFKHLKE-- 104
Cdd:cd09240   90 TFTWKDAFDkgslfgGSKKLALSSLGYEKVCVLFNIA----ALQSQIAAEQNLdTDEGLKLAAKLFQQAAGIFNHLKEtv 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 105 -SHLPKLITPaekgrDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLS--SLEPAYSA 181
Cdd:cd09240  166 lSALQQEPTP-----DLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQreDVRSLLPK 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 182 KWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYgetkgpgptvkpsghLFFRKLGNLV 261
Cdd:cd09240  241 DWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEY---------------VDVKDFAAKI 305
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 530366071 262 KNTLEKCQRENGFIYFQKIPtEAPQLEL--KANygLVEPIPF 301
Cdd:cd09240  306 SRALTAAKKDNDFIYHDRVP-DVKSLPPigKAA--LAKPTPV 344
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
35-315 2.30e-16

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: 78.98  E-value: 2.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  35 FKWTDTLQGQVPSAQQDAVFELISMGFNV-ALWytkyaSRLAGKENITEDEA-KEVHRSLKIAAGIFKHLKESHLPKLIT 112
Cdd:cd09246   89 FSWYDAFRPHRKATQANVHFEKAAVLFNLgALS-----SQLGLQQDRTTAEGiKQACHAFQAAAGAFAHLRDKVSGKTGG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 113 PAEKgrDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSS--LEPAYSAKWRKYLHLK 190
Cdd:cd09246  164 FRTP--DLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSppLKGHFDKSWVAHVQLK 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 191 MCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAealCKEygETKGPGPTVKpsghLFFRKLGNLVKNTLEKCQR 270
Cdd:cd09246  242 AAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAEA---RKQ--AKGVNGDELI----EAVSELEQVINELLERAEK 312
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530366071 271 ENGFIYFQKIPT--EAPQLELKAnygLVEPIPfefPPTSVQWTPETL 315
Cdd:cd09246  313 ENDCVYLDRVPApsDLPPLGAAS---MVKPAA---PPAELDASPEDM 353
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
35-308 1.65e-14

Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP) and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. HD-PTP participates in cell migration and endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185762  Cd Length: 361  Bit Score: 73.62  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  35 FKWTDTLQGQVpSAQQDAVFELISMGFNVALWYTKYAsrlAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPklitpA 114
Cdd:cd09239   93 FTWTDIFSGSE-VTHEDIKFEEASVLYNIGALHSQLG---ASDKRDSEEGMKVACTHFQCAAWAFAYLREHYPQ-----V 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 115 EKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLE-------PAYSAKWRKYL 187
Cdd:cd09239  164 YGAVDMSSQLLSFNYSLMLAQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRALENWEsnskiilGKIQKEWRKLV 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 188 HLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKlyaKAEALCKEYgetKGPGPTVKPSGHLFFrkLGNLVKNTLEK 267
Cdd:cd09239  244 QMKIAYYASIAHLHMGKQSEEQQKMGERVAYYQLAND---KLEEAIKNA---KGQPDTVNLQEALSF--TMDVIGGKRNS 315
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 530366071 268 CQRENGFIYFQKIPtEAPQLELKANYGLVEPIPFEFPPTSV 308
Cdd:cd09239  316 AKKENDFIYHEAVP-KLDTLQAVKGANLVKGIPFSPTDPEV 355
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
35-303 1.70e-09

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; This family contains the Bro1-like domain of RhoA-binding proteins, Rhophilin-1 and -2, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 and -2 bind both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 and -2, contain an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Their PDZ domains have limited homology. Rhophilin-1 and -2 have different activities. The Drosophila knockout of Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. Roles of Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix _like superfamily.


Pssm-ID: 185767  Cd Length: 350  Bit Score: 58.51  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  35 FKWTDTLQGqVPSAQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SHLPKLit 112
Cdd:cd09244   85 FHWYDSLTG-VPSVQRSVAFEKASVLFNIGALYTQIGAK---QDRTTEEGIEAAVDAFQRAAGAFNYLREnfSNAPSM-- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 113 paekgrDLESRLIEAYVIQCQAEAQEVT---IARAIELKHAPGLIAALAYETANF---YQKAdHTLSSLEPA-----YSa 181
Cdd:cd09244  159 ------DLSPEMLEALIKLMLAQAQECVfekLVLPGEDSKDIQACLDLAQEAAQVsdcYSEV-HKLMNQEPVkdyipYS- 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071 182 kWRKYLHLKMCFYTAYAYCYHGETLLASDK-------CGEAIRSLQEAEKLYakaeALCKEygetkgpgPTVKPSGHLFF 254
Cdd:cd09244  231 -WISLVEVKSEHYKALAHYYAAMGLLLEERrllgkahLKEALLLHEEALRLH----RMCRF--------LRNVDSLQEVL 297
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530366071 255 RKLGNLVKNTLEKCQRENGFiyfqKIPTEAPQLELKANYGLvEPIPFEF 303
Cdd:cd09244  298 KEAHDRSLNKYSSLEEEDDF----SDALDAPDIQAKTKQQL-EIIPPDF 341
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
8-207 2.30e-05

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily contains the Bro1-like domain of RhoA-binding protein, Rhophilin-2. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-1, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-2, binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-2 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Roles for Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. Rhophilin-2 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185772  Cd Length: 385  Bit Score: 46.00  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071   8 SYFSLLqGFInsldESTQESKLRYIQN-FKWTDTLQGqVPSAQQDAVFELISMGFNVALWYTKYASR-----LAGKENIT 81
Cdd:cd09249   62 SYFSQL-GFL----ENRFFPPTRQMGIlFTWYDSFTG-VPVSQQNLLLEKASILFNIGALYTQIGTRcnrqtQAGLESAV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  82 EdeakevhrSLKIAAGIFKHLKE--SHLPKLitpaekgrDLESRLIEAYVIQCQAEAQEVTIARAIelkhAPGL------ 153
Cdd:cd09249  136 D--------AFQRAAGVLNYLKEtfTHTPSY--------DMSPAMLSVLVKMMLAQAQECLFEKIS----LPGIrnefft 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530366071 154 ---IAALAYETANFYQKAdHTLSSLEPA-----YSakWRKYLHLKMCFYTAYAYCYHGETLL 207
Cdd:cd09249  196 lvkMAQEAAKVGEVYMQV-HTAMNQAPVkenipYS--WSSLVQVKAHHYNALAHYFVATLLI 254
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
35-132 6.64e-04

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily contains the Bro1-like domain of the RhoA-binding protein, Rhophilin-1. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding protein Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 binds both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 contains an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. The Drosophila knockout of the Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Rhophilin-1 lacks the V-shaped (V) domain found in many members of the BRO1_Alix_ like superfamily.


Pssm-ID: 185771  Cd Length: 384  Bit Score: 41.40  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530366071  35 FKWTDTLQGqVPSAQQDAVFELISMGFNVALWYTKYASRlagKENITEDEAKEVHRSLKIAAGIFKHLKE--SHLPKLIT 112
Cdd:cd09248   85 FHWYDSLTG-VPAQQRALAFEKGSVLFNIGALHTQIGAR---QDRSCTEGTRRAIDAFQRAAGAFSLLREnfSNAPSPDM 160
                         90       100
                 ....*....|....*....|
gi 530366071 113 PAEKGRDLEsRLIEAYVIQC 132
Cdd:cd09248  161 STASLSMLE-QLMVAQAQEC 179
 
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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