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Conserved domains on  [gi|145580014|pdb|2OEX|B]
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Chain B, Programmed cell death 6-interacting protein

Protein Classification

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 ...
 9-347 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: 583.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 88
Cdd:cd09235   1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       89 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 168
Cdd:cd09235  81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      169 IVLLCKPEPELNAAIPSANPAKT*QGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFD*TSKFLTALAQDGVINEEAL 248
Cdd:cd09235 161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      249 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 328
Cdd:cd09235 241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                       330
                ....*....|....*....
2OEX_B      329 LTEILVRFQNKCSDIVFAR 347
Cdd:cd09235 321 LTEILVKFQNKCSDFVFAR 339
 
Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 9-347 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: 583.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 88
Cdd:cd09235   1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       89 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 168
Cdd:cd09235  81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      169 IVLLCKPEPELNAAIPSANPAKT*QGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFD*TSKFLTALAQDGVINEEAL 248
Cdd:cd09235 161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      249 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 328
Cdd:cd09235 241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                       330
                ....*....|....*....
2OEX_B      329 LTEILVRFQNKCSDIVFAR 347
Cdd:cd09235 321 LTEILVKFQNKCSDFVFAR 339
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 61-350 3.72e-100

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: 297.61  E-value: 3.72e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B         61 TVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAE 140
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        141 GTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAK-T*QGSEVVNVLKSLLSNLDEVKKEREGLE 219
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        220 NDLK--SVNFD*TSKFLTALAQDGVIN-EEALSVTELDrVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNE-A 295
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
2OEX_B        296 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 350
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
 
Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 9-347 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: 583.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 88
Cdd:cd09235   1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       89 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 168
Cdd:cd09235  81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      169 IVLLCKPEPELNAAIPSANPAKT*QGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFD*TSKFLTALAQDGVINEEAL 248
Cdd:cd09235 161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      249 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 328
Cdd:cd09235 241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                       330
                ....*....|....*....
2OEX_B      329 LTEILVRFQNKCSDIVFAR 347
Cdd:cd09235 321 LTEILVKFQNKCSDFVFAR 339
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 9-347 4.09e-103

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: 306.96  E-value: 4.09e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSI-AQ*REATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIK 87
Cdd:cd08915   1 PYDVIESASAYNERQDDYVREHIvEPIEALNKLLNSFLAERNLPASIDDLQKPENLPDSIQHSQEIIEEGGLDNIEQSFK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       88 ELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTP-SNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHR 166
Cdd:cd08915  81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPsSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      167 DTIVLLCKPEPELNAAIPSANPAKT*QGSEVVNVLKSLLSNLDEVKKEREGLENDL--KSVNFD*TSKFLTALAQDGVIN 244
Cdd:cd08915 161 PNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELeiKSRNNDILPKLITEYKKNGTTE 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      245 EEALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNEANLREEVLKNLATAYDNFVELVANLKEGTK 324
Cdd:cd08915 241 FEDLFEEHL-KKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSNDSLDPREEALQDLEASYKKYLELKENLNEGSK 319

                       330       340
                ....*....|....*....|...
2OEX_B      325 FYNELTEILVRFQNKCSDIVFAR 347
Cdd:cd08915 320 FYNDLIEKVNRLLEECEDFVNAR 342
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 61-350 3.72e-100

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: 297.61  E-value: 3.72e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B         61 TVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAE 140
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        141 GTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAK-T*QGSEVVNVLKSLLSNLDEVKKEREGLE 219
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        220 NDLK--SVNFD*TSKFLTALAQDGVIN-EEALSVTELDrVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNE-A 295
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
2OEX_B        296 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 350
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
 9-347 2.03e-45

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: 158.67  E-value: 2.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REA-TTLANGVLASLNLPAAIEDVSGDT-VPQSILTKSRSVIEQGGIQTVDQLI 86
Cdd:cd09236   1 PFGVHLAISIYDDRKDRLVNESIIDELEElTNRAHSTLRSLNLPGSLQALEKPLgLPPSLLRHAEEIRQEDGLERIRASL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       87 KELPELLQRNREILDESLRLLDEEEATDNDLRAKF-KERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 165
Cdd:cd09236  81 DDVARLAASDRAILEEAMDILDDEASEDESLRRKFgTDRWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRRKLDEW 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      166 RDTIVLLCKPEPELNAAIPSAN-PAKT*QGSEVVNVLKSLLSNLDEVKKEREGLENDL--KSVNFD*TSKFLTA---LAQ 239
Cdd:cd09236 161 EDLIQILTGDERDLENFVPSSRrPSIPPELERHVRALRVSLEELDRLESRRRRKVERArtKARADDIRPEILREaarLER 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      240 DGVINE------EALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNEANLREEVLKNLATAYDNFV 313
Cdd:cd09236 241 EYPATEvapahfEDLFDKRL-AKYDKDLDAVSEEAQEQEEILQQIEVANKAFLQSRKGDPATKERERALQSLDLAYFKYK 319

                       330       340       350
                ....*....|....*....|....*....|....
2OEX_B      314 ELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 347
Cdd:cd09236 320 EIVSNLDEGRKFYNDLAKILSQFRDACKAWVYER 353
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
 9-347 3.36e-21

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: 92.92  E-value: 3.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 88
Cdd:cd09238   1 PESSAKALSKYTEMVDELIRTEADRLAAASDEARVALREMELPETLIALDGGASLPGDLGLDEEVEAVQISGGLAALEGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       89 LPELLQRNR---EILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 165
Cdd:cd09238  81 LPRLRELRRvctELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFRVNLEQAGDSDESLRRRIEDA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      166 rDTIVLLCKPEPELNAAIPSANPAKT*QGSE--VVNVLKSLLSNLDEVKKEREGLENDLKSV--NFD*TSKFLTAlaqdg 241
Cdd:cd09238 161 -MDGMLILDDEPAAAAAPTLRAPMLSTDEDDasIVGTLRSNLEELEALGNERAGIEDMMKALkrNDNILAKVMAT----- 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      242 VINEEALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFS--------K*KQSNNEANLREEVLKnlataydnFV 313
Cdd:cd09238 235 TGSYDALFKEEL-KKYDSVREAVSKNISSQDDLLSRLRALNEKFSqifdvegwRAATESHATQIRAAVAK--------YR 305

                       330       340       350
                ....*....|....*....|....*....|....
2OEX_B      314 ELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 347
Cdd:cd09238 306 ELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR 339
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 9-333 1.42e-19

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: 88.50  E-value: 1.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSvieQGGIQTVDQLIKE 88
Cdd:cd09237   1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLKERFEGENELMEIVS---GLKSSSVDSQLEL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       89 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 168
Cdd:cd09237  78 LRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPVKED 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      169 IVLLCKPEPELNAAIPSANPAKT*Q-------GSEVVNVLK------SLLSNLDEVKKEREGLENDLKS-VNFD*TSKFL 234
Cdd:cd09237 158 IALLLNGGSLWEELFGFSSSGSPEPslldlddSQNEQTVLKqikqleELLEDLNLIKEERQRVLKDLKQkIHNDDISDIL 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      235 TAL--AQDGVinEEALSVTELDRvYGGLTTKVQESLKKQEGLLKNIQVSHQEFSK*KQSNNEA-------NLREEVLKNL 305
Cdd:cd09237 238 ILNskSKSEI--EKQLFPEELEK-FKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQskekskqKLRKEFFEKL 314

                       330       340
                ....*....|....*....|....*...
2OEX_B      306 ATAYDNFVELVANLKEGTKFYNELTEIL 333
Cdd:cd09237 315 KKAYNSFKKFSAGLPKGLEFYDDLLKMA 342
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 9-342 2.50e-16

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: 78.87  E-value: 2.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B        9 PVSVQQSLAAYNQRKADLVNRSIAQ*REATTLANGVLASLNLPA--AIEDVSGDTVPQSILTKSRSV-IEQGGIQTVDQL 85
Cdd:cd09234   1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPlnVMDMDGQFELPQDLVERCAALsVRPDTIKNLVEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B       86 IKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKerwQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 165
Cdd:cd09234  81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVG---KRGSSIAHVTELKRELKKYKEAHEKASQSNTELHKAMNLH 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      166 RDTIVLLCKPEPELNAAIPSANPAKT*QGSEVVNVLKSLLSNLDEVKKEREGLENDLKSV--NFD*TSKFLTALAQDGvi 243
Cdd:cd09234 158 IANLKLLAGPLDELQKKLPSPSLLDRPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAihEDDITSKLVTTTGGDM-- 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2OEX_B      244 neEALSVTELDRvYGGLTTKVQESLKKQEGLLKN-IQVSHQEFSK*KQSNNEANLREEVLKNLATAYDNFVELVANLKEG 322
Cdd:cd09234 236 --EDLFKEELKK-HDQLVNLIEQNLAAQENILKAlTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKG 312

                       330       340
                ....*....|....*....|
2OEX_B      323 TKFYNELteilvrfQNKCSD 342
Cdd:cd09234 313 IDFYKKL-------EGNVSK 325
 
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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