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Conserved domains on  [gi|767922055|ref|XP_011531554|]
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programmed cell death 6-interacting protein isoform X1 [Homo sapiens]

Protein Classification

pleckstrin homology domain-containing family A member 7( domain architecture ID 13103387)

pleckstrin homology domain-containing family A member 7 (PLEKHA7) is required for zonula adherens biogenesis and maintenance

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 ...
 175-513 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: 621.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 254
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 255 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 334
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 335 IVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEAL 414
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 415 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 494
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                        330
                 ....*....|....*....
gi 767922055 495 LTEILVRFQNKCSDIVFAR 513
Cdd:cd09235  321 LTEILVKFQNKCSDFVFAR 339
BRO1_Alix_like super family cl14649
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 1-160 3.74e-86

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.


The actual alignment was detected with superfamily member cd09240:

Pssm-ID: 472700  Cd Length: 346  Bit Score: 274.17  E-value: 3.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYFYFQEVFPVLAAKHCIMQANAEYHQSILAK 80
Cdd:cd09240  189 MLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSLLPKDWIPVLAGKQAYFHALAEYHQSLVAK 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  81 QQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNV 160
Cdd:cd09240  267 AQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDNDFIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
Amelogenin super family cl33250
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 629-683 1.73e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


The actual alignment was detected with superfamily member smart00818:

Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.47  E-value: 1.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922055   629 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPF-PQPPQQSYYPQQ 683
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 527-681 2.51e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  527 SIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPG 606
Cdd:PHA03247 2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922055  607 SAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYP 681
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 175-513 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: 621.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 254
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 255 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 334
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 335 IVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEAL 414
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 415 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 494
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                        330
                 ....*....|....*....
gi 767922055 495 LTEILVRFQNKCSDIVFAR 513
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 ...
 227-516 6.95e-107

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: 326.11  E-value: 6.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  227 TVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAE 306
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  307 GTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAK-TMQGSEVVNVLKSLLSNLDEVKKEREGLE 385
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  386 NDLK--SVNFDMTSKFLTALAQDGVIN-EEALSVTELDrVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNE-A 461
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767922055  462 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 516
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 1-160 3.74e-86

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: 274.17  E-value: 3.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYFYFQEVFPVLAAKHCIMQANAEYHQSILAK 80
Cdd:cd09240  189 MLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSLLPKDWIPVLAGKQAYFHALAEYHQSLVAK 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  81 QQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNV 160
Cdd:cd09240  267 AQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDNDFIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 1-193 3.28e-67

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: 224.77  E-value: 3.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055    1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKyfyfqEVFPVLAAKHCIMQANAEYHQSILAK 80
Cdd:pfam03097 175 MLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDK-----EWISHVQAKAHHFKALAQYRQALDDE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   81 QQKKFGEEIARLQHAAELIKTvASRYDEYVNV----KDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKST 156
Cdd:pfam03097 250 EAKKYGEEIARLQLALSLLKE-ALKSDRYKKVledlKGLLDVVEEKLKRAEKDNDFIYHERVPSESSLPPIKPASMVKPI 328

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767922055  157 PVN-VPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLV 193
Cdd:pfam03097 329 PPLeLYPFQIGPDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 1-197 4.28e-62

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: 211.83  E-value: 4.28e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055     1 MLAQAQEVFFLKATRDKMK--DAIIAKLANQAADYFGDAFKQCQYKDTLPKYFYFqEVFPVLAAKHCIMQANAEYHQSIL 78
Cdd:smart01041 177 MLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGYIPK-SWIKLVQVKAHHFKALAHYYQALD 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055    79 AKQQKKFGEEIARLQHAAELIKT-----------VASRYDEYVNvkDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPI 147
Cdd:smart01041 256 LEEANKYGEAIARLQEALERLKEakkhlrckklgKADKLQEDLS--GLKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPI 333

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 767922055   148 GKATLVKSTPVNVPIsqKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSI 197
Cdd:smart01041 334 KKAPLVKPPPFSEVL--KGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 629-683 1.73e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.47  E-value: 1.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922055   629 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPF-PQPPQQSYYPQQ 683
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
YppG COG5894
Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];
639-677 2.00e-04

Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444596 [Multi-domain]  Cd Length: 112  Bit Score: 41.38  E-value: 2.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767922055 639 YAYGQYNMPYP-PVYHQSPGQAPYPGPQQPSYPFPQPPQQ 677
Cdd:COG5894   22 QPYGPYQNQHQqPYYQQTNTQQPFPPPSPTPYPSPKPLQT 61
SGP pfam17228
Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by ...
 635-678 2.18e-03

Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by purple sulphur bacteria to transiently store sulphur during the oxidization of reduced sulphur compounds. This proteobacterial family contains structural proteins of these sulphur globules, and includes sulphur globule protein CV1 (SgpA) and sulphur globule protein CV2 (SgpB).


Pssm-ID: 435798 [Multi-domain]  Cd Length: 97  Bit Score: 37.79  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767922055  635 GYNPYAYG---------QYNMPYPPVYHQSPGQAPYPGPQQPSypfPQPPQQS 678
Cdd:pfam17228  47 GYGDYGYGnpygygypyGYGAPYGAPYGYGPYGAPYGAPVAPA---PAAPAEA 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 527-681 2.51e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  527 SIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPG 606
Cdd:PHA03247 2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922055  607 SAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYP 681
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
Name Accession Description Interval E-value
V_Alix cd09235
Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...
 175-513 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: 621.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 254
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 255 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 334
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 335 IVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEAL 414
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 415 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 494
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                        330
                 ....*....|....*....
gi 767922055 495 LTEILVRFQNKCSDIVFAR 513
Cdd:cd09235  321 LTEILVKFQNKCSDFVFAR 339
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 175-513 5.55e-109

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: 333.15  E-value: 5.55e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSI-AQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIK 253
Cdd:cd08915    1 PYDVIESASAYNERQDDYVREHIvEPIEALNKLLNSFLAERNLPASIDDLQKPENLPDSIQHSQEIIEEGGLDNIEQSFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 254 ELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTP-SNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHR 332
Cdd:cd08915   81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPsSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 333 DTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDL--KSVNFDMTSKFLTALAQDGVIN 410
Cdd:cd08915  161 PNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELeiKSRNNDILPKLITEYKKNGTTE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 411 EEALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTK 490
Cdd:cd08915  241 FEDLFEEHL-KKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSNDSLDPREEALQDLEASYKKYLELKENLNEGSK 319

                        330       340
                 ....*....|....*....|...
gi 767922055 491 FYNELTEILVRFQNKCSDIVFAR 513
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 ...
 227-516 6.95e-107

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: 326.11  E-value: 6.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  227 TVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAE 306
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  307 GTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAK-TMQGSEVVNVLKSLLSNLDEVKKEREGLE 385
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  386 NDLK--SVNFDMTSKFLTALAQDGVIN-EEALSVTELDrVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNE-A 461
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767922055  462 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 516
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
 1-160 3.74e-86

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: 274.17  E-value: 3.74e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYFYFQEVFPVLAAKHCIMQANAEYHQSILAK 80
Cdd:cd09240  189 MLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSLLPKDWIPVLAGKQAYFHALAEYHQSLVAK 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  81 QQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNV 160
Cdd:cd09240  267 AQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDNDFIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 1-193 3.28e-67

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: 224.77  E-value: 3.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055    1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKyfyfqEVFPVLAAKHCIMQANAEYHQSILAK 80
Cdd:pfam03097 175 MLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDK-----EWISHVQAKAHHFKALAQYRQALDDE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   81 QQKKFGEEIARLQHAAELIKTvASRYDEYVNV----KDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKST 156
Cdd:pfam03097 250 EAKKYGEEIARLQLALSLLKE-ALKSDRYKKVledlKGLLDVVEEKLKRAEKDNDFIYHERVPSESSLPPIKPASMVKPI 328

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767922055  157 PVN-VPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLV 193
Cdd:pfam03097 329 PPLeLYPFQIGPDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
 1-197 4.28e-62

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: 211.83  E-value: 4.28e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055     1 MLAQAQEVFFLKATRDKMK--DAIIAKLANQAADYFGDAFKQCQYKDTLPKYFYFqEVFPVLAAKHCIMQANAEYHQSIL 78
Cdd:smart01041 177 MLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGYIPK-SWIKLVQVKAHHFKALAHYYQALD 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055    79 AKQQKKFGEEIARLQHAAELIKT-----------VASRYDEYVNvkDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPI 147
Cdd:smart01041 256 LEEANKYGEAIARLQEALERLKEakkhlrckklgKADKLQEDLS--GLKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPI 333

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 767922055   148 GKATLVKSTPVNVPIsqKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSI 197
Cdd:smart01041 334 KKAPLVKPPPFSEVL--KGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
 175-513 4.69e-46

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: 167.15  E-value: 4.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREA-TTLANGVLASLNLPAAIEDVS---GdtVPQSILTKSRSVIEQGGIQTVDQ 250
Cdd:cd09236    1 PFGVHLAISIYDDRKDRLVNESIIDELEElTNRAHSTLRSLNLPGSLQALEkplG--LPPSLLRHAEEIRQEDGLERIRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 251 LIKELPELLQRNREILDESLRLLDEEEATDNDLRAKF-KERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQ 329
Cdd:cd09236   79 SLDDVARLAASDRAILEEAMDILDDEASEDESLRRKFgTDRWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRRKLD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 330 SHRDTIVLLCKPEPELNAAIPSAN-PAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDL--KSVNFDMTSKFLTA---L 403
Cdd:cd09236  159 EWEDLIQILTGDERDLENFVPSSRrPSIPPELERHVRALRVSLEELDRLESRRRRKVERArtKARADDIRPEILREaarL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 404 AQDGVINE------EALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDN 477
Cdd:cd09236  239 EREYPATEvapahfEDLFDKRL-AKYDKDLDAVSEEAQEQEEILQQIEVANKAFLQSRKGDPATKERERALQSLDLAYFK 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767922055 478 FVELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 513
Cdd:cd09236  318 YKEIVSNLDEGRKFYNDLAKILSQFRDACKAWVYER 353
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 1-158 5.73e-41

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: 152.89  E-value: 5.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKM-KDAIIAKLANQAADYFGDAFKQCQYKDTLPKYFYFQEVFPVLAAKHCIMQANAEYHQSILA 79
Cdd:cd09034  182 MLAQAQECFLLKAEEDKKaKLSLLARLACEAAKYYEEALKCLSGVDLETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKL 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  80 KQQKKFGEEIARLQHAAELIKTVASRYDEY-----VNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVK 154
Cdd:cd09034  262 DEANKIGEAIARLQAALELLKESERLCKSFlldvwGNLKKLKEKIEKELEKAERENDFIYFEEVPPEDPLPEIKGALLVK 341


                 ....
gi 767922055 155 STPV 158
Cdd:cd09034  342 PPPL 345
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 1-180 1.50e-37

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: 143.56  E-value: 1.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKYFyfqevFPVLAAKHCIMQANAEYHQSILAK 80
Cdd:cd09241  174 MLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSDLIRSDW-----INHLKVKKHHFKAAAHYRMALVAL 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  81 QQKKFGEEIARLQHAAELIKTvASRYDEYVNVK------DFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVK 154
Cdd:cd09241  249 EKSKYGEEVARLRVALAACKE-ALKEARYGNKAvledlqGLKDIVKESLKRAERDNDLIYLQPVPPASELPPIKPASMVK 327

                        170       180
                 ....*....|....*....|....*...
gi 767922055 155 S-TPVNVPISQKF-TDLFEKMVPVSVQQ 180
Cdd:cd09241  328 AiVPPELEEGSKLgKPLFKDLLPYGVHE 355
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 1-159 6.86e-31

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: 124.43  E-value: 6.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCqykDTLPKYFYFQEVF-PVLAAKHCIMQANAEYHQSILA 79
Cdd:cd09246  181 MLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEAL---DSPPLKGHFDKSWvAHVQLKAAYFRAEALYRAAKDL 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  80 KQQKKFGEEIARLQHAAELI-------KTVASryDEYVNVKDFSDK-INRALAAAKKDNDFIYHDRVPDLKDLDPIGKAT 151
Cdd:cd09246  258 HEKEDIGEEIARLRAASDALaearkqaKGVNG--DELIEAVSELEQvINELLERAEKENDCVYLDRVPAPSDLPPLGAAS 335


                 ....*...
gi 767922055 152 LVKSTPVN 159
Cdd:cd09246  336 MVKPAAPP 343
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 1-159 2.91e-25

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: 107.75  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDK---MKDAIIAKLANQAADYFGDAFKQcqYKDTLPK-YFYFQEVFP-VLAAKHCIMQANAEYHQ 75
Cdd:cd09242  173 MLAQAQEIFLLKLINGDdaqKKASLISKLASATANLYESCVEF--LKEIQEKgISYGDPKWIsLVQCKAHYYKSLAAYYH 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  76 SILAKQQKKFGEEIARLQHAAELIKTVAS------------RYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKD 143
Cdd:cd09242  251 ALALEAAGKYGEAIAYLTQAESILKEANPqklslkasagdaAYALNDDFKGQKDTVEEKLKELEKDNDFIYHDIVPSEVT 330

                        170
                 ....*....|....*.
gi 767922055 144 LDPIGKATLVKSTPVN 159
Cdd:cd09242  331 LPSIKPLDAAKPIPIE 346
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
 175-513 9.60e-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: 99.85  E-value: 9.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 254
Cdd:cd09238    1 PESSAKALSKYTEMVDELIRTEADRLAAASDEARVALREMELPETLIALDGGASLPGDLGLDEEVEAVQISGGLAALEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 255 LPELLQRNR---EILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 331
Cdd:cd09238   81 LPRLRELRRvctELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFRVNLEQAGDSDESLRRRIEDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 332 rDTIVLLCKPEPELNAAIPSANPAKTMQGSE--VVNVLKSLLSNLDEVKKEREGLENDLKSV--NFDMTSKFLTAlaqdg 407
Cdd:cd09238  161 -MDGMLILDDEPAAAAAPTLRAPMLSTDEDDasIVGTLRSNLEELEALGNERAGIEDMMKALkrNDNILAKVMAT----- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 408 VINEEALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKM--------KQSNNEANLREEVLKnlataydnFV 479
Cdd:cd09238  235 TGSYDALFKEEL-KKYDSVREAVSKNISSQDDLLSRLRALNEKFSQIfdvegwraATESHATQIRAAVAK--------YR 305

                        330       340       350
                 ....*....|....*....|....*....|....
gi 767922055 480 ELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 513
Cdd:cd09238  306 ELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR 339
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 1-160 1.19e-22

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: 100.19  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   1 MLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQ-----CQYKDTLPKYFYfqevfpvLAAKHCIMQAN----- 70
Cdd:cd09239  181 MLAQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRAlenweSNSKIILGKIQK-------EWRKLVQMKIAyyasi 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  71 AEYHQSILAKQQKKFGEEIARLQHA---AELIKTVASRYDEYVNVKDFS----DKINRALAAAKKDNDFIYHDRVPDLKD 143
Cdd:cd09239  254 AHLHMGKQSEEQQKMGERVAYYQLAndkLEEAIKNAKGQPDTVNLQEALsftmDVIGGKRNSAKKENDFIYHEAVPKLDT 333

                        170
                 ....*....|....*..
gi 767922055 144 LDPIGKATLVKSTPVNV 160
Cdd:cd09239  334 LQAVKGANLVKGIPFSP 350
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 175-499 7.59e-22

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: 97.75  E-value: 7.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSgdtvpqSILTKSRSVIEQGGIQ---TVDQL 251
Cdd:cd09237    1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLK------ERFEGENELMEIVSGLkssSVDSQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 252 IKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 331
Cdd:cd09237   75 LELLRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 332 RDTIVLLCKPEPELNAA-IPSANPAKTM---------QGSEV---VNVLKSLLSNLDEVKKEREGLENDLKS-VNFDMTS 397
Cdd:cd09237  155 KEDIALLLNGGSLWEELfGFSSSGSPEPslldlddsqNEQTVlkqIKQLEELLEDLNLIKEERQRVLKDLKQkIHNDDIS 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 398 KFLTAL--AQDGVinEEALSVTELDRvYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEA-------NLREEVL 468
Cdd:cd09237  235 DILILNskSKSEI--EKQLFPEELEK-FKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQskekskqKLRKEFF 311

                        330       340       350
                 ....*....|....*....|....*....|.
gi 767922055 469 KNLATAYDNFVELVANLKEGTKFYNELTEIL 499
Cdd:cd09237  312 EKLKKAYNSFKKFSAGLPKGLEFYDDLLKMA 342
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 175-508 1.70e-17

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: 84.26  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 175 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPA--AIEDVSGDTVPQSILTKSRSV-IEQGGIQTVDQL 251
Cdd:cd09234    1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPlnVMDMDGQFELPQDLVERCAALsVRPDTIKNLVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 252 IKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKerwQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 331
Cdd:cd09234   81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVG---KRGSSIAHVTELKRELKKYKEAHEKASQSNTELHKAMNLH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 332 RDTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSV--NFDMTSKFLTALAQDGvi 409
Cdd:cd09234  158 IANLKLLAGPLDELQKKLPSPSLLDRPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAihEDDITSKLVTTTGGDM-- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055 410 neEALSVTELDRvYGGLTTKVQESLKKQEGLLKN-IQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEG 488
Cdd:cd09234  236 --EDLFKEELKK-HDQLVNLIEQNLAAQENILKAlTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKG 312

                        330       340
                 ....*....|....*....|
gi 767922055 489 TKFYNELteilvrfQNKCSD 508
Cdd:cd09234  313 IDFYKKL-------EGNVSK 325
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
 2-140 5.09e-09

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: 58.51  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   2 LAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAfkqcqyKDTL----PKYF-----YFQevfpvlaAKHCIMQANAE 72
Cdd:cd09243  185 TAEAQEVTVARAIELKHNAGLISALAYETAKLFQKA------DDSLssldPEYSgkwrkYLQ-------LKSVFYLAYAY 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  73 -YH-QSILAKQqkKFGEEIARLQHAAELIKTVASRYDEYVNVKD-----------FSDK----INRALAAAKKDNDFIYH 135
Cdd:cd09243  252 cYHgETLLAKD--KCGEAIRSLQESEKLYNKAEALCKEYAKTKGpgttakpdqhlFFRKlgplVKRTLEKCERENGFIYH 329


                 ....*
gi 767922055 136 DRVPD 140
Cdd:cd09243  330 QKVPD 334
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 2-149 1.31e-07

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: 53.93  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055   2 LAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAfKQ------CQYKDTLPKyfyFQEVFPVLAAKHcimQANAEYHQ 75
Cdd:cd09247  187 LAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEA-KNvlrslaTDLKDLDPR---FLRFISSCIALH---EARSQLYL 259

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767922055  76 SILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNV--KDFSDKINRALAAAKKDNDFIYHDRVPDLKDL-DPIGK 149
Cdd:cd09247  260 ARRLKEAGHIGVAVGVLREALRNLKKKLPGSDISSPVifRDERAEVATLLQKYEKENEVIYFEKVPDIDELpLPEGK 336
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 629-683 1.73e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.47  E-value: 1.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922055   629 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPF-PQPPQQSYYPQQ 683
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
YppG COG5894
Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];
639-677 2.00e-04

Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444596 [Multi-domain]  Cd Length: 112  Bit Score: 41.38  E-value: 2.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767922055 639 YAYGQYNMPYP-PVYHQSPGQAPYPGPQQPSYPFPQPPQQ 677
Cdd:COG5894   22 QPYGPYQNQHQqPYYQQTNTQQPFPPPSPTPYPSPKPLQT 61
SGP pfam17228
Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by ...
 635-678 2.18e-03

Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by purple sulphur bacteria to transiently store sulphur during the oxidization of reduced sulphur compounds. This proteobacterial family contains structural proteins of these sulphur globules, and includes sulphur globule protein CV1 (SgpA) and sulphur globule protein CV2 (SgpB).


Pssm-ID: 435798 [Multi-domain]  Cd Length: 97  Bit Score: 37.79  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767922055  635 GYNPYAYG---------QYNMPYPPVYHQSPGQAPYPGPQQPSypfPQPPQQS 678
Cdd:pfam17228  47 GYGDYGYGnpygygypyGYGAPYGAPYGYGPYGAPYGAPVAPA---PAAPAEA 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
 527-681 2.51e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922055  527 SIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPG 606
Cdd:PHA03247 2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922055  607 SAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYP 681
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
RCR pfam12273
Chitin synthesis regulation, resistance to Congo red; RCR proteins are ER membrane proteins ...
 635-683 6.40e-03

Chitin synthesis regulation, resistance to Congo red; RCR proteins are ER membrane proteins that regulate chitin deposition in fungal cell walls. Although chitin, a linear polymer of beta-1,4-linked N-acetylglucosamine, constitutes only 2% of the cell wall it plays a vital role in the overall protection of the cell wall against stress, noxious chemicals and osmotic pressure changes. Congo red is a cell wall-disrupting benzidine-type dye extensively used in many cell wall mutant studies that specifically targets chitin in yeast cells and inhibits growth. RCR proteins render the yeasts resistant to Congo red by diminishing the content of chitin in the cell wall. RCR proteins are probably regulating chitin synthase III interact directly with ubiquitin ligase Rsp5, and the VPEY motif is necessary for this, via interaction with the WW domains of Rsp5.


Pssm-ID: 432443 [Multi-domain]  Cd Length: 113  Bit Score: 37.01  E-value: 6.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922055  635 GYNPYaYGQ---YNMPYPPVYHQSPGQAPYPGPQQPSY-----------------PFPQPPQQSYYPQQ 683
Cdd:pfam12273  30 GLQPI-YGTgwmGGGPPPPSYGQSQQDPQPTGTYVPTYtpndgyydqqgnfhnagSGLQPPQQAYQPPT 97
 
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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