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Conserved domains on  [gi|569007066|ref|XP_006527061|]
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erlin-1 isoform X1 [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 ...
 18-310 0e+00

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: 574.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  18 AILLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNML 97
Cdd:cd03406    1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  98 APYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMAPGLTIQAVRVTKPKI 177
Cdd:cd03406   81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 178 PEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREK 257
Cdd:cd03406  161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569007066 258 AKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPSMFVDS 310
Cdd:cd03406  241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 18-310 0e+00

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: 574.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  18 AILLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNML 97
Cdd:cd03406    1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  98 APYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMAPGLTIQAVRVTKPKI 177
Cdd:cd03406   81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 178 PEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREK 257
Cdd:cd03406  161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569007066 258 AKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPSMFVDS 310
Cdd:cd03406  241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 23-189 1.68e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 113.52  E-value: 1.68e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066    23 ASIHKIEEGHLAVYYRGGALLTsPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAv 102
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   103 fDIVRNYTADYdkTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNtmAPGLTIQAVRVTKPKIPEAIR 182
Cdd:smart00244  79 -AVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAE--AWGIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 569007066   183 RNFELME 189
Cdd:smart00244 154 EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 27-209 5.99e-28

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: 107.41  E-value: 5.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   27 KIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNmLAPYAVFDIV 106
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYR-VNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  107 RNY-TADYDKTLIFNKIHHELNQFCSAHTLQEVYIElFDQIDENLKQALQKDLNTMapGLTIQAVRVTKPKIPEAIRRNf 185
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAKY--GVEIIDVQITDIDPPPEIAEA- 155

                         170       180
                  ....*....|....*....|....
gi 569007066  186 elMEAEKTKLLIAAQKQKVVEKEA 209
Cdd:pfam01145 156 --IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 8-316 4.56e-21

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 91.44  E-value: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   8 LLVAAVVGLVAILLYASIHKIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIY 87
Cdd:COG0330    4 ILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  88 IDrievvnMLAPYAVFDIVRNY--TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMapGL 165
Cdd:COG0330   83 VD------AVVQYRITDPAKFLynVENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 166 TIQAVRVTKPKIPEAIRRNFE-LMEAE----KTKLLIAAQKQKVVEKeAETERKRAVIEAEKIAQVAKIRfqqkvmeket 240
Cdd:COG0330  154 EVVDVEIKDIDPPEEVQDAMEdRMKAErereAAILEAEGYREAAIIR-AEGEAQRAIIEAEAYREAQILR---------- 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007066 241 ekriSEIEDAAFLAREKAKADAEYYAAHKYatsnkhkltpeyleLKKYQAIASNSkiyfgSNIPSMFVDSSCALKY 316
Cdd:COG0330  223 ----AEGEAEAFRIVAEAYSAAPFVLFYRS--------------LEALEEVLSPN-----SKVIVLPPDGNGFLKY 275
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 186-281 2.13e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 186 ELMEAEKTKLLIAAQKQKVVE--KEAETERKRAVIEAEKIAQVAKIRF--QQKVMEK-----ETEKRISEIEDAAFLARE 256
Cdd:PRK09510 102 RLKQLEKERLAAQEQKKQAEEaaKQAALKQKQAEEAAAKAAAAAKAKAeaEAKRAAAaakkaAAEAKKKAEAEAAKKAAA 181

                         90       100
                 ....*....|....*....|....*
gi 569007066 257 KAKADAEYYAAHKYATSNKHKLTPE 281
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAE 206
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 18-310 0e+00

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: 574.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  18 AILLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNML 97
Cdd:cd03406    1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  98 APYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMAPGLTIQAVRVTKPKI 177
Cdd:cd03406   81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 178 PEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREK 257
Cdd:cd03406  161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569007066 258 AKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPSMFVDS 310
Cdd:cd03406  241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 23-189 1.68e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 113.52  E-value: 1.68e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066    23 ASIHKIEEGHLAVYYRGGALLTsPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAv 102
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   103 fDIVRNYTADYdkTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNtmAPGLTIQAVRVTKPKIPEAIR 182
Cdd:smart00244  79 -AVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAE--AWGIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 569007066   183 RNFELME 189
Cdd:smart00244 154 EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 27-209 5.99e-28

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: 107.41  E-value: 5.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   27 KIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNmLAPYAVFDIV 106
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYR-VNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  107 RNY-TADYDKTLIFNKIHHELNQFCSAHTLQEVYIElFDQIDENLKQALQKDLNTMapGLTIQAVRVTKPKIPEAIRRNf 185
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAKY--GVEIIDVQITDIDPPPEIAEA- 155

                         170       180
                  ....*....|....*....|....
gi 569007066  186 elMEAEKTKLLIAAQKQKVVEKEA 209
Cdd:pfam01145 156 --IEAKQTAEQEAEAEIARAEAEA 177
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 67-179 3.16e-22

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: 90.12  E-value: 3.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  67 TLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVyIELFDQI 146
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 569007066 147 DENLKQALQKDLNTMapGLTIQAVRVTKPKIPE 179
Cdd:cd02106   80 AKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 8-316 4.56e-21

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 91.44  E-value: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   8 LLVAAVVGLVAILLYASIHKIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIY 87
Cdd:COG0330    4 ILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  88 IDrievvnMLAPYAVFDIVRNY--TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMapGL 165
Cdd:COG0330   83 VD------AVVQYRITDPAKFLynVENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 166 TIQAVRVTKPKIPEAIRRNFE-LMEAE----KTKLLIAAQKQKVVEKeAETERKRAVIEAEKIAQVAKIRfqqkvmeket 240
Cdd:COG0330  154 EVVDVEIKDIDPPEEVQDAMEdRMKAErereAAILEAEGYREAAIIR-AEGEAQRAIIEAEAYREAQILR---------- 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569007066 241 ekriSEIEDAAFLAREKAKADAEYYAAHKYatsnkhkltpeyleLKKYQAIASNSkiyfgSNIPSMFVDSSCALKY 316
Cdd:COG0330  223 ----AEGEAEAFRIVAEAYSAAPFVLFYRS--------------LEALEEVLSPN-----SKVIVLPPDGNGFLKY 275
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 25-225 2.23e-15

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: 73.70  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  25 IHKIEEGHLAV-YYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKnVPCGTSGGVMIYIDrIEVVNMLAPYAVF 103
Cdd:cd03401    1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTVNID-LSVLYRPDPEKLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 104 DIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELfDQIDENLKQALQKDLNtmAPGLTIQAVRVTKPKIPEAIRR 183
Cdd:cd03401   79 ELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKR-EEVSAEIREALTERLA--PFGIIVDDVLITNIDFPDEYEK 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 569007066 184 NFE-LMEAEktkllIAAQKQKVVEKEAETERKRAVIEAEKIAQ 225
Cdd:cd03401  156 AIEaKQVAE-----QEAERAKFELEKAEQEAERKVIEAEGEAE 193
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 11-241 1.86e-07

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 51.74  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  11 AAVVGLVAILLYASIHKIEEGHLAVYYRGGALlTSPSGPGYHIMLPFIttFRSVQTTlQTDEVKNVPCGTSG---GVMIY 87
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFP--IEVVEKV-NVTQVRSVEIGFRVpeeSLMLT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  88 IDR-IEVVNMLAPYAVFDIVrNY---TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMAP 163
Cdd:cd03404   77 GDEnIVDVDFVVQYRISDPV-AYlfnVRDPEETLR-QAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 164 GLTIQAVRVTKPKIPEAIRRNFElmEAektkllIAAQ--KQKVVeKEAETERK----RAVIEAEKIAQVAKIRFQQKVME 237
Cdd:cd03404  155 GIEIVQVQLQDADPPEEVQDAFD--DV------NAARqdKERLI-NEAQAYANevipRARGEAARIIQEAEAYKAEVVAR 225


                 ....
gi 569007066 238 KETE 241
Cdd:cd03404  226 AEGD 229
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 24-266 3.98e-06

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 47.48  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  24 SIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYID-----RIEvvnmla 98
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDsyarwRIT------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  99 pyavfDIVRNYTA----DYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNTMapGLTIQAVRVTK 174
Cdd:cd03405   75 -----DPLRFYQSvggeEGAESRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 175 PKIPEAIRRN-FELMEAEKTKllIAAQ-----KQKVVEKEAETERKRAVIEAEKIAQVAKIRfqqkvmeKETEKRISEIE 248
Cdd:cd03405  148 IDLPEEVSESvYERMRAERER--IAAEyraegEEEAEKIRAEADRERTVILAEAYREAEEIR-------GEGDAEAARIY 218

                        250
                 ....*....|....*...
gi 569007066 249 DAAFlarekaKADAEYYA 266
Cdd:cd03405  219 AEAY------GKDPEFYS 230
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 168-263 3.46e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  168 QAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAEtERKRAVIEAEKiaqvakirfQQKVMEKETEKRisei 247
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEER---------KRKLLEKEMEER---- 525

                          90
                  ....*....|....*.
gi 569007066  248 EDAAFLAREKAKADAE 263
Cdd:pfam17380 526 QKAIYEEERRREAEEE 541
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
189-267 4.73e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.78  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 189 EAEKTKLLIAAQKQKVVEKEAETERK--RAVIEAEKIAQVAKIRFQQKV------MEKETEKRISEIEDAAFLAREKA-- 258
Cdd:COG2268  231 EREIETARIAEAEAELAKKKAEERREaeTARAEAEAAYEIAEANAEREVqrqleiAEREREIELQEKEAEREEAELEAdv 310

                         90
                 ....*....|.
gi 569007066 259 --KADAEYYAA 267
Cdd:COG2268  311 rkPAEAEKQAA 321
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 186-281 2.13e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 186 ELMEAEKTKLLIAAQKQKVVE--KEAETERKRAVIEAEKIAQVAKIRF--QQKVMEK-----ETEKRISEIEDAAFLARE 256
Cdd:PRK09510 102 RLKQLEKERLAAQEQKKQAEEaaKQAALKQKQAEEAAAKAAAAAKAKAeaEAKRAAAaakkaAAEAKKKAEAEAAKKAAA 181

                         90       100
                 ....*....|....*....|....*
gi 569007066 257 KAKADAEYYAAHKYATSNKHKLTPE 281
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKKKAEAE 206
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 190-271 4.24e-03

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 36.26  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066  190 AEKTKLLiaAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQkvMEKETEKRISEiEDAAFLAREKAKADAEYYAAHK 269
Cdd:pfam16999  11 AEREAAL--DQQIEAARKEAEREVEAAEAEAARILREAEAKAKA--LQAEYRQELAA-ETARIREEARARAEAEAQAVRT 85


                  ..
gi 569007066  270 YA 271
Cdd:pfam16999  86 RA 87
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 189-277 7.67e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 37.86  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 189 EAEKTKLLIAAQKQKvveKEAETERKRAVIEAEKIAQVAKIR----FQQKVMEKETEKRISEIEDAAFLAREKAKADAEY 264
Cdd:PRK09510 164 AAEAKKKAEAEAAKK---AAAEAKKKAEAEAAAKAAAEAKKKaeaeAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240

                         90
                 ....*....|...
gi 569007066 265 YAAHKYATSNKHK 277
Cdd:PRK09510 241 AAAAKAAEKAAAA 253
PTZ00491 PTZ00491
major vault protein; Provisional
 189-263 9.28e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 38.07  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066 189 EAEKTKLL--------IAAQKQKVVEKEAETERKRavIEAEKIAQVAKIRFQQKVMEKETE------KRISEIEDA---A 251
Cdd:PTZ00491 695 EEQRTKLLelqaesaaVESSGQSRAEALAEAEARL--IEAEAEVEQAELRAKALRIEAEAEleklrkRQELELEYEqaqN 772

                         90
                 ....*....|..
gi 569007066 252 FLAREKAKADAE 263
Cdd:PTZ00491 773 ELEIAKAKELAD 784
PRK11029 PRK11029
protease modulator HflC;
7-70 9.74e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 37.41  E-value: 9.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007066   7 RLLVAAVVGLVAILLYASIHKIEEGHLAVYYRGGALLTSPSG------PGYHIMLPFITTFRSVQTTLQT 70
Cdd:PRK11029   2 RKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyaPGLHFKIPFIETVKMLDARIQT 71
 
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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