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Conserved domains on  [gi|154800489|ref|NP_001094096|]
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erlin-1 isoform a [Homo sapiens]

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 ...
 23-310 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: 567.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  23 ASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAV 102
Cdd:cd03406    6 FSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRLDKESV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 103 FDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIR 182
Cdd:cd03406   86 YDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKIPEAIR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 183 RNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADA 262
Cdd:cd03406  166 RNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 154800489 263 EYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDS 310
Cdd:cd03406  246 EYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 23-310 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: 567.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  23 ASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAV 102
Cdd:cd03406    6 FSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRLDKESV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 103 FDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIR 182
Cdd:cd03406   86 YDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKIPEAIR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 183 RNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADA 262
Cdd:cd03406  166 RNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 154800489 263 EYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDS 310
Cdd:cd03406  246 EYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 23-189 1.38e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 113.91  E-value: 1.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489    23 ASIHKIEEGHLAVYYRGGALLTsPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAv 102
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489   103 fDIVRNYTADYdkTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPEAIR 182
Cdd:smart00244  79 -AVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAE--AWGIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 154800489   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 8.02e-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: 107.02  E-value: 8.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489   27 KIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNmLAPYAVFDIV 106
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYR-VNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  107 RNY-TADYDKTLIFNKIHHELNQFCSAHTLQEVYIElFDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPEAIRRNf 185
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELA--KYGVEIIDVQITDIDPPPEIAEA- 155

                         170       180
                  ....*....|....*....|....
gi 154800489  186 elMEAEKTKLLIAAQKQKVVEKEA 209
Cdd:pfam01145 156 --IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 22-299 1.51e-16

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 78.73  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  22 YASIHKIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDrievvnMLAPYA 101
Cdd:COG0330   18 FSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVD------AVVQYR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 102 VFDIVRNY--TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPE 179
Cdd:COG0330   91 ITDPAKFLynVENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALD--PYGIEVVDVEIKDIDPPE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 180 AIRRNFE-LMEAEKTKllIAAqkqkvvEKEAETERKKAVIEAEKIAQVAKIRFQQkvmEKETEKRISEIEDAAFLAREKA 258
Cdd:COG0330  168 EVQDAMEdRMKAERER--EAA------ILEAEGYREAAIIRAEGEAQRAIIEAEA---YREAQILRAEGEAEAFRIVAEA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 154800489 259 KADAEYYAAHKYatsnkhkltpeyleLKKYQAIAS-NSKIYF 299
Cdd:COG0330  237 YSAAPFVLFYRS--------------LEALEEVLSpNSKVIV 264
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 198-281 3.74e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 198 AAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHK 277
Cdd:PRK09510 123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                 ....
gi 154800489 278 LTPE 281
Cdd:PRK09510 203 AEAE 206
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 23-310 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: 567.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  23 ASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAV 102
Cdd:cd03406    6 FSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRLDKESV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 103 FDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIR 182
Cdd:cd03406   86 YDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKIPEAIR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 183 RNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADA 262
Cdd:cd03406  166 RNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 154800489 263 EYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDS 310
Cdd:cd03406  246 EYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 23-189 1.38e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 113.91  E-value: 1.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489    23 ASIHKIEEGHLAVYYRGGALLTsPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAv 102
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489   103 fDIVRNYTADYdkTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPEAIR 182
Cdd:smart00244  79 -AVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAE--AWGIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 154800489   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 8.02e-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: 107.02  E-value: 8.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489   27 KIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNmLAPYAVFDIV 106
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYR-VNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  107 RNY-TADYDKTLIFNKIHHELNQFCSAHTLQEVYIElFDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPEAIRRNf 185
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELA--KYGVEIIDVQITDIDPPPEIAEA- 155

                         170       180
                  ....*....|....*....|....
gi 154800489  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 5.17e-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: 89.35  E-value: 5.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  67 TLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVyIELFDQI 146
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154800489 147 DENLKQALQKDLNlmAPGLTIQAVRVTKPKIPE 179
Cdd:cd02106   80 AKAVKEDLEEDLE--NFGVVISDVDITSIEPPD 110
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 22-299 1.51e-16

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 78.73  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  22 YASIHKIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDrievvnMLAPYA 101
Cdd:COG0330   18 FSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVD------AVVQYR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 102 VFDIVRNY--TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPE 179
Cdd:COG0330   91 ITDPAKFLynVENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALD--PYGIEVVDVEIKDIDPPE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 180 AIRRNFE-LMEAEKTKllIAAqkqkvvEKEAETERKKAVIEAEKIAQVAKIRFQQkvmEKETEKRISEIEDAAFLAREKA 258
Cdd:COG0330  168 EVQDAMEdRMKAERER--EAA------ILEAEGYREAAIIRAEGEAQRAIIEAEA---YREAQILRAEGEAEAFRIVAEA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 154800489 259 KADAEYYAAHKYatsnkhkltpeyleLKKYQAIAS-NSKIYF 299
Cdd:COG0330  237 YSAAPFVLFYRS--------------LEALEEVLSpNSKVIV 264
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 25-225 7.87e-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: 72.16  E-value: 7.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  25 IHKIEEGHLAV-YYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKnVPCGTSGGVMIYIDrIEVVNMLAPYAVF 103
Cdd:cd03401    1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTVNID-LSVLYRPDPEKLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 104 DIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELfDQIDENLKQALQKDLNlmAPGLTIQAVRVTKPKIPEAIRR 183
Cdd:cd03401   79 ELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKR-EEVSAEIREALTERLA--PFGIIVDDVLITNIDFPDEYEK 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 154800489 184 NFE-LMEAEktkllIAAQKQKVVEKEAETERKKAVIEAEKIAQ 225
Cdd:cd03401  156 AIEaKQVAE-----QEAERAKFELEKAEQEAERKVIEAEGEAE 193
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 24-266 1.29e-05

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: 45.94  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  24 SIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYID-----RIEvvnmla 98
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDsyarwRIT------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  99 pyavfDIVRNYTA----DYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDL-NLmapGLTIQAVRVT 173
Cdd:cd03405   75 -----DPLRFYQSvggeEGAESRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAkEY---GIEVVDVRIK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 174 KPKIPEAIRRN-FELMEAEKTKllIAAQ-----KQKVVEKEAETERKKAVIEAEKIAQVAKIRfqqkvmeKETEKRISEI 247
Cdd:cd03405  147 RIDLPEEVSESvYERMRAERER--IAAEyraegEEEAEKIRAEADRERTVILAEAYREAEEIR-------GEGDAEAARI 217

                        250
                 ....*....|....*....
gi 154800489 248 EDAAFlarekaKADAEYYA 266
Cdd:cd03405  218 YAEAY------GKDPEFYS 230
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 24-241 5.81e-05

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: 44.04  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  24 SIHKIEEGHLAVYYRGGALlTSPSGPGYHIMLPFIttFRSVQTTlQTDEVKNVPCGTSG---GVMIYIDR-IEVVNMLAP 99
Cdd:cd03404   14 GFYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFP--IEVVEKV-NVTQVRSVEIGFRVpeeSLMLTGDEnIVDVDFVVQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 100 YAVFDIVrNY---TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPK 176
Cdd:cd03404   90 YRISDPV-AYlfnVRDPEETLR-QAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDAD 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154800489 177 IPEAIRRNFElmEAektkllIAAQ--KQKVVeKEAETERK----KAVIEAEKIAQVAKIRFQQKVMEKETE 241
Cdd:cd03404  168 PPEEVQDAFD--DV------NAARqdKERLI-NEAQAYANevipRARGEAARIIQEAEAYKAEVVARAEGD 229
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 198-281 3.74e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 198 AAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHK 277
Cdd:PRK09510 123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                 ....
gi 154800489 278 LTPE 281
Cdd:PRK09510 203 AEAE 206
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 168-263 9.22e-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: 41.26  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  168 QAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAEtERKKAVIEAEKiaqvakirfQQKVMEKETEKRisei 247
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEER---------KRKLLEKEMEER---- 525

                          90
                  ....*....|....*.
gi 154800489  248 EDAAFLAREKAKADAE 263
Cdd:pfam17380 526 QKAIYEEERRREAEEE 541
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 189-277 2.41e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.40  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 189 EAEKTKLLIAAQKQKVVE---KEAETERK-KAVIEAEKIAQVAKirfQQKVMEKETEKRISEIEDAAFLAREKAKADAEY 264
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAAeakKKAEAEAAaKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240

                         90
                 ....*....|...
gi 154800489 265 YAAHKYATSNKHK 277
Cdd:PRK09510 241 AAAAKAAEKAAAA 253
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
148-267 4.39e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 148 ENLKQALQKDLNLMapGLTIQAVRVT-------------KPKIPEAIR-RNFELMEAEK-TKLLIAAQKQ---------- 202
Cdd:COG2268  154 EKVQEVAGTDLAKN--GLELESVAITdledennyldalgRRKIAEIIRdARIAEAEAEReTEIAIAQANReaeeaeleqe 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489 203 ------KVVEKEAETERKKAviEAEKIAQVAKIRFQQKVMEKETEKR-----------------ISEIEDAAFLAREKA- 258
Cdd:COG2268  232 reietaRIAEAEAELAKKKA--EERREAETARAEAEAAYEIAEANAErevqrqleiaerereieLQEKEAEREEAELEAd 309

                        170
                 ....*....|..
gi 154800489 259 ---KADAEYYAA 267
Cdd:COG2268  310 vrkPAEAEKQAA 321
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 190-271 8.97e-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: 35.49  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154800489  190 AEKTKLLiaAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQkvMEKETEKRISEiEDAAFLAREKAKADAEYYAAHK 269
Cdd:pfam16999  11 AEREAAL--DQQIEAARKEAEREVEAAEAEAARILREAEAKAKA--LQAEYRQELAA-ETARIREEARARAEAEAQAVRT 85


                  ..
gi 154800489  270 YA 271
Cdd:pfam16999  86 RA 87
 
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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