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Conserved domains on  [gi|2220174419|ref|NP_001391045|]
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erlin-2 isoform 5 [Mus musculus]

Protein Classification

erlin( domain architecture ID 10130465)

erlin family protein similar to Homo sapiens erlin-1 and erlin-2, which forms the ERLIN1/ERLIN2 complex that mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 59-288 2.40e-167

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


:

Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 466.77  E-value: 2.40e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  59 SGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTS 138
Cdd:cd03406    64 SGGVMIYFDRIEVVNRLDKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 139 MAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKET 218
Cdd:cd03406   144 MAPGLEIIAVRVTKPKIPEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEA 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 219 EKKISEIEDAAFLAREKAKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 288
Cdd:cd03406   224 EKKISEIEDEMHLAREKARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 59-288 2.40e-167

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 466.77  E-value: 2.40e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  59 SGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTS 138
Cdd:cd03406    64 SGGVMIYFDRIEVVNRLDKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 139 MAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKET 218
Cdd:cd03406   144 MAPGLEIIAVRVTKPKIPEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEA 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 219 EKKISEIEDAAFLAREKAKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 288
Cdd:cd03406   224 EKKISEIEDEMHLAREKARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 48-167 6.26e-12

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 62.68  E-value: 6.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419   48 SGNVITtslsnSGGVMIYFDRieVVNFLVPNAVYDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDEN 127
Cdd:smart00244  52 PQETIT-----KDNVKVSVDA--VVYYRVLDPLRAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISEN 122

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2220174419  128 LKLALQQDLTSMapGLVIQAVRVTKPNIPEAIRRNYELME 167
Cdd:smart00244 123 IREELNEAAEAW--GIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 59-187 2.84e-10

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 58.49  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  59 SGGVMIYFDRieVVNFLV-PNAVYDIVKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDL 136
Cdd:pfam01145  55 KDGVPVNVDV--TVIYRVnPDDPPKLVQNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEEL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2220174419 137 tsMAPGLVIQAVRVTKPNIPEAIRRNyelMESEKTKLLIAAQKQKVVEKEA 187
Cdd:pfam01145 132 --AKYGVEIIDVQITDIDPPPEIAEA---IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 71-288 3.42e-07

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 50.61  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  71 VVNFLVPNAvYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRV 150
Cdd:COG0330    86 VVQYRITDP-AKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GIEVVDVEI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 151 TKPNIPEAIRRNYElmesektKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEItygqkvmEKETEKkiseieDAAF 230
Cdd:COG0330   161 KDIDPPEEVQDAME-------DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-------EAEAYR------EAQI 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2220174419 231 LareKAKADAEcyTALKIAEAnkLKLTPEYLQLM---KYKAIAS-NSKIYF----GKDIPNMFMDS 288
Cdd:COG0330   221 L---RAEGEAE--AFRIVAEA--YSAAPFVLFYRsleALEEVLSpNSKVIVlppdGNGFLKYLLKS 279
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 176-259 3.61e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 176 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTALKIAEANKLK 255
Cdd:PRK09510  123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                  ....
gi 2220174419 256 LTPE 259
Cdd:PRK09510  203 AEAE 206
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-253 5.10e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.29  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 167 ESEKTKLLIAAQKQKVVE---KEAETERK-KALIEAEKVAQVAEITYGQKVMEK-ETEKKISEIEDAAFLAREKAKADAE 241
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEeaaKQAEEEAKaKAAAEAKKKAEEAKKKAEAEAKAKaEAEAKAKAEEAKAKAEAAKAKAAAE 208

                          90
                  ....*....|..
gi 2220174419 242 cytALKIAEANK 253
Cdd:TIGR02794 209 ---AAAKAEAEA 217
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 59-288 2.40e-167

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 466.77  E-value: 2.40e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  59 SGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTS 138
Cdd:cd03406    64 SGGVMIYFDRIEVVNRLDKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNK 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 139 MAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKET 218
Cdd:cd03406   144 MAPGLEIIAVRVTKPKIPEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEA 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 219 EKKISEIEDAAFLAREKAKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 288
Cdd:cd03406   224 EKKISEIEDEMHLAREKARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 59-157 8.25e-21

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 85.49  E-value: 8.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  59 SGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVyIELFDQIDENLKLALQQDLTS 138
Cdd:cd02106    15 ADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEIAKAVKEDLEEDLEN 93

                          90
                  ....*....|....*....
gi 2220174419 139 MapGLVIQAVRVTKPNIPE 157
Cdd:cd02106    94 F--GVVISDVDITSIEPPD 110
PHB smart00244
prohibitin homologues; prohibitin homologues
 48-167 6.26e-12

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 62.68  E-value: 6.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419   48 SGNVITtslsnSGGVMIYFDRieVVNFLVPNAVYDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDEN 127
Cdd:smart00244  52 PQETIT-----KDNVKVSVDA--VVYYRVLDPLRAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISEN 122

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2220174419  128 LKLALQQDLTSMapGLVIQAVRVTKPNIPEAIRRNYELME 167
Cdd:smart00244 123 IREELNEAAEAW--GIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 59-187 2.84e-10

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 58.49  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  59 SGGVMIYFDRieVVNFLV-PNAVYDIVKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDL 136
Cdd:pfam01145  55 KDGVPVNVDV--TVIYRVnPDDPPKLVQNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEEL 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2220174419 137 tsMAPGLVIQAVRVTKPNIPEAIRRNyelMESEKTKLLIAAQKQKVVEKEA 187
Cdd:pfam01145 132 --AKYGVEIIDVQITDIDPPPEIAEA---IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 71-288 3.42e-07

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 50.61  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  71 VVNFLVPNAvYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRV 150
Cdd:COG0330    86 VVQYRITDP-AKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GIEVVDVEI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 151 TKPNIPEAIRRNYElmesektKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEItygqkvmEKETEKkiseieDAAF 230
Cdd:COG0330   161 KDIDPPEEVQDAME-------DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-------EAEAYR------EAQI 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2220174419 231 LareKAKADAEcyTALKIAEAnkLKLTPEYLQLM---KYKAIAS-NSKIYF----GKDIPNMFMDS 288
Cdd:COG0330   221 L---RAEGEAE--AFRIVAEA--YSAAPFVLFYRsleALEEVLSpNSKVIVlppdGNGFLKYLLKS 279
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 176-259 3.61e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 176 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTALKIAEANKLK 255
Cdd:PRK09510  123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                  ....
gi 2220174419 256 LTPE 259
Cdd:PRK09510  203 AEAE 206
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 72-203 4.56e-04

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 40.57  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419  72 VNF-LVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYI---ELFDQIDENLKLALQQDltsmapGLVIQA 147
Cdd:cd03401    68 VLYrPDPEKLPELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTkreEVSAEIREALTERLAPF------GIIVDD 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2220174419 148 VRVTKPNIPEAIRRNYElmesEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQ 203
Cdd:cd03401   142 VLITNIDFPDEYEKAIE----AKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAE 193
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
131-251 1.70e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 131 ALQQDLTSMapGLVIQAVRVT-------------KPNIPEAIR-RNYELMESEK-TKLLIAAQKQ--------------- 180
Cdd:COG2268   159 VAGTDLAKN--GLELESVAITdledennyldalgRRKIAEIIRdARIAEAEAEReTEIAIAQANReaeeaeleqereiet 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 181 -KVVEKEAETERKKAL---------IEAEKVAQVAEITYGQKV------MEKETEKKISEIEDAAFLAREKA----KADA 240
Cdd:COG2268   237 aRIAEAEAELAKKKAEerreaetarAEAEAAYEIAEANAEREVqrqleiAEREREIELQEKEAEREEAELEAdvrkPAEA 316

                         170
                  ....*....|.
gi 2220174419 241 ECYTALKIAEA 251
Cdd:COG2268   317 EKQAAEAEAEA 327
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
157-253 3.65e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.87  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 157 EAIRRNYELMESEKTKLLIAAQK--QKVVEKEAETERKKALIEAEKVAQVAE----ITYGQKVMEKETEKKISEIEDAAF 230
Cdd:COG3064    30 EAEQKAKEEAEEERLAELEAKRQaeEEAREAKAEAEQRAAELAAEAAKKLAEaekaAAEAEKKAAAEKAKAAKEAEAAAA 109

                          90       100
                  ....*....|....*....|...
gi 2220174419 231 LAREKAKADAEcytalKIAEANK 253
Cdd:COG3064   110 AEKAAAAAEKE-----KAEEAKR 127
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-253 5.10e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.29  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 167 ESEKTKLLIAAQKQKVVE---KEAETERK-KALIEAEKVAQVAEITYGQKVMEK-ETEKKISEIEDAAFLAREKAKADAE 241
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEeaaKQAEEEAKaKAAAEAKKKAEEAKKKAEAEAKAKaEAEAKAKAEEAKAKAEAAKAKAAAE 208

                          90
                  ....*....|..
gi 2220174419 242 cytALKIAEANK 253
Cdd:TIGR02794 209 ---AAAKAEAEA 217
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 167-251 9.19e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 37.48  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2220174419 167 ESEKTKLLIAAQKQKvvekeAETERKKALIEAEKVAQVAEityGQKVMEKETEKKiseiedAAFLAREKAKADAECYTAL 246
Cdd:PRK09510  164 AAEAKKKAEAEAAKK-----AAAEAKKKAEAEAAAKAAAE---AKKKAEAEAKKK------AAAEAKKKAAAEAKAAAAK 229


                  ....*
gi 2220174419 247 KIAEA 251
Cdd:PRK09510  230 AAAEA 234
 
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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