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Conserved domains on  [gi|755531729|ref|XP_011241243|]
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programmed cell death 6-interacting protein isoform X1 [Mus musculus]

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: 608.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKE 444
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 445 LPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDT 524
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 525 IALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEAL 604
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 605 SVTELDRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 684
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                        330
                 ....*....|....*....
gi 755531729 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: 608.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   2 ASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGgEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPK 81
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSG-EEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  82 FPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFL 161
Cdd:cd09240   80 FPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 162 HIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYF 241
Cdd:cd09240  160 HLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 242 YFQEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALTAAKKDND 321
Cdd:cd09240  238 LPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDND 317

                        330       340
                 ....*....|....*....|....*....
gi 755531729 322 FIYHDRVPDLKDLDPIGKATLVKPTPVNV 350
Cdd:cd09240  318 FIYHDRVPDVKSLPPIGKAALAKPTPVNV 346
Amelogenin super family cl33250
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 823-877 2.22e-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: 45.55  E-value: 2.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755531729   823 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPF-PQPPQQSYYPQQ 877
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
 
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: 608.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKE 444
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 445 LPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDT 524
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 525 IALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEAL 604
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 605 SVTELDRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 684
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                        330
                 ....*....|....*....
gi 755531729 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: 608.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   2 ASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGgEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPK 81
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSG-EEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  82 FPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFL 161
Cdd:cd09240   80 FPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 162 HIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYF 241
Cdd:cd09240  160 HLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 242 YFQEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALTAAKKDND 321
Cdd:cd09240  238 LPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDND 317

                        330       340
                 ....*....|....*....|....*....
gi 755531729 322 FIYHDRVPDLKDLDPIGKATLVKPTPVNV 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 1.12e-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: 460803  Cd Length: 366  Bit Score: 421.99  E-value: 1.12e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729    4 FIWVQLKKTSEVDLAKPLVKFIQQTYpsGGEEQAQYCRAAEELSKLRRSALgRPLDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTY--GSQDPSSFEDDLAELNKLRQDAV-RGANEDESGLDLLYKYYAQLELLELRFP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   84 FsENQICLTFTWKDAFDKGSlfggsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:pfam03097  78 I-DIQIGIEFTWYDAFGTSS-----KKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  164 KDTVLSAlsrePTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKyfyf 243
Cdd:pfam03097 152 KENFLHA----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDK---- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  244 qEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNvASRYDEYVNV----KDFSDKINRALTAAKKD 319
Cdd:pfam03097 224 -EWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKE-ALKSDRYKKVledlKGLLDVVEEKLKRAEKD 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531729  320 NDFIYHDRVPDLKDLDPIGKATLVKPTPVN-VPVSQKFTDLFEKMVPVSVQQSLAVFSQRKADLV 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 1.11e-138

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: 417.14  E-value: 1.11e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729     4 FIWVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSALGRplDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETY---SEDSSSYEDEIAELNRLRQAARTP--SRDESGLELLLKYYGQLEALELRFP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729    84 FSENQICLTFTWKDAFDkgslfgGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:smart01041  76 PPEGQLKLSFTWYDSLD------TGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   164 KDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMK--DAIIAKLANQAADYFGDAFKQCQYKDTLPKYF 241
Cdd:smart01041 150 KENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGYI 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   242 YFqEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKN-----------VASRYDEYVNvkDFSDKIN 310
Cdd:smart01041 230 PK-SWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEakkhlrckklgKADKLQEDLS--GLKDVVE 306

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531729   311 RALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNVPVsqKFTDLFEKMVPVSVQQSLAVFSQRKADLVNRSI 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 4.39e-104

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: 323.80  E-value: 4.39e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  417 TVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAE 496
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  497 GAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELNAAIPSANPAK-TMQGSEVVSVLKSLLSNLDEIKKERESLE 575
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  576 NDLK--SVNFDMTSKFLTALAQDGVIN-EEALSVTELDrIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNE-A 651
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755531729  652 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 706
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 823-877 2.22e-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: 45.55  E-value: 2.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755531729   823 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPF-PQPPQQSYYPQQ 877
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
YppG COG5894
Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];
833-871 1.39e-04

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


Pssm-ID: 444596 [Multi-domain]  Cd Length: 112  Bit Score: 42.15  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755531729 833 YAYGQYNMPYP-PVYHQSPGQAPYPGPQQPTYPFPQPPQQ 871
Cdd:COG5894   22 QPYGPYQNQHQqPYYQQTNTQQPFPPPSPTPYPSPKPLQT 61
RCR pfam12273
Chitin synthesis regulation, resistance to Congo red; RCR proteins are ER membrane proteins ...
 829-877 7.32e-04

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: 40.09  E-value: 7.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755531729  829 GYNPYaYGQ---YNMPYPPVYHQSPGQAPYPGPQQPTY-----------------PFPQPPQQSYYPQQ 877
Cdd:pfam12273  30 GLQPI-YGTgwmGGGPPPPSYGQSQQDPQPTGTYVPTYtpndgyydqqgnfhnagSGLQPPQQAYQPPT 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 377-656 2.02e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   377 QRKADLVNRSIAQMREATTLANGVLASLNlpAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRnREIL 456
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLR--KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   457 EESLRLLDEEEATDNDLRAKFKDRWQRTpsNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELN 536
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQL--KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   537 AAIPSANpaktMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRIYGGL 616
Cdd:TIGR02168  845 EQIEELS----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 755531729   617 TSKVQESLKKQEGLlkniqvshqefsKMKQSNNEANLREE 656
Cdd:TIGR02168  921 REKLAQLELRLEGL------------EVRIDNLQERLSEE 948
 
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: 608.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKE 444
Cdd:cd09235    1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNLPAAIEDVSGDTVPQSLLEKSRTVIEKGGIQTIDQLIKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 445 LPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDT 524
Cdd:cd09235   81 LPELLQRNREILDEALRMLDEEEASDNQLRAQFKERWTRTPSNKLTKPLRAEGSKYRTILDNAVQADKIVREKYESHREG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 525 IALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEAL 604
Cdd:cd09235  161 IELLSKPEEELANAIPSASPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKSATFDMKSKFLSALAQDGAINEEAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 605 SVTELDRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNE 684
Cdd:cd09235  241 SVEELDRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSNSGANEREEVLKDLAAAYDAFMELTANLKEGTKFYND 320

                        330
                 ....*....|....*....
gi 755531729 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: 608.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   2 ASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGgEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPK 81
Cdd:cd09240    1 ASFISVPLKKSSEVDLVKPLEKFIKNTYSSG-EEQADYKEAIKELNKLRNNAVCRPLDKHESSLELLLRYYDQLCAIEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  82 FPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFL 161
Cdd:cd09240   80 FPFSESQIQVTFTWKDAFDKGSLFGGSKKLALSSLGYEKVCVLFNIAALQSQIAAEQNLDTDEGLKLAAKLFQQAAGIFN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 162 HIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTlpKYF 241
Cdd:cd09240  160 HLKETVLSALQQEPTPDLSPDTLSALSALMLAQAQEVFYLKATRDKMKDAIIAKLAAQAADYYGDAFKQCQREDV--RSL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 242 YFQEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALTAAKKDND 321
Cdd:cd09240  238 LPKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQHALELIKTAQSRAGEYVDVKDFAAKISRALTAAKKDND 317

                        330       340
                 ....*....|....*....|....*....
gi 755531729 322 FIYHDRVPDLKDLDPIGKATLVKPTPVNV 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 1.12e-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: 460803  Cd Length: 366  Bit Score: 421.99  E-value: 1.12e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729    4 FIWVQLKKTSEVDLAKPLVKFIQQTYpsGGEEQAQYCRAAEELSKLRRSALgRPLDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:pfam03097   1 LLSIPLKKTEEVDLKKPLKNYISSTY--GSQDPSSFEDDLAELNKLRQDAV-RGANEDESGLDLLYKYYAQLELLELRFP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   84 FsENQICLTFTWKDAFDKGSlfggsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:pfam03097  78 I-DIQIGIEFTWYDAFGTSS-----KKVSQSSLAFEKASVLFNIAALYSQLAASQNRSTDEGLKRACKYFQQAAGCFQYL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  164 KDTVLSAlsrePTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKyfyf 243
Cdd:pfam03097 152 KENFLHA----PSPDLSPETLKALSNLMLAQAQECFWEKAINDNKKDSLIAKLAAQVSELYEEALEALKLSGLIDK---- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  244 qEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNvASRYDEYVNV----KDFSDKINRALTAAKKD 319
Cdd:pfam03097 224 -EWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARLQLALSLLKE-ALKSDRYKKVledlKGLLDVVEEKLKRAEKD 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531729  320 NDFIYHDRVPDLKDLDPIGKATLVKPTPVN-VPVSQKFTDLFEKMVPVSVQQSLAVFSQRKADLV 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 1.11e-138

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: 417.14  E-value: 1.11e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729     4 FIWVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSALGRplDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:smart01041   1 LIPLPLKETKEVDFSKPLKDYIKETY---SEDSSSYEDEIAELNRLRQAARTP--SRDESGLELLLKYYGQLEALELRFP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729    84 FSENQICLTFTWKDAFDkgslfgGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:smart01041  76 PPEGQLKLSFTWYDSLD------TGVPSTQSSLAFEKASVLFNLGALYSQIAAEQNRDTEEGLKEACKAFQQAAGVFNYL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   164 KDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMK--DAIIAKLANQAADYFGDAFKQCQYKDTLPKYF 241
Cdd:smart01041 150 KENFLHALSTEPSVDLSPETLSALSSLMLAQAQECFFEKAILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVKGYI 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   242 YFqEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKN-----------VASRYDEYVNvkDFSDKIN 310
Cdd:smart01041 230 PK-SWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIARLQEALERLKEakkhlrckklgKADKLQEDLS--GLKDVVE 306

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531729   311 RALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNVPVsqKFTDLFEKMVPVSVQQSLAVFSQRKADLVNRSI 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 4.39e-104

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: 323.80  E-value: 4.39e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  417 TVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAE 496
Cdd:pfam13949   1 GLPPSLREKAEEVRQQGGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATLRAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  497 GAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELNAAIPSANPAK-TMQGSEVVSVLKSLLSNLDEIKKERESLE 575
Cdd:pfam13949  81 IRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSSRRAKnSPSVEEQVAKLRELLNKLNELKREREQLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  576 NDLK--SVNFDMTSKFLTALAQDGVIN-EEALSVTELDrIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNE-A 651
Cdd:pfam13949 161 KDLKekARNDDISPKLLLEKARLIAPNqEEQLFEEELE-KYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSEkQ 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755531729  652 NLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTE 706
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARRSE 294
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 365-703 5.18e-101

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: 317.75  E-value: 5.18e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSI-AQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIK 443
Cdd:cd08915    1 PYDVIESASAYNERQDDYVREHIvEPIEALNKLLNSFLAERNLPASIDDLQKPENLPDSIQHSQEIIEEGGLDNIEQSFK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 444 ELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTP-SNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHR 522
Cdd:cd08915   81 ELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPsSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 523 DTIALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDL--KSVNFDMTSKFLTALAQDGVIN 600
Cdd:cd08915  161 PNLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELeiKSRNNDILPKLITEYKKNGTTE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 601 EEALSVTELdRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTK 680
Cdd:cd08915  241 FEDLFEEHL-KKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKNSNDSLDPREEALQDLEASYKKYLELKENLNEGSK 319

                        330       340
                 ....*....|....*....|...
gi 755531729 681 FYNELTEILVRFQNKCSDIVFAR 703
Cdd:cd08915  320 FYNDLIEKVNRLLEECEDFVNAR 342
BRO1_Alix_like cd09034
Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...
 4-348 4.14e-97

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: 307.74  E-value: 4.14e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   4 FIWVQLKKTSEVDLAKPLVKFIQQTYPSggEEQAQYCRAAEELSKLRRSALGRPLDK--HEGALETLLRYYDQICSIEPK 81
Cdd:cd09034    1 FIGLPLKKTKEVDVKVPLSKFIPKNYGE--LEATAVEDLIEKLSKLRNNIVTEQNNDttCENLLEALKEYLPYLLGLEKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  82 FPFSENQICLTFTWKDAFDKGslfggsVKLALaSLGYEKSCVLFNCAALASQIAAEQNLDN-DEGLKTAAKQYQFASGAF 160
Cdd:cd09034   79 LPFQKLRDNVEFTWTDSFDTK------KESAT-SLRYELLSILFNLAALASQLANEKLITGsEEDLKQAIKSLQKAAGYF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 161 LHIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKM-KDAIIAKLANQAADYFGDAFKQCQYKDTLPK 239
Cdd:cd09034  152 EYLKEHVLPLPPDELPVDLTEAVLSALSLIMLAQAQECFLLKAEEDKKaKLSLLARLACEAAKYYEEALKCLSGVDLETI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 240 YFYFQEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEY-----VNVKDFSDKINRALT 314
Cdd:cd09034  232 KNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAALELLKESERLCKSFlldvwGNLKKLKEKIEKELE 311

                        330       340       350
                 ....*....|....*....|....*....|....
gi 755531729 315 AAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPV 348
Cdd:cd09034  312 KAERENDFIYFEEVPPEDPLPEIKGALLVKPPPL 345
BRO1_Alix_like_1 cd09246
Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...
 10-349 1.96e-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: 266.19  E-value: 1.96e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  10 KKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAA-EELSKLRRSALgRPLDKHEGALETLLRYYDQICSIEPKFPFSENQ 88
Cdd:cd09246    7 KKTETVDLVSPLRAYISETY---SEREAQDAEDDlAELQQLRSEVR-TLQEKHAASRELLLRYYRALCAVESRFPISEES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  89 --ICLTFTWKDAFDkgslfgGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDT 166
Cdd:cd09246   83 ghARVSFSWYDAFR------PHRKATQANVHFEKAAVLFNLGALSSQLGLQQDRTTAEGIKQACHAFQAAAGAFAHLRDK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 167 VLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCqykDTLPKYFYFQEV 246
Cdd:cd09246  157 VSGKTGGFRTPDLTAECLGMLESLMLAQAQECFYEKAVADGKSPAVCSKLAKQARSYYEEALEAL---DSPPLKGHFDKS 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 247 FPT-LAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNvASRYDEYVNVKDFSDK-------INRALTAAKK 318
Cdd:cd09246  234 WVAhVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLRAASDALAE-ARKQAKGVNGDELIEAvseleqvINELLERAEK 312

                        330       340       350
                 ....*....|....*....|....*....|.
gi 755531729 319 DNDFIYHDRVPDLKDLDPIGKATLVKPTPVN 349
Cdd:cd09246  313 ENDCVYLDRVPAPSDLPPLGAASMVKPAAPP 343
BRO1_ScRim20-like cd09241
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...
 4-370 1.21e-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: 245.64  E-value: 1.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   4 FIWVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSALGrpLDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:cd09241    2 LLSIPFKRTLPVDLKDALRNYISNHY---FQTPSSFEDDLAEIDKLRNDAIN--PEPSVNGLSLLKEYYAQLVVLSKKFP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  84 fsenQICLTFTWKDAFDKGSlfggSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:cd09241   77 ----DDQLEFTWYPTLGYKS----SGPVSLSSLKFERANILYNLGALYSQLALSENRYTDEGLKRACSYFQASAGCFEYI 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 164 KDTVLSALSREPtvDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKYFyf 243
Cdd:cd09241  149 LQHLLPTLSPPP--DLDENTLKALESLMLAQAQECFWQKAISDGTKDSLIAKLAAQVSDYYQEALKYANKSDLIRSDW-- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 244 qevFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNvASRYDEYVNVK------DFSDKINRALTAAK 317
Cdd:cd09241  225 ---INHLKVKKHHFKAAAHYRMALVALEKSKYGEEVARLRVALAACKE-ALKEARYGNKAvledlqGLKDIVKESLKRAE 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755531729 318 KDNDFIYHDRVPDLKDLDPIGKATLVKP-TPVNVPVSQKF-TDLFEKMVPVSVQQ 370
Cdd:cd09241  301 RDNDLIYLQPVPPASELPPIKPASMVKAiVPPELEEGSKLgKPLFKDLLPYGVHE 355
BRO1_ScBro1_like cd09242
Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...
 4-349 2.47e-73

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: 244.50  E-value: 2.47e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   4 FIWVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSALGRplDKHEGALETLLRYYDQICSIEPKFP 83
Cdd:cd09242    1 LISLPLKDTEEVDWKKPLSSYLKRSY---GSSTFYYEEEIAEFDRLRQDANGV--LADETGRDLLYKYYGQLELLELRFP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  84 FSENQICLTFTWKDAFDKGSLFGGSvklalaSLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:cd09242   76 FNNKELKVDFTWYDAFYKSKKVKQH------SLAFEKASVLFNIGALLSQLAAEKYREDEDDLKEAITNLQQAAGCFQYI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 164 KDTVLSAlsrePTVDISPDTVGTLSLIMLAQAQEVFFLKATRDK---MKDAIIAKLANQAADYFGDAFKqcQYKDTLPK- 239
Cdd:cd09242  150 NENFLHA----PSVDLQQENVKFLVKLMLAQAQEIFLLKLINGDdaqKKASLISKLASATANLYESCVE--FLKEIQEKg 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 240 YFYFQEVFPTLA-AKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIK--------NVASRYDEY----VNVKDFS 306
Cdd:cd09242  224 ISYGDPKWISLVqCKAHYYKSLAAYYHALALEAAGKYGEAIAYLTQAESILKeanpqklsLKASAGDAAyalnDDFKGQK 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 755531729 307 DKINRALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVN 349
Cdd:cd09242  304 DTVEEKLKELEKDNDFIYHDIVPSEVTLPSIKPLDAAKPIPIE 346
BRO1_HD-PTP_like cd09239
Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...
 5-350 2.08e-59

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: 206.90  E-value: 2.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   5 IWVQLKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSALGRPLDKhEGALeTLLRYYDQICSIEPKFPF 84
Cdd:cd09239    9 LWLQLKSSGEFTFQPALKKYILENY---GEDPELYSEELKSLEQLRQEAVNPPRDF-EGCS-VLKRYYGQLHLLQSRFPM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  85 -SENQICLTFTWKDAFDKGSLFGGSVKlalaslgYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHI 163
Cdd:cd09239   84 gAGQEAAVPFTWTDIFSGSEVTHEDIK-------FEEASVLYNIGALHSQLGASDKRDSEEGMKVACTHFQCAAWAFAYL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 164 KDTVLSALSrepTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQ-----CQYKDTLP 238
Cdd:cd09239  157 REHYPQVYG---AVDMSSQLLSFNYSLMLAQAQECLLEKSLLDNRKSHITAKVSAQVVEYYKEALRAlenweSNSKIILG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 239 KYFyfqevfpTLAAKQCIMQAN-----AEYHQSILAKQQKKFGEEIARLQHA----AELIKNvASRYDEYVNVKDFS--- 306
Cdd:cd09239  234 KIQ-------KEWRKLVQMKIAyyasiAHLHMGKQSEEQQKMGERVAYYQLAndklEEAIKN-AKGQPDTVNLQEALsft 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 755531729 307 -DKINRALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNV 350
Cdd:cd09239  306 mDVIGGKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPFSP 350
V_AnPalA_UmRIM20_like cd09236
Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...
 365-703 1.56e-48

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: 176.01  E-value: 1.56e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREA-TTLANGVLASLNLPAAIEDVS---GdtVPQSILTKSTSVVEQGGIQTVDQ 440
Cdd:cd09236    1 PFGVHLAISIYDDRKDRLVNESIIDELEElTNRAHSTLRSLNLPGSLQALEkplG--LPPSLLRHAEEIRQEDGLERIRA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 441 LIKELPELLQRNREILEESLRLLDEEEATDNDLRAKF-KDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQ 519
Cdd:cd09236   79 SLDDVARLAASDRAILEEAMDILDDEASEDESLRRKFgTDRWTRPDSHEANPKLYTQAAEYEGYLKQAGASDELVRRKLD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 520 SHRDTIALLCKPEPELNAAIPSAN-PAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDL--KSVNFDMTSKFLTA---L 593
Cdd:cd09236  159 EWEDLIQILTGDERDLENFVPSSRrPSIPPELERHVRALRVSLEELDRLESRRRRKVERArtKARADDIRPEILREaarL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 594 AQDGVINE------EALSVTELdRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDN 667
Cdd:cd09236  239 EREYPATEvapahfEDLFDKRL-AKYDKDLDAVSEEAQEQEEILQQIEVANKAFLQSRKGDPATKERERALQSLDLAYFK 317

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 755531729 668 FVELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 703
Cdd:cd09236  318 YKEIVSNLDEGRKFYNDLAKILSQFRDACKAWVYER 353
BRO1_Rhophilin cd09244
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...
 9-202 8.43e-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: 121.68  E-value: 8.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   9 LKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSAlgRPLDKHEGALETLLRYYDQICSIEPKFPFSENQ 88
Cdd:cd09244    6 LKETKEIDFMEPFKDFILEHY---SEDPSLYEDEIADFTDLRQAM--RTPSRDEAGIELLFEYYNQLYFVERRFFPPDRS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  89 ICLTFTWKDafdkgSLFGgsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTvl 168
Cdd:cd09244   81 LGIYFHWYD-----SLTG--VPSVQRSVAFEKASVLFNIGALYTQIGAKQDRTTEEGIEAAVDAFQRAAGAFNYLREN-- 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 755531729 169 saLSREPTVDISPDTVGTLSLIMLAQAQEVFFLK 202
Cdd:cd09244  152 --FSNAPSMDLSPEMLEALIKLMLAQAQECVFEK 183
BRO1_Rhophilin_1 cd09248
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-1; This subfamily ...
 9-277 1.66e-27

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: 115.75  E-value: 1.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   9 LKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSAlgRPLDKHEGALETLLRYYDQICSIEPKFPFSENQ 88
Cdd:cd09248    6 LKETKELDLPTPLKELISEHF---GEDGTSYEAEIRELEDLRQAM--RTPSRSEAGLELLMAYYNQLCFLDARFFPPAKS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  89 ICLTFTWKDafdkgSLFGgsVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTvl 168
Cdd:cd09248   81 LGLFFHWYD-----SLTG--VPAQQRALAFEKGSVLFNIGALHTQIGARQDRSCTEGTRRAIDAFQRAAGAFSLLREN-- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 169 saLSREPTVDISPDTVGTLSLIMLAQAQEVFF------LKATRDKMKDAI-IAKLANQAADYFG---DAFKQCQYKDTLP 238
Cdd:cd09248  152 --FSNAPSPDMSTASLSMLEQLMVAQAQECIFeglllpLLATPQDFFAQLqLAQEAAQVAAEYRlvhRTMAQPPVRDYVP 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 755531729 239 ---------KYFYFQEVFPTLAAKQCIMQANAEyhQSILAKQQKKFGE 277
Cdd:cd09248  230 fswtalvhvKAEHFCALAHYHAAMALCDSSPAS--EGELATQEKAFLQ 275
V_Alix_like_1 cd09238
Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...
 365-703 1.44e-24

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: 106.02  E-value: 1.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKE 444
Cdd:cd09238    1 PESSAKALSKYTEMVDELIRTEADRLAAASDEARVALREMELPETLIALDGGASLPGDLGLDEEVEAVQISGGLAALEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 445 LPELLQRNR---EILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSH 521
Cdd:cd09238   81 LPRLRELRRvctELLAAAQESLEAEATEDSAARTQYGTAWTRPPSATLTKNLWERLNRFRVNLEQAGDSDESLRRRIEDA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 522 RDTIALLCKPE-----PELNAAIPSANPAKtmqgSEVVSVLKSLLSNLDEIKKERESLENDLKSV--NFDMTSKFLTAla 594
Cdd:cd09238  161 MDGMLILDDEPaaaaaPTLRAPMLSTDEDD----ASIVGTLRSNLEELEALGNERAGIEDMMKALkrNDNILAKVMAT-- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 595 qdgVINEEALSVTELDRiYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKM--------KQSNNEANLREEVLKnlatayd 666
Cdd:cd09238  235 ---TGSYDALFKEELKK-YDSVREAVSKNISSQDDLLSRLRALNEKFSQIfdvegwraATESHATQIRAAVAK------- 303

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 755531729 667 nFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR 703
Cdd:cd09238  304 -YRELREGMEEGLRFYSGFQEAVRRLKQECEDFVMTR 339
V_ScBro1_like cd09237
Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...
 365-689 3.71e-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: 98.90  E-value: 3.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGgiqTVDQLIKE 444
Cdd:cd09237    1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNLPKLLVDLKERFEGENELMEIVSGLKSS---SVDSQLEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 445 LPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDT 524
Cdd:cd09237   78 LRPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLVDPVKED 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 525 IALLCKPEPELNAA-IPSANPAKTM---------QGSEV---VSVLKSLLSNLDEIKKERESLENDLKS-VNFDMTSKFL 590
Cdd:cd09237  158 IALLLNGGSLWEELfGFSSSGSPEPslldlddsqNEQTVlkqIKQLEELLEDLNLIKEERQRVLKDLKQkIHNDDISDIL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 591 TAL--AQDGVinEEALSVTELDRiYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEA-------NLREEVLKNL 661
Cdd:cd09237  238 ILNskSKSEI--EKQLFPEELEK-FKPLQNRLEATIFKQSSLINELKIELDKLFKLPGVKEKQskekskqKLRKEFFEKL 314

                        330       340
                 ....*....|....*....|....*...
gi 755531729 662 ATAYDNFVELVANLKEGTKFYNELTEIL 689
Cdd:cd09237  315 KKAYNSFKKFSAGLPKGLEFYDDLLKMA 342
BRO1_Rhophilin_2 cd09249
Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin-2; This subfamily ...
 9-221 6.82e-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: 98.77  E-value: 6.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   9 LKKTSEVDLAKPLVKFIQQTYpsgGEEQAQYCRAAEELSKLRRSAlgRPLDKHEGALETLLRYYDQICSIEPKFPFSENQ 88
Cdd:cd09249    6 LKETKDVDFSVPLKDFILEHY---SEDGSEYEDEIADLMDLRQAC--RTPSRDEAGVELLMSYFSQLGFLENRFFPPTRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  89 ICLTFTWKDAFDkgslfggSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTvl 168
Cdd:cd09249   81 MGILFTWYDSFT-------GVPVSQQNLLLEKASILFNIGALYTQIGTRCNRQTQAGLESAVDAFQRAAGVLNYLKET-- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755531729 169 saLSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDA--IIAKLANQAA 221
Cdd:cd09249  152 --FTHTPSYDMSPAMLSVLVKMMLAQAQECLFEKISLPGIRNEffTLVKMAQEAA 204
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 365-698 1.01e-20

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: 94.28  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 365 PVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPA--AIEDVSGDTVPQSILTKSTSV-VEQGGIQTVDQL 441
Cdd:cd09234    1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPlnVMDMDGQFELPQDLVERCAALsVRPDTIKNLVEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 442 IKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKdrwQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSH 521
Cdd:cd09234   81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVG---KRGSSIAHVTELKRELKKYKEAHEKASQSNTELHKAMNLH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 522 RDTIALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSV--NFDMTSKFLTALAQDGvi 599
Cdd:cd09234  158 IANLKLLAGPLDELQKKLPSPSLLDRPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAihEDDITSKLVTTTGGDM-- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 600 neEALSVTELDRiYGGLTSKVQESLKKQEGLLKN-IQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEG 678
Cdd:cd09234  236 --EDLFKEELKK-HDQLVNLIEQNLAAQENILKAlTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKG 312

                        330       340
                 ....*....|....*....|
gi 755531729 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 ...
 91-347 3.67e-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: 77.77  E-value: 3.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  91 LTFTWKDafdkgSLFGGSVkLALASLGYEKSCVLFNCAAL----ASQIAAEQNLDNDEGlKTAAKQYQFASGAFLHIKDT 166
Cdd:cd09243   85 INFKWTD-----SLLGNEP-SVQQDAIFELASMLFNVALWytkhASKLAGKEDITEDEA-KDVHKSLRTAAGIFQFVKEN 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 167 VLSALSR--EPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAfkqcqyKDTL----PKY 240
Cdd:cd09243  158 YIPKLIEpaEKGSDLDPRVLEAYINQCTAEAQEVTVARAIELKHNAGLISALAYETAKLFQKA------DDSLssldPEY 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 241 F-----YFQevfptlaAKQCIMQANAE-YH-QSILAKQqkKFGEEIARLQHAAELIKNVASRYDEYVNVKD--------- 304
Cdd:cd09243  232 SgkwrkYLQ-------LKSVFYLAYAYcYHgETLLAKD--KCGEAIRSLQESEKLYNKAEALCKEYAKTKGpgttakpdq 302

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755531729 305 --FSDK----INRALTAAKKDNDFIYHDRVPD-LKDLDPigKAT--LVKPTP 347
Cdd:cd09243  303 hlFFRKlgplVKRTLEKCERENGFIYHQKVPDeVPQLEL--KATygLVSPEE 352
BRO1_Alix_like_2 cd09247
Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...
 114-348 7.55e-12

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: 67.80  E-value: 7.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 114 ASLGYEKSCVLFNCAALASQIAAEQNLDNDegLKTAAKQYQFASGAFLHIKDTVLSALSREPTVDISPD--TVG---TLS 188
Cdd:cd09247  106 DSLRFELGMVLFLYGAALRERASEVLPTED--FKEAATHLRRAAGVFEFLAHDELPRLRGALSADERPPecTPSlalAMS 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 189 LIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAfKQ------CQYKDTLPKYFYFqevfptLAAKQCIMQANAE 262
Cdd:cd09247  184 LLCLAEAQAVTARKAEEKGTSPSLLAKLHYGATQFLEEA-KNvlrslaTDLKDLDPRFLRF------ISSCIALHEARSQ 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 263 YHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNV--KDFSDKINRALTAAKKDNDFIYHDRVPDLKDL-DPIGK 339
Cdd:cd09247  257 LYLARRLKEAGHIGVAVGVLREALRNLKKKLPGSDISSPVifRDERAEVATLLQKYEKENEVIYFEKVPDIDELpLPEGK 336


                 ....*....
gi 755531729 340 aTLVKPTPV 348
Cdd:cd09247  337 -VIVKPVPY 344
BRO1_UmRIM23-like cd09245
Protein-interacting, Bro1-like domain of Ustilago maydis Rim23 (PalC), and related domains; ...
 91-353 1.70e-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: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729  91 LTFTWKDAFdKGSLFGGSVKLALASLGYEKSCVLFNCA-ALASQ----------------IAAEQNLDNDEGLKTAAKQY 153
Cdd:cd09245   88 PTFEWRTTL-SSTSGRESPRLPLPGLHYELAFVLLTYAyALSNLarsilaplgayetdrsISDASRKQRDERLKAATKLL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 154 QFASGAFLHIKDTVLSALSRE-----PTVDISPDTVGTLSLIMLAQAQEVFFLK-----ATRDKMKD------------- 210
Cdd:cd09245  167 CKAAGIFDYLATRVLPQWESNrggapPPPDLSPEVLSALSSLALAEATLLAVRKldpypAAVDKDWMtpgpplpkvhpsa 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 211 AIIAKLANQAADYFGDAFKQCQykdTLPKYFYFQEVFPTLAA----KQCIMQANAEYHQSILAKQQKKFGEEIARLQHAA 286
Cdd:cd09245  247 HLLARLCLAASEHAESARALLS---TPGSKRGSGEVSEELLRylsdLRRVARALACKFLGIDAGENGKVGEAIGWLRAAK 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729 287 ---ELIKNVASRYDEYVNVKDFSDK------------------INRALTAAKKDNDFIYHDRVPDLKDLD---PIGKAtL 342
Cdd:cd09245  324 kelEDLKSPSGVASKAKLKKSWKEKredrkvekgagveeelrtLEMLLKKYKKMNDTVSFQPVPPSSELQssmPSGRE-A 402

                        330
                 ....*....|.
gi 755531729 343 VKPTPVNVPVS 353
Cdd:cd09245  403 HTAKPYTPPPS 413
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 823-877 2.22e-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: 45.55  E-value: 2.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755531729   823 QMPMPmGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPF-PQPPQQSYYPQQ 877
Cdd:smart00818  73 LMPVP-GQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMqPQPPVHPIPPLP 127
YppG COG5894
Spore coat protein YppG [Cell cycle control, cell division, chromosome partitioning];
833-871 1.39e-04

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


Pssm-ID: 444596 [Multi-domain]  Cd Length: 112  Bit Score: 42.15  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755531729 833 YAYGQYNMPYP-PVYHQSPGQAPYPGPQQPTYPFPQPPQQ 871
Cdd:COG5894   22 QPYGPYQNQHQqPYYQQTNTQQPFPPPSPTPYPSPKPLQT 61
RCR pfam12273
Chitin synthesis regulation, resistance to Congo red; RCR proteins are ER membrane proteins ...
 829-877 7.32e-04

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: 40.09  E-value: 7.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755531729  829 GYNPYaYGQ---YNMPYPPVYHQSPGQAPYPGPQQPTY-----------------PFPQPPQQSYYPQQ 877
Cdd:pfam12273  30 GLQPI-YGTgwmGGGPPPPSYGQSQQDPQPTGTYVPTYtpndgyydqqgnfhnagSGLQPPQQAYQPPT 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 377-656 2.02e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   377 QRKADLVNRSIAQMREATTLANGVLASLNlpAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRnREIL 456
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLR--KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   457 EESLRLLDEEEATDNDLRAKFKDRWQRTpsNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELN 536
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQL--KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531729   537 AAIPSANpaktMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRIYGGL 616
Cdd:TIGR02168  845 EQIEELS----EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 755531729   617 TSKVQESLKKQEGLlkniqvshqefsKMKQSNNEANLREE 656
Cdd:TIGR02168  921 REKLAQLELRLEGL------------EVRIDNLQERLSEE 948
SGP pfam17228
Sulphur globule protein; Sulphur globules are membrane-bounded intracellular globules, used by ...
 829-872 2.82e-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: 2.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755531729  829 GYNPYAYG---------QYNMPYPPVYHQSPGQAPYPGPQQPTypfPQPPQQS 872
Cdd:pfam17228  47 GYGDYGYGnpygygypyGYGAPYGAPYGYGPYGAPYGAPVAPA---PAAPAEA 96
 
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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