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Conserved domains on  [gi|193617669|ref|XP_001945718|]
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programmed cell death 6-interacting protein [Acyrthosiphon pisum]

Protein Classification

BRO1_Alix and V_Alix domain-containing protein( domain architecture ID 10174044)

BRO1_Alix and V_Alix domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 364-700 0e+00

Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction modules; This family contains the middle V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X) and related domains. It belongs to the V_Alix_like superfamily which includes the V-domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), is part of the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in membrane remodeling processes, including the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), the abscission reactions of mammalian cell division, and in apoptosis. The Alix V-domain is a dimerization domain, and contains a binding site, partially conserved in the V_Alix_like superfamily, for the retroviral late assembly (L) domain YPXnL motif. In addition to the V-domain, Alix also has an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex, in particular CHMP4. The Bro1-like domain of Alix can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. 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: 185748  Cd Length: 339  Bit Score: 560.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEIGKLRESTQILNGCLASLNLPAALEDVKGVGIPQSLVEKSNSLRMNGGVQKLENMIRE 443
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 444 LPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIHKRA 523
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 524 IYLLSEGQEAMQNVLPVGSSSGVNfANSTAADKLKHLMEEVEVLKNERDVIETELKCATTDMKSKFLNALSEEGSIHEAN 603
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTL-QGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 604 LSTESLDQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKSSGG---QREALFKDLASGYDVFNDLQSNLVEGTKFYN 680
Cdd:cd09235  240 ISVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSganEREEVLKDLAAAYDAFMELTANLKEGTKFYN 319

                        330       340
                 ....*....|....*....|
gi 193617669 681 DLTEILITAQNKISDFCFAR 700
Cdd:cd09235  320 DLTEILVKFQNKCSDFVFAR 339
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 5-349 0e+00

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: 527.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   5 TSLLAVPTKRASEVNIVKPLRNLISSHYNSADNPEDYTEAINELSKLRSQALWKVLDKYDNSLELIYTYYDQMTSLESKV 84
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSGEEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  85 PSSE--VQIPFKWKDAFNKMTSFFanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIF 162
Cdd:cd09240   81 PFSEsqIQVTFTWKDAFDKGSLFG--GSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 163 NTLKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMERETVMMSV 242
Cdd:cd09240  159 NHLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDVRSLL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 243 DKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCARSY-YNELLNKAIQELNEAKKDNDF 321
Cdd:cd09240  239 PKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVdVKDFAAKISRALTAAKKDNDF 318

                        330       340
                 ....*....|....*....|....*...
gi 193617669 322 IYHERIPDVKHLELISKVIIAKPTPVPS 349
Cdd:cd09240  319 IYHDRVPDVKSLPPIGKAALAKPTPVNV 346
 
Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 364-700 0e+00

Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction modules; This family contains the middle V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X) and related domains. It belongs to the V_Alix_like superfamily which includes the V-domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), is part of the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in membrane remodeling processes, including the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), the abscission reactions of mammalian cell division, and in apoptosis. The Alix V-domain is a dimerization domain, and contains a binding site, partially conserved in the V_Alix_like superfamily, for the retroviral late assembly (L) domain YPXnL motif. In addition to the V-domain, Alix also has an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex, in particular CHMP4. The Bro1-like domain of Alix can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. 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: 185748  Cd Length: 339  Bit Score: 560.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEIGKLRESTQILNGCLASLNLPAALEDVKGVGIPQSLVEKSNSLRMNGGVQKLENMIRE 443
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 444 LPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIHKRA 523
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 524 IYLLSEGQEAMQNVLPVGSSSGVNfANSTAADKLKHLMEEVEVLKNERDVIETELKCATTDMKSKFLNALSEEGSIHEAN 603
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTL-QGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 604 LSTESLDQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKSSGG---QREALFKDLASGYDVFNDLQSNLVEGTKFYN 680
Cdd:cd09235  240 ISVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSganEREEVLKDLAAAYDAFMELTANLKEGTKFYN 319

                        330       340
                 ....*....|....*....|
gi 193617669 681 DLTEILITAQNKISDFCFAR 700
Cdd:cd09235  320 DLTEILVKFQNKCSDFVFAR 339
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 5-349 0e+00

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: 527.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   5 TSLLAVPTKRASEVNIVKPLRNLISSHYNSADNPEDYTEAINELSKLRSQALWKVLDKYDNSLELIYTYYDQMTSLESKV 84
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSGEEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  85 PSSE--VQIPFKWKDAFNKMTSFFanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIF 162
Cdd:cd09240   81 PFSEsqIQVTFTWKDAFDKGSLFG--GSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 163 NTLKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMERETVMMSV 242
Cdd:cd09240  159 NHLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDVRSLL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 243 DKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCARSY-YNELLNKAIQELNEAKKDNDF 321
Cdd:cd09240  239 PKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVdVKDFAAKISRALTAAKKDNDF 318

                        330       340
                 ....*....|....*....|....*...
gi 193617669 322 IYHERIPDVKHLELISKVIIAKPTPVPS 349
Cdd:cd09240  319 IYHDRVPDVKSLPPIGKAALAKPTPVNV 346
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 7-382 2.88e-128

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: 388.09  E-value: 2.88e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669    7 LLAVPTKRASEVNIVKPLRNLISSHYnSADNPEDYTEAINELSKLRSQALWKVLDKyDNSLELIYTYYDQMTSLESKVP- 85
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTY-GSQDPSSFEDDLAELNKLRQDAVRGANED-ESGLDLLYKYYAQLELLELRFPi 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   86 SSEVQIPFKWKDAFNKmtsffanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNTL 165
Cdd:pfam03097  79 DIQIGIEFTWYDAFGT-------SSKKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  166 KTTVMNviqqDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMEretVMMSVDKE 245
Cdd:pfam03097 152 KENFLH----APSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALK---LSGLIDKE 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  246 WTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCARSYYNELLN---KAIQE-LNEAKKDNDF 321
Cdd:pfam03097 225 WISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALKSDRYKKVLEDLKgllDVVEEkLKRAEKDNDF 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193617669  322 IYHERIPDVKHLELISKVIIAKPTPVPSRFSS-KFKDLFEDLVPISVQQALSAYEVRKTELV 382
Cdd:pfam03097 305 IYHERVPSESSLPPIKPASMVKPIPPLELYPFqIGPDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 7-386 3.69e-106

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: 331.24  E-value: 3.69e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669     7 LLAVPTKRASEVNIVKPLRNLISSHYNsaDNPEDYTEAINELSKLRSQALWkvLDKYDNSLELIYTYYDQMTSLESKVPS 86
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYS--EDSSSYEDEIAELNRLRQAART--PSRDESGLELLLKYYGQLEALELRFPP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669    87 SEVQ--IPFKWKDAFNkmtsffanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNT 164
Cdd:smart01041  77 PEGQlkLSFTWYDSLD--------TGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   165 LKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMK--DQTIAKLCAQCEEYYAETVKMMERETVMMS- 241
Cdd:smart01041 149 LKENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGy 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   242 VDKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQE--RCARSYYNELLNKAIQ--------E 311
Cdd:smart01041 229 IPKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKhlRCKKLGKADKLQEDLSglkdvveeK 308

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193617669   312 LNEAKKDNDFIYHERIPDVKHLELISKVIIAKPTPVPSrfSSKFKDLFEDLVPISVQQALSAYEVRKTELVNSEI 386
Cdd:smart01041 309 LKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSE--VLKGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 416-703 1.11e-89

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 284.90  E-value: 1.11e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  416 GIPQSLVEKSNSLRMNGGVQKLENMIRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVN 495
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  496 ITKYREIIKNAKSADKMIHEKFEIHKRAIYLLSEGQEAMQNVLPVGSSSGVNFANSTAADKLKHLMEEVEVLKNERDVIE 575
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKNSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  576 TELK--CATTDMKSKFLNALSEEGSI-HEANLSTESLDQsYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKSSGG--- 649
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPnQEEQLFEEELEK-YDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSekq 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193617669  650 -QREALFKDLASGYDVFNDLQSNLVEGTKFYNDLTEILITAQNKISDFCFARKAE 703
Cdd:pfam13949 240 rQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 408-521 8.37e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 408 ALEDVKGVGIPQSLVEK------SNSLRMNGGVQKLENMIRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWN 481
Cdd:PRK00409 490 AFEIAKRLGLPENIIEEakkligEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLE 569

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 193617669 482 RTKSnvltqvfkvnitKYREIIKNAKS-ADKMIHEKFEIHK 521
Cdd:PRK00409 570 EAEK------------EAQQAIKEAKKeADEIIKELRQLQK 598
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 379-634 8.46e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 379 TELVNSEIGKLRESTQILNGCLAslNLPAALEDVKgvgipQSLVEKSNSLRMNGGVQKLENMIRELpELLKRNEEIINES 458
Cdd:COG5185  263 TDLRLEKLGENAESSKRLNENAN--NLIKQFENTK-----EKIAEYTKSIDIKKATESLEEQLAAA-EAEQELEESKRET 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 459 ERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIHKRAIylLSEGQEAMQNVL 538
Cdd:COG5185  335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQ--RGYAQEILATLE 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 539 PVGSSSGVNFANSTAAdkLKHLMEEVEVLKNERDVIETELKCATTDMKSKFLNALSEEGSIHEANLST---------ESL 609
Cdd:COG5185  413 DTLKAADRQIEELQRQ--IEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSkkedlneelTQI 490

                        250       260
                 ....*....|....*....|....*
gi 193617669 610 DQSYGHLKAQVNDSLARQEKLLSNI 634
Cdd:COG5185  491 ESRVSTLKATLEKLRAKLERQLEGV 515
 
Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 364-700 0e+00

Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction modules; This family contains the middle V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X) and related domains. It belongs to the V_Alix_like superfamily which includes the V-domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), is part of the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in membrane remodeling processes, including the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), the abscission reactions of mammalian cell division, and in apoptosis. The Alix V-domain is a dimerization domain, and contains a binding site, partially conserved in the V_Alix_like superfamily, for the retroviral late assembly (L) domain YPXnL motif. In addition to the V-domain, Alix also has an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex, in particular CHMP4. The Bro1-like domain of Alix can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. 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: 185748  Cd Length: 339  Bit Score: 560.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEIGKLRESTQILNGCLASLNLPAALEDVKGVGIPQSLVEKSNSLRMNGGVQKLENMIRE 443
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 444 LPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIHKRA 523
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 524 IYLLSEGQEAMQNVLPVGSSSGVNfANSTAADKLKHLMEEVEVLKNERDVIETELKCATTDMKSKFLNALSEEGSIHEAN 603
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTL-QGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 604 LSTESLDQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKSSGG---QREALFKDLASGYDVFNDLQSNLVEGTKFYN 680
Cdd:cd09235  240 ISVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSganEREEVLKDLAAAYDAFMELTANLKEGTKFYN 319

                        330       340
                 ....*....|....*....|
gi 193617669 681 DLTEILITAQNKISDFCFAR 700
Cdd:cd09235  320 DLTEILVKFQNKCSDFVFAR 339
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 5-349 0e+00

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: 527.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   5 TSLLAVPTKRASEVNIVKPLRNLISSHYNSADNPEDYTEAINELSKLRSQALWKVLDKYDNSLELIYTYYDQMTSLESKV 84
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSGEEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  85 PSSE--VQIPFKWKDAFNKMTSFFanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIF 162
Cdd:cd09240   81 PFSEsqIQVTFTWKDAFDKGSLFG--GSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 163 NTLKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMERETVMMSV 242
Cdd:cd09240  159 NHLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDVRSLL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 243 DKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCARSY-YNELLNKAIQELNEAKKDNDF 321
Cdd:cd09240  239 PKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVdVKDFAAKISRALTAAKKDNDF 318

                        330       340
                 ....*....|....*....|....*...
gi 193617669 322 IYHERIPDVKHLELISKVIIAKPTPVPS 349
Cdd:cd09240  319 IYHDRVPDVKSLPPIGKAALAKPTPVNV 346
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 7-382 2.88e-128

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: 388.09  E-value: 2.88e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669    7 LLAVPTKRASEVNIVKPLRNLISSHYnSADNPEDYTEAINELSKLRSQALWKVLDKyDNSLELIYTYYDQMTSLESKVP- 85
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTY-GSQDPSSFEDDLAELNKLRQDAVRGANED-ESGLDLLYKYYAQLELLELRFPi 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   86 SSEVQIPFKWKDAFNKmtsffanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNTL 165
Cdd:pfam03097  79 DIQIGIEFTWYDAFGT-------SSKKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  166 KTTVMNviqqDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMEretVMMSVDKE 245
Cdd:pfam03097 152 KENFLH----APSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALK---LSGLIDKE 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  246 WTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCARSYYNELLN---KAIQE-LNEAKKDNDF 321
Cdd:pfam03097 225 WISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKEALKSDRYKKVLEDLKgllDVVEEkLKRAEKDNDF 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193617669  322 IYHERIPDVKHLELISKVIIAKPTPVPSRFSS-KFKDLFEDLVPISVQQALSAYEVRKTELV 382
Cdd:pfam03097 305 IYHERVPSESSLPPIKPASMVKPIPPLELYPFqIGPDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 7-386 3.69e-106

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: 331.24  E-value: 3.69e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669     7 LLAVPTKRASEVNIVKPLRNLISSHYNsaDNPEDYTEAINELSKLRSQALWkvLDKYDNSLELIYTYYDQMTSLESKVPS 86
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETYS--EDSSSYEDEIAELNRLRQAART--PSRDESGLELLLKYYGQLEALELRFPP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669    87 SEVQ--IPFKWKDAFNkmtsffanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNT 164
Cdd:smart01041  77 PEGQlkLSFTWYDSLD--------TGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNY 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   165 LKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMK--DQTIAKLCAQCEEYYAETVKMMERETVMMS- 241
Cdd:smart01041 149 LKENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGy 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   242 VDKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQE--RCARSYYNELLNKAIQ--------E 311
Cdd:smart01041 229 IPKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEAKKhlRCKKLGKADKLQEDLSglkdvveeK 308

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193617669   312 LNEAKKDNDFIYHERIPDVKHLELISKVIIAKPTPVPSrfSSKFKDLFEDLVPISVQQALSAYEVRKTELVNSEI 386
Cdd:smart01041 309 LKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSE--VLKGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 416-703 1.11e-89

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 284.90  E-value: 1.11e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  416 GIPQSLVEKSNSLRMNGGVQKLENMIRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVN 495
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  496 ITKYREIIKNAKSADKMIHEKFEIHKRAIYLLSEGQEAMQNVLPVGSSSGVNFANSTAADKLKHLMEEVEVLKNERDVIE 575
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKNSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  576 TELK--CATTDMKSKFLNALSEEGSI-HEANLSTESLDQsYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKSSGG--- 649
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPnQEEQLFEEELEK-YDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSekq 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193617669  650 -QREALFKDLASGYDVFNDLQSNLVEGTKFYNDLTEILITAQNKISDFCFARKAE 703
Cdd:pfam13949 240 rQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 7-369 3.68e-69

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: 232.54  E-value: 3.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   7 LLAVPTKRASEVNIVKPLRNLISSHYNSAdnPEDYTEAINELSKLRSQALwkVLDKYDNSLELIYTYYDQMTSLESKVPs 86
Cdd:cd09241    2 LLSIPFKRTLPVDLKDALRNYISNHYFQT--PSSFEDDLAEIDKLRNDAI--NPEPSVNGLSLLKEYYAQLVVLSKKFP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  87 sEVQIPFKWKDAFnkmtSFFANGKVSITlcSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNTLK 166
Cdd:cd09241   77 -DDQLEFTWYPTL----GYKSSGPVSLS--SLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYIL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 167 TTVMNVIqqDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMERETvmmSVDKEW 246
Cdd:cd09241  150 QHLLPTL--SPPPDLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSD---LIRSDW 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 247 TSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVG---QERCARSYYNEL--LNKAIQE-LNEAKKDND 320
Cdd:cd09241  225 INHLKVKKHHFKAAAHYRMALVALEKSKYGEEVARLRVALAACKEAlkeARYGNKAVLEDLqgLKDIVKEsLKRAERDND 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193617669 321 FIYHERIPDVKHLELISKVIIAKPTpVPSRFSSKFKD---LFEDLVPISVQQ 369
Cdd:cd09241  305 LIYLQPVPPASELPPIKPASMVKAI-VPPELEEGSKLgkpLFKDLLPYGVHE 355
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 7-349 1.17e-64

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: 220.35  E-value: 1.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   7 LLAVPTKRASEVNIVKPLRNLISSHYnSADNPEDYTEAINELSKLRSQALwKVLDKYDNSLELIYTYYDQMTSLESKVPS 86
Cdd:cd09246    1 MLSIHRKKTETVDLVSPLRAYISETY-SEREAQDAEDDLAELQQLRSEVR-TLQEKHAASRELLLRYYRALCAVESRFPI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  87 SE----VQIPFKWKDAFNkmtsffanGKVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIF 162
Cdd:cd09246   79 SEesghARVSFSWYDAFR--------PHRKATQANVHFEKAAVLFNLGALSSQLGLQQDRTTAEGIKQACHAFQAAAGAF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 163 NTLKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMMERETVMMSV 242
Cdd:cd09246  151 AHLRDKVSGKTGGFRTPDLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEALDSPPLKGHF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 243 DKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFL-------KVGQERCARSYYNELLNKAIQELNEA 315
Cdd:cd09246  231 DKSWVAHVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALaearkqaKGVNGDELIEAVSELEQVINELLERA 310

                        330       340       350
                 ....*....|....*....|....*....|....
gi 193617669 316 KKDNDFIYHERIPDVKHLELISKVIIAKPTPVPS 349
Cdd:cd09246  311 EKENDCVYLDRVPAPSDLPPLGAASMVKPAAPPA 344
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 7-348 7.78e-63

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: 215.22  E-value: 7.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   7 LLAVPTKRASEVNIVKPLRNLISSHYNSadNPEDYTEAINELSKLRSQAlwkVLDKYDNS-LELIYTYYDQMTSLESKVP 85
Cdd:cd09242    1 LISLPLKDTEEVDWKKPLSSYLKRSYGS--STFYYEEEIAEFDRLRQDA---NGVLADETgRDLLYKYYGQLELLELRFP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  86 SSEVQI--PFKWKDAFNKMTSFfangkvsiTLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFN 163
Cdd:cd09242   76 FNNKELkvDFTWYDAFYKSKKV--------KQHSLAFEKASVLFNIGALLSQLAAEKYREDEDDLKEAITNLQQAAGCFQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 164 TLKTTVMNViqqdPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDK---MKDQTIAKLCAQCEEYYAETVKMMERE--TV 238
Cdd:cd09242  148 YINENFLHA----PSVDLQQENVKFLVKLMLAQAQEIFLLKLINGDdaqKKASLISKLASATANLYESCVEFLKEIqeKG 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 239 MMSVDKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLK---------VGQERCARSYYNELLnKAI 309
Cdd:cd09242  224 ISYGDPKWISLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKeanpqklslKASAGDAAYALNDDF-KGQ 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 193617669 310 QE-----LNEAKKDNDFIYHERIPDVKHLELISKVIIAKPTPVP 348
Cdd:cd09242  303 KDtveekLKELEKDNDFIYHDIVPSEVTLPSIKPLDAAKPIPIE 346
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 7-347 7.68e-52

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: 184.48  E-value: 7.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   7 LLAVPTKRASEVNIVKPLRNLISSHYNSAdNPEDYTEAINELSKLRSQALWKVLDKYDNS--LELIYTYYDQMTSLESKV 84
Cdd:cd09034    1 FIGLPLKKTKEVDVKVPLSKFIPKNYGEL-EATAVEDLIEKLSKLRNNIVTEQNNDTTCEnlLEALKEYLPYLLGLEKKL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  85 PSS--EVQIPFKWKDAFNKmtsffangKVSITLcSFAYERICVLFNIAAQQSAIASAQNL-ETDDGLKMAAKLLQQSAGI 161
Cdd:cd09034   80 PFQklRDNVEFTWTDSFDT--------KKESAT-SLRYELLSILFNLAALASQLANEKLItGSEEDLKQAIKSLQKAAGY 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 162 FNTLKTTVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKM-KDQTIAKLCAQCEEYYAE---TVKMMERET 237
Cdd:cd09034  151 FEYLKEHVLPLPPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKaKLSLLARLACEAAKYYEEalkCLSGVDLET 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 238 VmMSVDKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCA------RSYYNELLNKAIQE 311
Cdd:cd09034  231 I-KNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKsflldvWGNLKKLKEKIEKE 309

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 193617669 312 LNEAKKDNDFIYHERIPDVKHLELISKVIIAKPTPV 347
Cdd:cd09034  310 LEKAERENDFIYFEEVPPEDPLPEIKGALLVKPPPL 345
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 364-700 6.83e-49

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all 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. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 176.38  E-value: 6.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEI-GKLRESTQILNGCLASLNLPAALEDVKGVGIPQSLVEKSNSLRMNGGVQKLENMIR 442
Cdd:cd08915    1 PYDVIESASAYNERQDDYVREHIvEPIEALNKLLNSFLAERNLPASIDDLQKPENLPDSIQHSQEIIEEGGLDNIEQSFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 443 ELPELLKRNEEIINESERMLNEEQASDEQLQAQFKE-KWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIHK 521
Cdd:cd08915   81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTlRWRRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 522 RAIYLLSEGQEAMQNVLPVGSSSGVNFANSTAADkLKHLMEEVEVLKNERDVIETELKCATT--DMKSKFLNALSEEGSI 599
Cdd:cd08915  161 PNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSS-LRPLLNEVSELEKERERFISELEIKSRnnDILPKLITEYKKNGTT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 600 HEANLSTESLdQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKSSGG---QREALFKDLASGYDVFNDLQSNLVEGT 676
Cdd:cd08915  240 EFEDLFEEHL-KKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSNDsldPREEALQDLEASYKKYLELKENLNEGS 318

                        330       340
                 ....*....|....*....|....
gi 193617669 677 KFYNDLTEILITAQNKISDFCFAR 700
Cdd:cd08915  319 KFYNDLIEKVNRLLEECEDFVNAR 342
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 7-347 9.98e-46

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: 167.99  E-value: 9.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   7 LLAVPTKRASEVNIVKPLRNLISSHYNsaDNPEDYTEAINELSKLRSQALWKVLDKydNSLELIYTYYDQMTSLESKVPS 86
Cdd:cd09239    8 MLWLQLKSSGEFTFQPALKKYILENYG--EDPELYSEELKSLEQLRQEAVNPPRDF--EGCSVLKRYYGQLHLLQSRFPM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  87 SEVQ---IPFKWKDAFNKMTsffangkvsITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFN 163
Cdd:cd09239   84 GAGQeaaVPFTWTDIFSGSE---------VTHEDIKFEEASVLYNIGALHSQLGASDKRDSEEGMKVACTHFQCAAWAFA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 164 TLKTTVMNVIQQDptpDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCAQCEEYYAETVKMME-----RETV 238
Cdd:cd09239  155 YLREHYPQVYGAV---DMSSQLLSFNYSLMLAQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRALEnwesnSKII 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 239 MMSVDKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIA-------RLNVAISFLKvGQErcARSYYNELLNKAIQ- 310
Cdd:cd09239  232 LGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVAyyqlandKLEEAIKNAK-GQP--DTVNLQEALSFTMDv 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193617669 311 ---ELNEAKKDNDFIYHERIPDVKHLELISKVIIAKPTPV 347
Cdd:cd09239  309 iggKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPF 348
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
 364-687 2.68e-40

Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.


Pssm-ID: 185749 [Multi-domain]  Cd Length: 353  Bit Score: 152.13  E-value: 2.68e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVN-SEIGKLRESTQILNGCLASLNLPAALEDV-KGVGIPQSLVEKSNSLRMNGGVQKLENMI 441
Cdd:cd09236    1 PFGVHLAISIYDDRKDRLVNeSIIDELEELTNRAHSTLRSLNLPGSLQALeKPLGLPPSLLRHAEEIRQEDGLERIRASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 442 RELPELLKRNEEIINESERMLNEEQASDEQLQAQF-KEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIH 520
Cdd:cd09236   81 DDVARLAASDRAILEEAMDILDDEASEDESLRRKFgTDRWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRRKLDEW 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 521 KRAIYLLSEGQEAMQNVLPvgSSSGVNFANST--AADKLKHLMEEVEVLKNERD--VIETELKCATTDMKSKFL---NAL 593
Cdd:cd09236  161 EDLIQILTGDERDLENFVP--SSRRPSIPPELerHVRALRVSLEELDRLESRRRrkVERARTKARADDIRPEILreaARL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 594 SEEGSIHEANLS-----TESLDQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFCREKS---SGGQREALFKDLASGYDVF 665
Cdd:cd09236  239 EREYPATEVAPAhfedlFDKRLAKYDKDLDAVSEEAQEQEEILQQIEVANKAFLQSRKgdpATKERERALQSLDLAYFKY 318

                        330       340
                 ....*....|....*....|..
gi 193617669 666 NDLQSNLVEGTKFYNDLTEILI 687
Cdd:cd09236  319 KEIVSNLDEGRKFYNDLAKILS 340
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
 13-359 6.58e-33

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: 130.54  E-value: 6.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  13 KRASEVNIVKPLRNLISSHYnSADnPEDYTEAINELSKLRSQALWKVLDKydNSLELIYTYYDQMTSLESKV--PSSEVQ 90
Cdd:cd09244    7 KETKEIDFMEPFKDFILEHY-SED-PSLYEDEIADFTDLRQAMRTPSRDE--AGIELLFEYYNQLYFVERRFfpPDRSLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  91 IPFKWKDAFNKmtsffangkVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNTLKTTVM 170
Cdd:cd09244   83 IYFHWYDSLTG---------VPSVQRSVAFEKASVLFNIGALYTQIGAKQDRTTEEGIEAAVDAFQRAAGAFNYLRENFS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 171 NViqqdPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTI------AKLCAQCEEYYAETVKMMERETVMMSVDK 244
Cdd:cd09244  154 NA----PSMDLSPEMLEALIKLMLAQAQECVFEKLVLPGEDSKDIqacldlAQEAAQVSDCYSEVHKLMNQEPVKDYIPY 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 245 EWTSNVYGKQSIFHGLAQYYQAMVcknnkTVGEQIARLnvAISFLK---VGQERCAR---------------SYYNELLN 306
Cdd:cd09244  230 SWISLVEVKSEHYKALAHYYAAMG-----LLLEERRLL--GKAHLKealLLHEEALRlhrmcrflrnvdslqEVLKEAHD 302

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193617669 307 KAIQELNEAKKDNDFIYHERIPDVKHLeliSKviiAKPTPVPSRFSS-KFKDLF 359
Cdd:cd09244  303 RSLNKYSSLEEEDDFSDALDAPDIQAK---TK---QQLEIIPPDFTQvKVKDLF 350
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 13-269 3.98e-23

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: 102.27  E-value: 3.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  13 KRASEVNIVKPLRNLISSHYnsADNPEDYTEAINELSKLRsQALwKVLDKYDNSLELIYTYYDQMTSLESKV--PSSEVQ 90
Cdd:cd09248    7 KETKELDLPTPLKELISEHF--GEDGTSYEAEIRELEDLR-QAM-RTPSRSEAGLELLMAYYNQLCFLDARFfpPAKSLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  91 IPFKWKDAfnkMTSFFANGKvsitlcSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNTLKTTVM 170
Cdd:cd09248   83 LFFHWYDS---LTGVPAQQR------ALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLLRENFS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 171 NViqqdPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQTI--AKLC-----AQCEEYYAETVKMMERETVMMSVD 243
Cdd:cd09248  154 NA----PSPDMSTASLSMLEQLMVAQAQECIFEGLLLPLLATPQDffAQLQlaqeaAQVAAEYRLVHRTMAQPPVRDYVP 229

                        250       260
                 ....*....|....*....|....*.
gi 193617669 244 KEWTSNVYGKQSIFHGLAQYYQAMVC 269
Cdd:cd09248  230 FSWTALVHVKAEHFCALAHYHAAMAL 255
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
 364-700 6.72e-23

Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This domain family is comprised of uncharacterized plant proteins. It belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), (His-Domain) type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. 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. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_Rim20_Bro1_like superfamily also have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members of the V_Alix_like superfamily also have a proline-rich region (PRR).


Pssm-ID: 185751  Cd Length: 339  Bit Score: 101.01  E-value: 6.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEIGKLRESTQILNGCLASLNLPAALEDVKG---VGIPQSLVEKSNSLRMNGGVQKLENM 440
Cdd:cd09238    1 PESSAKALSKYTEMVDELIRTEADRLAAASDEARVALREMELPETLIALDGgasLPGDLGLDEEVEAVQISGGLAALEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 441 IRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIH 520
Cdd:cd09238   81 LPRLRELRRVCTELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFRVNLEQAGDSDESLRRRIEDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 521 KRAIYLLSEgqEAMQNVLPVGSSSGVNFA--NSTAADKLKHLMEEVEVLKNERDVIETELKcattDMKSK--FLNALSEE 596
Cdd:cd09238  161 MDGMLILDD--EPAAAAAPTLRAPMLSTDedDASIVGTLRSNLEELEALGNERAGIEDMMK----ALKRNdnILAKVMAT 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 597 GSIHEANLSTESldQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFCR-----------EKSSGGQREALFKdlasgydvF 665
Cdd:cd09238  235 TGSYDALFKEEL--KKYDSVREAVSKNISSQDDLLSRLRALNEKFSQifdvegwraatESHATQIRAAVAK--------Y 304

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 193617669 666 NDLQSNLVEGTKFYNDLTEILITAQNKISDFCFAR 700
Cdd:cd09238  305 RELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR 339
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
 7-268 5.13e-19

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: 89.91  E-value: 5.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669   7 LLAVPTKRASEVNIVKPLRNLISSHYnSADNPEdYTEAINELSKLRsQALwKVLDKYDNSLELIYTYYDQMTSLESKV-- 84
Cdd:cd09249    1 LIPLGLKETKDVDFSVPLKDFILEHY-SEDGSE-YEDEIADLMDLR-QAC-RTPSRDEAGVELLMSYFSQLGFLENRFfp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  85 PSSEVQIPFKWKDAFNKmtsffangkVSITLCSFAYERICVLFNIAAQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNT 164
Cdd:cd09249   77 PTRQMGILFTWYDSFTG---------VPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTQAGLESAVDAFQRAAGVLNY 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 165 LKTTVMNViqqdPTPDLNPDTLAMLSSLMLAQAQEVFIVKANIDKMKDQ-----TIAKLCAQCEEYYAETVKMMERETVM 239
Cdd:cd09249  148 LKETFTHT----PSYDMSPAMLSVLVKMMLAQAQECLFEKISLPGIRNEfftlvKMAQEAAKVGEVYMQVHTAMNQAPVK 223

                        250       260
                 ....*....|....*....|....*....
gi 193617669 240 MSVDKEWTSNVYGKQSIFHGLAQYYQAMV 268
Cdd:cd09249  224 ENIPYSWSSLVQVKAHHYNALAHYFVATL 252
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 141-347 2.19e-18

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: 87.45  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 141 NLETDDgLKMAAKLLQQSAGIFNTLKTTVMNVIQQDP-TPDLNPDTLAMLSSLM----LAQAQEVFIVKANIDKMKDQTI 215
Cdd:cd09247  130 VLPTED-FKEAATHLRRAAGVFEFLAHDELPRLRGALsADERPPECTPSLALAMsllcLAEAQAVTARKAEEKGTSPSLL 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 216 AKLCAQCEEYYAETVKMM-ERETVMMSVDKEWTSNVYGKQSIFHGLAQYYQAMVCKNNKTVGEQIARL---NVAISFLKV 291
Cdd:cd09247  209 AKLHYGATQFLEEAKNVLrSLATDLKDLDPRFLRFISSCIALHEARSQLYLARRLKEAGHIGVAVGVLreaLRNLKKKLP 288

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 193617669 292 GQERCARSYYNELLNKAIQELNEAKKDNDFIYHERIPDVKHLELISKVIIAKPTPV 347
Cdd:cd09247  289 GSDISSPVIFRDERAEVATLLQKYEKENEVIYFEKVPDIDELPLPEGKVIVKPVPY 344
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 364-696 1.13e-14

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to 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 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: 185747 [Multi-domain]  Cd Length: 337  Bit Score: 76.18  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEIGKLRESTQILNGCLASLNLPA---ALEDVKgVGIPQSLVEKSNSLRMN-GGVQKLEN 439
Cdd:cd09234    1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPlnvMDMDGQ-FELPQDLVERCAALSVRpDTIKNLVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 440 MIRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEkwnRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEI 519
Cdd:cd09234   80 AMGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVGK---RGSSIAHVTELKRELKKYKEAHEKASQSNTELHKAMNL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 520 HKRAIYLLSEGQEAMQNVLPVGSSSGVNFANStAADKLKHLMEEVEVLKNERDVIETELKCATT--DMKSKFLnalseeg 597
Cdd:cd09234  157 HIANLKLLAGPLDELQKKLPSPSLLDRPEDEA-IEKELKRILNKVNEMRKQRRSLEQQLRDAIHedDITSKLV------- 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 598 SIHEANLST--ESLDQSYGHLKAQVNDSLARQEKLLSNIQVVNSEFC--REKSS--GGQREALFKDLASGYDVFNDLQSN 671
Cdd:cd09234  229 TTTGGDMEDlfKEELKKHDQLVNLIEQNLAAQENILKALTEANAKYApvRKALSetKQKRESTISSLIASYEAYEDLLKK 308

                        330       340
                 ....*....|....*....|....*
gi 193617669 672 LVEGTKFYNDLteilitaQNKISDF 696
Cdd:cd09234  309 SQKGIDFYKKL-------EGNVSKL 326
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 364-686 3.83e-13

Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.


Pssm-ID: 185750 [Multi-domain]  Cd Length: 356  Bit Score: 71.55  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 364 PISVQQALSAYEVRKTELVNSEIGKLRESTQILNGCLASLNLPAALEDVKgvgipqSLVEKSNSLRMNGGVQK---LENM 440
Cdd:cd09237    1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLK------ERFEGENELMEIVSGLKsssVDSQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 441 IRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIH 520
Cdd:cd09237   75 LELLRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 521 KRAIYLLSEGQEAmQNVLPVGSSSGVN--------FANSTAA-----DKLKHLMEEVEVLKNERDVIETELK--CATTDM 585
Cdd:cd09237  155 KEDIALLLNGGSL-WEELFGFSSSGSPepslldldDSQNEQTvlkqiKQLEELLEDLNLIKEERQRVLKDLKqkIHNDDI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 586 KSKFL----NALSEEGSIHEANLS-----TESLDQSYGHLKAQVNDSLARQEKLLSNIQVVNsEFCREKSSGGQREALFK 656
Cdd:cd09237  234 SDILIlnskSKSEIEKQLFPEELEkfkplQNRLEATIFKQSSLINELKIELDKLFKLPGVKE-KQSKEKSKQKLRKEFFE 312

                        330       340       350
                 ....*....|....*....|....*....|
gi 193617669 657 DLASGYDVFNDLQSNLVEGTKFYNDLTEIL 686
Cdd:cd09237  313 KLKKAYNSFKKFSAGLPKGLEFYDDLLKMA 342
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
 143-289 9.83e-09

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: 58.19  E-value: 9.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 143 ETDDGLKMAAKLLQQSAGIFNTLKT-----TVMNVIQQDPTPDLNPDTLAMLSSLMLAQAQEVFIVK-----ANIDKMKD 212
Cdd:cd09245  154 QRDERLKAATKLLCKAAGIFDYLATrvlpqWESNRGGAPPPPDLSPEVLSALSSLALAEATLLAVRKldpypAAVDKDWM 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 213 -------------QTIAKLCAQCEEYYAETVKM---MERETVMMSVDKEWTSNVygkqsifHGLAQYYQAMVCK------ 270
Cdd:cd09245  234 tpgpplpkvhpsaHLLARLCLAASEHAESARALlstPGSKRGSGEVSEELLRYL-------SDLRRVARALACKflgida 306

                        170       180
                 ....*....|....*....|.
gi 193617669 271 --NNKtVGEQIARLNVAISFL 289
Cdd:cd09245  307 geNGK-VGEAIGWLRAAKKEL 326
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 45-346 3.73e-06

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: 50.03  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669  45 INELSKLRSQALwKVLDKYDNSLELIYTYYDQMTSL-------------ESKVPSSevqIPFKWKDAFNkmtsffanGKV 111
Cdd:cd09243   30 CSDLRTARARLL-ELLSDPSNDVDTVKTAFNAYLSLlqgfilaldgktqESKLRYL---INFKWTDSLL--------GNE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 112 SITLCSFAYERICVLFNIA---AQQSAIASAQNLETDDGLKMAAKLLQQSAGIFNTLKTTVMNVIQQDPTP--DLNPDTL 186
Cdd:cd09243   98 PSVQQDAIFELASMLFNVAlwyTKHASKLAGKEDITEDEAKDVHKSLRTAAGIFQFVKENYIPKLIEPAEKgsDLDPRVL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 187 AMLSSLMLAQAQEVFIVKANIDKMKDQTIAKLCaqceeyyAETVKMMER-ETVMMSVDKE----WTSNVYGKQSIFHGLA 261
Cdd:cd09243  178 EAYINQCTAEAQEVTVARAIELKHNAGLISALA-------YETAKLFQKaDDSLSSLDPEysgkWRKYLQLKSVFYLAYA 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 262 QYYQAMVCKNNKTVGEQIARLNVAISFLKVGQERCaRSY--------------------YNELLNKAiqeLNEAKKDNDF 321
Cdd:cd09243  251 YCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALC-KEYaktkgpgttakpdqhlffrkLGPLVKRT---LEKCERENGF 326

                        330       340
                 ....*....|....*....|....*.
gi 193617669 322 IYHERIPD-VKHLELISKVIIAKPTP 346
Cdd:cd09243  327 IYHQKVPDeVPQLELKATYGLVSPEE 352
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 408-521 8.37e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 408 ALEDVKGVGIPQSLVEK------SNSLRMNGGVQKLENMIRELPELLKRNEEIINESERMLNEEQASDEQLQAQFKEKWN 481
Cdd:PRK00409 490 AFEIAKRLGLPENIIEEakkligEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLE 569

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 193617669 482 RTKSnvltqvfkvnitKYREIIKNAKS-ADKMIHEKFEIHK 521
Cdd:PRK00409 570 EAEK------------EAQQAIKEAKKeADEIIKELRQLQK 598
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 379-634 8.46e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 379 TELVNSEIGKLRESTQILNGCLAslNLPAALEDVKgvgipQSLVEKSNSLRMNGGVQKLENMIRELpELLKRNEEIINES 458
Cdd:COG5185  263 TDLRLEKLGENAESSKRLNENAN--NLIKQFENTK-----EKIAEYTKSIDIKKATESLEEQLAAA-EAEQELEESKRET 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 459 ERMLNEEQASDEQLQAQFKEKWNRTKSNVLTQVFKVNITKYREIIKNAKSADKMIHEKFEIHKRAIylLSEGQEAMQNVL 538
Cdd:COG5185  335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQ--RGYAQEILATLE 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193617669 539 PVGSSSGVNFANSTAAdkLKHLMEEVEVLKNERDVIETELKCATTDMKSKFLNALSEEGSIHEANLST---------ESL 609
Cdd:COG5185  413 DTLKAADRQIEELQRQ--IEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSkkedlneelTQI 490

                        250       260
                 ....*....|....*....|....*
gi 193617669 610 DQSYGHLKAQVNDSLARQEKLLSNI 634
Cdd:COG5185  491 ESRVSTLKATLEKLRAKLERQLEGV 515
 
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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