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Conserved domains on  [gi|241982780|ref|NP_001155901|]
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programmed cell death 6-interacting protein isoform 2 [Homo sapiens]

Protein Classification

pleckstrin homology domain-containing family A member 7( domain architecture ID 12964703)

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 ...
365-703 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: 625.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 444
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 445 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 524
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 525 IVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEAL 604
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 605 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 684
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320
                        330
                 ....*....|....*....
gi 241982780 685 LTEILVRFQNKCSDIVFAR 703
Cdd:cd09235  321 LTEILVKFQNKCSDFVFAR 339
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
2-350 0e+00

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2.


:

Pssm-ID: 185763  Cd Length: 346  Bit Score: 611.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   2 ATFISVQLKKTSEVDLAKPLVKFIQQTYPSGgEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPK 81
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSG-EEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  82 FPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFL 161
Cdd:cd09240   80 FPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 162 HIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYF 241
Cdd:cd09240  160 HLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 242 YFQEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDND 321
Cdd:cd09240  238 LPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDND 317
                        330       340
                 ....*....|....*....|....*....
gi 241982780 322 FIYHDRVPDLKDLDPIGKATLVKSTPVNV 350
Cdd:cd09240  318 FIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
Amelogenin super family cl33250
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
819-873 4.09e-05

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: 44.78  E-value: 4.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 241982780   819 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPF-PQPPQQSYYPQQ 873
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
PHA03247 super family cl33720
large tegument protein UL36; Provisional
717-871 3.30e-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: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  717 SIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPG 796
Cdd:PHA03247 2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  797 SAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYP 871
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 ...
365-703 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: 625.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 444
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 445 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 524
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 525 IVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEAL 604
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 605 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 684
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320
                        330
                 ....*....|....*....
gi 241982780 685 LTEILVRFQNKCSDIVFAR 703
Cdd:cd09235  321 LTEILVKFQNKCSDFVFAR 339
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
2-350 0e+00

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2.


Pssm-ID: 185763  Cd Length: 346  Bit Score: 611.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   2 ATFISVQLKKTSEVDLAKPLVKFIQQTYPSGgEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPK 81
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSG-EEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  82 FPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFL 161
Cdd:cd09240   80 FPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 162 HIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYF 241
Cdd:cd09240  160 HLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 242 YFQEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDND 321
Cdd:cd09240  238 LPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDND 317
                        330       340
                 ....*....|....*....|....*....
gi 241982780 322 FIYHDRVPDLKDLDPIGKATLVKSTPVNV 350
Cdd:cd09240  318 FIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-383 2.74e-143

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: 428.54  E-value: 2.74e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780    4 FISVQLKKTSEVDLAKPLVKFIQQTYpsGGEEQAQYCRAAEELSKLRRAAVgRPLDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTY--GSQDPSSFEDDLAELNKLRQDAV-RGANEDESGLDLLYKYYAQLELLELRFP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   84 FsENQICLTFTWKDAFDKGSlfggsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:pfam03097  78 I-DIQIGIEFTWYDAFGTSS-----KKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  164 KETVLSAlsrePTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKyfyf 243
Cdd:pfam03097 152 KENFLHA----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDK---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  244 qEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTvASRYDEYVNV----KDFSDKINRALAAAKKD 319
Cdd:pfam03097 224 -EWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKE-ALKSDRYKKVledlKGLLDVVEEKLKRAEKD 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  320 NDFIYHDRVPDLKDLDPIGKATLVKSTPVN-VPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLV 383
Cdd:pfam03097 302 NDFIYHERVPSESSLPPIKPASMVKPIPPLeLYPFQIGPDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-387 3.70e-140

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: 420.99  E-value: 3.70e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780     4 FISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAVGRplDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETY---SEDSSSYEDEIAELNRLRQAARTP--SRDESGLELLLKYYGQLEALELRFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780    84 FSENQICLTFTWKDAFDkgslfgGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:smart01041  76 PPEGQLKLSFTWYDSLD------TGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   164 KETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMK--DAIIAKLANQAADYFGDAFKQCQYKDTLPKYF 241
Cdd:smart01041 150 KENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGYI 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   242 YFqEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKT-----------VASRYDEYVNvkDFSDKIN 310
Cdd:smart01041 230 PK-SWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEakkhlrckklgKADKLQEDLS--GLKDVVE 306
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982780   311 RALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPIsqKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSI 387
Cdd:smart01041 307 EKLKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSEVL--KGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
417-706 1.10e-105

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: 328.04  E-value: 1.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  417 TVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAE 496
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  497 GTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAK-TMQGSEVVNVLKSLLSNLDEVKKEREGLE 575
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  576 NDLK--SVNFDMTSKFLTALAQDGVIN-EEALSVTELDrVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNE-A 651
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  652 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 706
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
819-873 4.09e-05

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: 44.78  E-value: 4.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 241982780   819 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPF-PQPPQQSYYPQQ 873
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
YppG COG5894
Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];
829-867 6.97e-05

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


Pssm-ID: 444596 [Multi-domain]  Cd Length: 112  Bit Score: 42.92  E-value: 6.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 241982780 829 YAYGQYNMPYP-PVYHQSPGQAPYPGPQQPSYPFPQPPQQ 867
Cdd:COG5894   22 QPYGPYQNQHQqPYYQQTNTQQPFPPPSPTPYPSPKPLQT 61
SGP pfam17228
Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by ...
825-868 2.83e-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: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 241982780  825 GYNPYAYG---------QYNMPYPPVYHQSPGQAPYPGPQQPSypfPQPPQQS 868
Cdd:pfam17228  47 GYGDYGYGnpygygypyGYGAPYGAPYGYGPYGAPYGAPVAPA---PAAPAEA 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
717-871 3.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  717 SIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPG 796
Cdd:PHA03247 2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  797 SAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYP 871
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 ...
365-703 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: 625.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 444
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 445 LPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDT 524
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 525 IVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEAL 604
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 605 SVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 684
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320
                        330
                 ....*....|....*....
gi 241982780 685 LTEILVRFQNKCSDIVFAR 703
Cdd:cd09235  321 LTEILVKFQNKCSDFVFAR 339
BRO1_Alix cd09240
Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...
2-350 0e+00

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2.


Pssm-ID: 185763  Cd Length: 346  Bit Score: 611.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   2 ATFISVQLKKTSEVDLAKPLVKFIQQTYPSGgEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPK 81
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSG-EEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  82 FPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFL 161
Cdd:cd09240   80 FPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 162 HIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYF 241
Cdd:cd09240  160 HLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 242 YFQEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDND 321
Cdd:cd09240  238 LPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDND 317
                        330       340
                 ....*....|....*....|....*....
gi 241982780 322 FIYHDRVPDLKDLDPIGKATLVKSTPVNV 350
Cdd:cd09240  318 FIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
BRO1 pfam03097
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-383 2.74e-143

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: 428.54  E-value: 2.74e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780    4 FISVQLKKTSEVDLAKPLVKFIQQTYpsGGEEQAQYCRAAEELSKLRRAAVgRPLDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTY--GSQDPSSFEDDLAELNKLRQDAV-RGANEDESGLDLLYKYYAQLELLELRFP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   84 FsENQICLTFTWKDAFDKGSlfggsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:pfam03097  78 I-DIQIGIEFTWYDAFGTSS-----KKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  164 KETVLSAlsrePTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKyfyf 243
Cdd:pfam03097 152 KENFLHA----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDK---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  244 qEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTvASRYDEYVNV----KDFSDKINRALAAAKKD 319
Cdd:pfam03097 224 -EWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKE-ALKSDRYKKVledlKGLLDVVEEKLKRAEKD 301
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  320 NDFIYHDRVPDLKDLDPIGKATLVKSTPVN-VPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLV 383
Cdd:pfam03097 302 NDFIYHERVPSESSLPPIKPASMVKPIPPLeLYPFQIGPDLFKKLVPLSVHEAASAYSERKAKLV 366
BRO1 smart01041
BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...
4-387 3.70e-140

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: 420.99  E-value: 3.70e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780     4 FISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAVGRplDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETY---SEDSSSYEDEIAELNRLRQAARTP--SRDESGLELLLKYYGQLEALELRFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780    84 FSENQICLTFTWKDAFDkgslfgGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:smart01041  76 PPEGQLKLSFTWYDSLD------TGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   164 KETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMK--DAIIAKLANQAADYFGDAFKQCQYKDTLPKYF 241
Cdd:smart01041 150 KENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGYI 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   242 YFqEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKT-----------VASRYDEYVNvkDFSDKIN 310
Cdd:smart01041 230 PK-SWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEakkhlrckklgKADKLQEDLS--GLKDVVE 306
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 241982780   311 RALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPIsqKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSI 387
Cdd:smart01041 307 EKLKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSEVL--KGPDLFAKLVPMAVHEAASLYSEEKAKLVRAEI 381
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
365-703 3.89e-108

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: 336.24  E-value: 3.89e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSI-AQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIK 443
Cdd:cd08915    1 PYDVIESASAYNERQDDYVREHIvEPIEALNKLLNSFLAERNLPASIDDLQKPENLPDSIQHSQEIIEEGGLDNIEQSFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 444 ELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTP-SNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHR 522
Cdd:cd08915   81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPsSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 523 DTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDL--KSVNFDMTSKFLTALAQDGVIN 600
Cdd:cd08915  161 PNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELeiKSRNNDILPKLITEYKKNGTTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 601 EEALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTK 680
Cdd:cd08915  241 FEDLFEEHL-KKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSNDSLDPREEALQDLEASYKKYLELKENLNEGSK 319
                        330       340
                 ....*....|....*....|...
gi 241982780 681 FYNELTEILVRFQNKCSDIVFAR 703
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 ...
417-706 1.10e-105

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: 328.04  E-value: 1.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  417 TVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAE 496
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  497 GTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAK-TMQGSEVVNVLKSLLSNLDEVKKEREGLE 575
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  576 NDLK--SVNFDMTSKFLTALAQDGVIN-EEALSVTELDrVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNE-A 651
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  652 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 706
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
4-348 7.97e-98

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: 309.28  E-value: 7.97e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   4 FISVQLKKTSEVDLAKPLVKFIQQTYPSggEEQAQYCRAAEELSKLRRAAVGRPLDK--HEGALETLLRYYDQICSIEPK 81
Cdd:cd09034    1 FIGLPLKKTKEVDVKVPLSKFIPKNYGE--LEATAVEDLIEKLSKLRNNIVTEQNNDttCENLLEALKEYLPYLLGLEKK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  82 FPFSENQICLTFTWKDAFDKGslfggsVKLALaSLGYEKSCVLFNCAALASQIAAEQNLDN-DEGLKIAAKHYQFASGAF 160
Cdd:cd09034   79 LPFQKLRDNVEFTWTDSFDTK------KESAT-SLRYELLSILFNLAALASQLANEKLITGsEEDLKQAIKSLQKAAGYF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 161 LHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKM-KDAIIAKLANQAADYFGDAFKQCQYKDTLPK 239
Cdd:cd09034  152 EYLKEHVLPLPPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKaKLSLLARLACEAAKYYEEALKCLSGVDLETI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 240 YFYFQEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEY-----VNVKDFSDKINRALA 314
Cdd:cd09034  232 KNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKSFlldvwGNLKKLKEKIEKELE 311
                        330       340       350
                 ....*....|....*....|....*....|....
gi 241982780 315 AAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPV 348
Cdd:cd09034  312 KAERENDFIYFEEVPPEDPLPEIKGALLVKPPPL 345
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
6-349 1.46e-81

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: 266.57  E-value: 1.46e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   6 SVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAA-EELSKLRRAAVgRPLDKHEGALETLLRYYDQICSIEPKFPF 84
Cdd:cd09246    3 SIHRKKTETVDLVSPLRAYISETY---SEREAQDAEDDlAELQQLRSEVR-TLQEKHAASRELLLRYYRALCAVESRFPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  85 SENQ--ICLTFTWKDAFDkgslfgGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLH 162
Cdd:cd09246   79 SEESghARVSFSWYDAFR------PHRKATQANVHFEKAAVLFNLGALSSQLGLQQDRTTAEGIKQACHAFQAAAGAFAH 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 163 IKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCqykDTLPKYFY 242
Cdd:cd09246  153 LRDKVSGKTGGFRTPDLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEAL---DSPPLKGH 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 243 FQEVF-PVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELI-------KTVASryDEYVNVKDFSDK-INRAL 313
Cdd:cd09246  230 FDKSWvAHVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALaearkqaKGVNG--DELIEAVSELEQvINELL 307
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 241982780 314 AAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVN 349
Cdd:cd09246  308 ERAEKENDCVYLDRVPAPSDLPPLGAASMVKPAAPP 343
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
4-349 4.96e-74

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: 246.04  E-value: 4.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   4 FISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAVGRplDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:cd09242    1 LISLPLKDTEEVDWKKPLSSYLKRSY---GSSTFYYEEEIAEFDRLRQDANGV--LADETGRDLLYKYYGQLELLELRFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  84 FSENQICLTFTWKDAFDKGSLFGGSvklalaSLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:cd09242   76 FNNKELKVDFTWYDAFYKSKKVKQH------SLAFEKASVLFNIGALLSQLAAEKYREDEDDLKEAITNLQQAAGCFQYI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 164 KETVLSAlsrePTVDISPDTVGTLSLIMLAQAQEVFFLKATRDK---MKDAIIAKLANQAADYFGDAFKqcQYKDTLPK- 239
Cdd:cd09242  150 NENFLHA----PSVDLQQENVKFLVKLMLAQAQEIFLLKLINGDdaqKKASLISKLASATANLYESCVE--FLKEIQEKg 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 240 YFYFQEVFP-VLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVAS------------RYDEYVNVKDFS 306
Cdd:cd09242  224 ISYGDPKWIsLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKEANPqklslkasagdaAYALNDDFKGQK 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 241982780 307 DKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVN 349
Cdd:cd09242  304 DTVEEKLKELEKDNDFIYHDIVPSEVTLPSIKPLDAAKPIPIE 346
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
4-370 3.06e-73

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: 244.48  E-value: 3.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   4 FISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAVGrpLDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:cd09241    2 LLSIPFKRTLPVDLKDALRNYISNHY---FQTPSSFEDDLAEIDKLRNDAIN--PEPSVNGLSLLKEYYAQLVVLSKKFP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  84 fsenQICLTFTWKDAFDKGSlfggSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:cd09241   77 ----DDQLEFTWYPTLGYKS----SGPVSLSSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 164 KETVLSALSREPtvDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKYFyf 243
Cdd:cd09241  149 LQHLLPTLSPPP--DLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSDLIRSDW-- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 244 qevFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTvASRYDEYVNVK------DFSDKINRALAAAK 317
Cdd:cd09241  225 ---INHLKVKKHHFKAAAHYRMALVALEKSKYGEEVARLRVALAACKE-ALKEARYGNKAvledlqGLKDIVKESLKRAE 300
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 241982780 318 KDNDFIYHDRVPDLKDLDPIGKATLVKS-TPVNVPISQKF-TDLFEKMVPVSVQQ 370
Cdd:cd09241  301 RDNDLIYLQPVPPASELPPIKPASMVKAiVPPELEEGSKLgKPLFKDLLPYGVHE 355
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
5-350 3.55e-60

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: 208.82  E-value: 3.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   5 ISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAVGRPLDKhEGALeTLLRYYDQICSIEPKFPF 84
Cdd:cd09239    9 LWLQLKSSGEFTFQPALKKYILENY---GEDPELYSEELKSLEQLRQEAVNPPRDF-EGCS-VLKRYYGQLHLLQSRFPM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  85 -SENQICLTFTWKDAFDKGSLFGGSVKlalaslgYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHI 163
Cdd:cd09239   84 gAGQEAAVPFTWTDIFSGSEVTHEDIK-------FEEASVLYNIGALHSQLGASDKRDSEEGMKVACTHFQCAAWAFAYL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 164 KETVLSALSrepTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQ-----CQYKDTLP 238
Cdd:cd09239  157 REHYPQVYG---AVDMSSQLLSFNYSLMLAQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRAlenweSNSKIILG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 239 KYFYfqevfpvLAAKHCIMQAN-----AEYHQSILAKQQKKFGEEIARLQHA---AELIKTVASRYDEYVNVKDFS---- 306
Cdd:cd09239  234 KIQK-------EWRKLVQMKIAyyasiAHLHMGKQSEEQQKMGERVAYYQLAndkLEEAIKNAKGQPDTVNLQEALsftm 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 241982780 307 DKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNV 350
Cdd:cd09239  307 DVIGGKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPFSP 350
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
365-703 6.92e-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: 168.30  E-value: 6.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREA-TTLANGVLASLNLPAAIEDVS---GdtVPQSILTKSRSVIEQGGIQTVDQ 440
Cdd:cd09236    1 PFGVHLAISIYDDRKDRLVNESIIDELEElTNRAHSTLRSLNLPGSLQALEkplG--LPPSLLRHAEEIRQEDGLERIRA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 441 LIKELPELLQRNREILDESLRLLDEEEATDNDLRAKF-KERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQ 519
Cdd:cd09236   79 SLDDVARLAASDRAILEEAMDILDDEASEDESLRRKFgTDRWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRRKLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 520 SHRDTIVLLCKPEPELNAAIPSAN-PAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDL--KSVNFDMTSKFLTA---L 593
Cdd:cd09236  159 EWEDLIQILTGDERDLENFVPSSRrPSIPPELERHVRALRVSLEELDRLESRRRRKVERArtKARADDIRPEILREaarL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 594 AQDGVINE------EALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDN 667
Cdd:cd09236  239 EREYPATEvapahfEDLFDKRL-AKYDKDLDAVSEEAQEQEEILQQIEVANKAFLQSRKGDPATKERERALQSLDLAYFK 317
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 241982780 668 FVELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 703
Cdd:cd09236  318 YKEIVSNLDEGRKFYNDLAKILSQFRDACKAWVYER 353
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
5-202 1.82e-30

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


Pssm-ID: 185767  Cd Length: 350  Bit Score: 123.61  E-value: 1.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   5 ISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAvgRPLDKHEGALETLLRYYDQICSIEPKFPF 84
Cdd:cd09244    2 IPLGLKETKEIDFMEPFKDFILEHY---SEDPSLYEDEIADFTDLRQAM--RTPSRDEAGIELLFEYYNQLYFVERRFFP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  85 SENQICLTFTWKDafdkgSLFGgsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIK 164
Cdd:cd09244   77 PDRSLGIYFHWYD-----SLTG--VPSVQRSVAFEKASVLFNIGALYTQIGAKQDRTTEEGIEAAVDAFQRAAGAFNYLR 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 241982780 165 ETvlsaLSREPTVDISPDTVGTLSLIMLAQAQEVFFLK 202
Cdd:cd09244  150 EN----FSNAPSMDLSPEMLEALIKLMLAQAQECVFEK 183
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
5-277 8.02e-28

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


Pssm-ID: 185771  Cd Length: 384  Bit Score: 116.52  E-value: 8.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   5 ISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAvgRPLDKHEGALETLLRYYDQICSIEPKFPF 84
Cdd:cd09248    2 IPLGLKETKELDLPTPLKELISEHF---GEDGTSYEAEIRELEDLRQAM--RTPSRSEAGLELLMAYYNQLCFLDARFFP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  85 SENQICLTFTWKDafdkgSLFGgsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIK 164
Cdd:cd09248   77 PAKSLGLFFHWYD-----SLTG--VPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 165 ETvlsaLSREPTVDISPDTVGTLSLIMLAQAQEVFF------LKATRDKMKDAI-IAKLANQAADYFG---DAFKQCQYK 234
Cdd:cd09248  150 EN----FSNAPSPDMSTASLSMLEQLMVAQAQECIFeglllpLLATPQDFFAQLqLAQEAAQVAAEYRlvhRTMAQPPVR 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 241982780 235 DTLPKYFYF-----QEVFPVLAAKHCIMQAnAEYH---QSILAKQQKKFGE 277
Cdd:cd09248  226 DYVPFSWTAlvhvkAEHFCALAHYHAAMAL-CDSSpasEGELATQEKAFLQ 275
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
365-703 6.20e-23

Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This domain family is comprised of uncharacterized plant proteins. It belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), (His-Domain) type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_Rim20_Bro1_like superfamily also have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members of the V_Alix_like superfamily also have a proline-rich region (PRR).


Pssm-ID: 185751  Cd Length: 339  Bit Score: 101.01  E-value: 6.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKE 444
Cdd:cd09238    1 PESSAKALSKYTEMVDELIRTEADRLAAASDEARVALREMELPETLIALDGGASLPGDLGLDEEVEAVQISGGLAALEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 445 LPELLQRNR---EILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 521
Cdd:cd09238   81 LPRLRELRRvctELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFRVNLEQAGDSDESLRRRIEDA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 522 rDTIVLLCKPEPELNAAIPSANPAKTMQGSE--VVNVLKSLLSNLDEVKKEREGLENDLKSV--NFDMTSKFLTAlaqdg 597
Cdd:cd09238  161 -MDGMLILDDEPAAAAAPTLRAPMLSTDEDDasIVGTLRSNLEELEALGNERAGIEDMMKALkrNDNILAKVMAT----- 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 598 VINEEALSVTELdRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKM--------KQSNNEANLREEVLKnlataydnFV 669
Cdd:cd09238  235 TGSYDALFKEEL-KKYDSVREAVSKNISSQDDLLSRLRALNEKFSQIfdvegwraATESHATQIRAAVAK--------YR 305
                        330       340       350
                 ....*....|....*....|....*....|....
gi 241982780 670 ELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 703
Cdd:cd09238  306 ELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR 339
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
5-221 1.21e-22

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


Pssm-ID: 185772  Cd Length: 385  Bit Score: 101.08  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780   5 ISVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRAAvgRPLDKHEGALETLLRYYDQICSIEPKFPF 84
Cdd:cd09249    2 IPLGLKETKDVDFSVPLKDFILEHY---SEDGSEYEDEIADLMDLRQAC--RTPSRDEAGVELLMSYFSQLGFLENRFFP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  85 SENQICLTFTWKDAFDkgslfggSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIK 164
Cdd:cd09249   77 PTRQMGILFTWYDSFT-------GVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTQAGLESAVDAFQRAAGVLNYLK 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 241982780 165 ETvlsaLSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDA--IIAKLANQAA 221
Cdd:cd09249  150 ET----FTHTPSYDMSPAMLSVLVKMMLAQAQECLFEKISLPGIRNEffTLVKMAQEAA 204
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
365-689 6.37e-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: 98.52  E-value: 6.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSgdtvpqSILTKSRSVIEQGGIQ---TVDQL 441
Cdd:cd09237    1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLK------ERFEGENELMEIVSGLkssSVDSQ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 442 IKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 521
Cdd:cd09237   75 LELLRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 522 RDTIVLLCKPEPELNAA-IPSANPAKTM---------QGSEV---VNVLKSLLSNLDEVKKEREGLENDLKS-VNFDMTS 587
Cdd:cd09237  155 KEDIALLLNGGSLWEELfGFSSSGSPEPslldlddsqNEQTVlkqIKQLEELLEDLNLIKEERQRVLKDLKQkIHNDDIS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 588 KFL-----TALAQDGVINEEalsvtELDRvYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEA-------NLRE 655
Cdd:cd09237  235 DILilnskSKSEIEKQLFPE-----ELEK-FKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQskekskqKLRK 308
                        330       340       350
                 ....*....|....*....|....*....|....
gi 241982780 656 EVLKNLATAYDNFVELVANLKEGTKFYNELTEIL 689
Cdd:cd09237  309 EFFEKLKKAYNSFKKFSAGLPKGLEFYDDLLKMA 342
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
365-698 1.03e-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: 85.42  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 365 PVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPA--AIEDVSGDTVPQSILTKSRSV-IEQGGIQTVDQL 441
Cdd:cd09234    1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPlnVMDMDGQFELPQDLVERCAALsVRPDTIKNLVEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 442 IKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKerwQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSH 521
Cdd:cd09234   81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVG---KRGSSIAHVTELKRELKKYKEAHEKASQSNTELHKAMNLH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 522 RDTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSV--NFDMTSKFLTALAQDGvi 599
Cdd:cd09234  158 IANLKLLAGPLDELQKKLPSPSLLDRPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAihEDDITSKLVTTTGGDM-- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 600 neEALSVTELDRvYGGLTTKVQESLKKQEGLLKN-IQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEG 678
Cdd:cd09234  236 --EDLFKEELKK-HDQLVNLIEQNLAAQENILKAlTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKG 312
                        330       340
                 ....*....|....*....|
gi 241982780 679 TKFYNELteilvrfQNKCSD 698
Cdd:cd09234  313 IDFYKKL-------EGNVSK 325
BRO1_Brox_like cd09243
Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...
91-330 9.83e-15

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: 76.61  E-value: 9.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  91 LTFTWKDafdkgSLFGGSVkLALASLGYEKSCVLFNCAAL----ASQIAAEQNLDNDEG------LKIAAkhyqfasGAF 160
Cdd:cd09243   85 INFKWTD-----SLLGNEP-SVQQDAIFELASMLFNVALWytkhASKLAGKEDITEDEAkdvhksLRTAA-------GIF 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 161 LHIKETVLSALSR--EPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAfkqcqyKDTL- 237
Cdd:cd09243  152 QFVKENYIPKLIEpaEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKA------DDSLs 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 238 ---PKYF-----YFQevfpvlaAKHCIMQANAE-YH-QSILAKQqkKFGEEIARLQHAAELIKTVASRYDEYVNVKD--- 304
Cdd:cd09243  226 sldPEYSgkwrkYLQ-------LKSVFYLAYAYcYHgETLLAKD--KCGEAIRSLQESEKLYNKAEALCKEYAKTKGpgt 296
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 241982780 305 --------FSDK----INRALAAAKKDNDFIYHDRVPD 330
Cdd:cd09243  297 takpdqhlFFRKlgplVKRTLEKCERENGFIYHQKVPD 334
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
114-339 1.28e-13

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: 73.19  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 114 ASLGYEKSCVLFNCAALASQIAAEQNLDNDegLKIAAKHYQFASGAFLHIKETVLSALSREPTVDISPD--TVG---TLS 188
Cdd:cd09247  106 DSLRFELGMVLFLYGAALRERASEVLPTED--FKEAATHLRRAAGVFEFLAHDELPRLRGALSADERPPecTPSlalAMS 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 189 LIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAfKQ------CQYKDTLPKyfyFQEVFPVLAAKHcimQANAE 262
Cdd:cd09247  184 LLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEA-KNvlrslaTDLKDLDPR---FLRFISSCIALH---EARSQ 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 263 YHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNV--KDFSDKINRALAAAKKDNDFIYHDRVPDLKDL-DPIGK 339
Cdd:cd09247  257 LYLARRLKEAGHIGVAVGVLREALRNLKKKLPGSDISSPVifRDERAEVATLLQKYEKENEVIYFEKVPDIDELpLPEGK 336
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
91-353 1.67e-07

Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; This family contains the Bro1-like domain of Ustilago maydis Rim23 (also known as PalC), and related proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Rim20 and Rim23 participate in the response to the external pH via the Rim101 pathway. Through its Bro1-like domain, Rim23 allows the interaction between the endosomal and plasma membrane complexes. Bro1-like domains are boomerang-shape, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Intermediates in the Rim101 pathway may play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.


Pssm-ID: 185768  Cd Length: 413  Bit Score: 54.72  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  91 LTFTWKDAFdKGSLFGGSVKLALASLGYEKSCVLFNCA-ALASQ----------------IAAEQNLDNDEGLKIAAKHY 153
Cdd:cd09245   88 PTFEWRTTL-SSTSGRESPRLPLPGLHYELAFVLLTYAyALSNLarsilaplgayetdrsISDASRKQRDERLKAATKLL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 154 QFASGAFLHIKETVLSALSRE-----PTVDISPDTVGTLSLIMLAQAQEVFFLK-----ATRDKMKD------------- 210
Cdd:cd09245  167 CKAAGIFDYLATRVLPQWESNrggapPPPDLSPEVLSALSSLALAEATLLAVRKldpypAAVDKDWMtpgpplpkvhpsa 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 211 AIIAKLANQAADYFGDAFKQCQykdTLPKYFYFQEVFP-------VLAAKHcimQANAEYHQSILAKQQKKFGEEIARLQ 283
Cdd:cd09245  247 HLLARLCLAASEHAESARALLS---TPGSKRGSGEVSEellrylsDLRRVA---RALACKFLGIDAGENGKVGEAIGWLR 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780 284 HAA---ELIKTVASRYDEYVNVKDFSDK------------------INRALAAAKKDNDFIYHDRVPDLKDLD---PIGK 339
Cdd:cd09245  321 AAKkelEDLKSPSGVASKAKLKKSWKEKredrkvekgagveeelrtLEMLLKKYKKMNDTVSFQPVPPSSELQssmPSGR 400
                        330
                 ....*....|....
gi 241982780 340 AtLVKSTPVNVPIS 353
Cdd:cd09245  401 E-AHTAKPYTPPPS 413
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
819-873 4.09e-05

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: 44.78  E-value: 4.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 241982780   819 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPF-PQPPQQSYYPQQ 873
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
YppG COG5894
Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];
829-867 6.97e-05

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


Pssm-ID: 444596 [Multi-domain]  Cd Length: 112  Bit Score: 42.92  E-value: 6.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 241982780 829 YAYGQYNMPYP-PVYHQSPGQAPYPGPQQPSYPFPQPPQQ 867
Cdd:COG5894   22 QPYGPYQNQHQqPYYQQTNTQQPFPPPSPTPYPSPKPLQT 61
SGP pfam17228
Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by ...
825-868 2.83e-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: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 241982780  825 GYNPYAYG---------QYNMPYPPVYHQSPGQAPYPGPQQPSypfPQPPQQS 868
Cdd:pfam17228  47 GYGDYGYGnpygygypyGYGAPYGAPYGYGPYGAPYGAPVAPA---PAAPAEA 96
PHA03247 PHA03247
large tegument protein UL36; Provisional
717-871 3.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982780  717 SIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPG 796
Cdd:PHA03247 2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPA 2776
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 241982780  797 SAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYP 871
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
RCR pfam12273
Chitin synthesis regulation, resistance to Congo red; RCR proteins are ER membrane proteins ...
825-873 3.49e-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: 38.16  E-value: 3.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 241982780  825 GYNPYaYGQ---YNMPYPPVYHQSPGQAPYPGPQQPSY-----------------PFPQPPQQSYYPQQ 873
Cdd:pfam12273  30 GLQPI-YGTgwmGGGPPPPSYGQSQQDPQPTGTYVPTYtpndgyydqqgnfhnagSGLQPPQQAYQPPT 97
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
831-873 5.74e-03

YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 115 and 181 amino acids in length. There are two completely conserved residues (F and G) that may be functionally important.


Pssm-ID: 372950 [Multi-domain]  Cd Length: 101  Bit Score: 37.10  E-value: 5.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 241982780  831 YGQYNMPYPpVYHQSPGQAP----YPgPQQPSYPFPQPPQQSY--YPQQ 873
Cdd:pfam14179   1 YQHNSQPYP-YFSQQVYQQPvqpqYP-PFAPQQYMPQPPMPYMnpYPKQ 47
SKG6 pfam08693
SKG6 family; SKG6/Axl2 are membrane proteins that show polarised intracellular localization. ...
819-872 7.39e-03

SKG6 family; SKG6/Axl2 are membrane proteins that show polarised intracellular localization. SKG6_Tmem is the highly conserved transmembrane alpha-helical domain of SKG6 and Axl2 proteins,. The full-length fungal protein has a negative regulatory function in cytokinesis.


Pssm-ID: 462564  Cd Length: 663  Bit Score: 40.12  E-value: 7.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 241982780  819 QMPMPMGYNPYAYGQYN--MPYPPVYHQspgQAPYPGPQQP-SYPFPQPPQQSYYPQ 872
Cdd:pfam08693 429 QQPVYNHQQQYSASQYNnnHQQQQYAYQ---PHQYYPQQQNyGYPQPQMQIQYNHPQ 482
 
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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