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Conserved domains on  [gi|1868070931|ref|XP_035315735|]
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erlin-1 isoform X2 [Cricetulus griseus]

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 ...
 25-275 2.90e-180

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: 498.36  E-value: 2.90e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  25 IHRIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFD 104
Cdd:cd03406     8 IHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRLDKESVYD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 105 IVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNVMAPGLTIQAVRVTKPKIPEAIRRN 184
Cdd:cd03406    88 TVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKIPEAIRRN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 185 FELMEAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEY 264
Cdd:cd03406   168 YEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADAEY 247

                         250
                  ....*....|.
gi 1868070931 265 YAAHKYATSNK 275
Cdd:cd03406   248 YRALREAEANK 258
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 25-275 2.90e-180

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: 498.36  E-value: 2.90e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  25 IHRIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFD 104
Cdd:cd03406     8 IHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRLDKESVYD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 105 IVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNVMAPGLTIQAVRVTKPKIPEAIRRN 184
Cdd:cd03406    88 TVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKIPEAIRRN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 185 FELMEAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEY 264
Cdd:cd03406   168 YEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADAEY 247

                         250
                  ....*....|.
gi 1868070931 265 YAAHKYATSNK 275
Cdd:cd03406   248 YRALREAEANK 258
PHB smart00244
prohibitin homologues; prohibitin homologues
 25-189 5.28e-29

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 108.52  E-value: 5.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931   25 IHRIEEGHLAVYYRGGALLTsPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAvfD 104
Cdd:smart00244   3 IKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR--A 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  105 IVRNYTADYdkTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRRN 184
Cdd:smart00244  80 VYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAE--AWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 1868070931  185 FELME 189
Cdd:smart00244 156 MEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 27-209 6.80e-27

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: 103.56  E-value: 6.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  27 RIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNmLAPYAVFDIV 106
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYR-VNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 107 RNY-TADYDKTLIFNKIHHELNQFCSAHTLQEVYIElFDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRRNf 185
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELA--KYGVEIIDVQITDIDPPPEIAEA- 155

                         170       180
                  ....*....|....*....|....
gi 1868070931 186 elMEAEKTKLLIAAQKQKVVEKEA 209
Cdd:pfam01145 156 --IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 28-270 6.59e-15

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 73.34  E-value: 6.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  28 IEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDrievvnMLAPYAVFDIVR 107
Cdd:COG0330    24 VPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVD------AVVQYRITDPAK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 108 NY--TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRRNF 185
Cdd:COG0330    97 FLynVENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALD--PYGIEVVDVEIKDIDPPEEVQDAM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 186 E-LMEAE----KTKLLIAAQKQKVVEKeAETERKRAVIEAEKIAQVAKIRfqqkvmeketekriSEIEDAAFLAREKAKA 260
Cdd:COG0330   174 EdRMKAErereAAILEAEGYREAAIIR-AEGEAQRAIIEAEAYREAQILR--------------AEGEAEAFRIVAEAYS 238

                         250
                  ....*....|
gi 1868070931 261 DAEYYAAHKY 270
Cdd:COG0330   239 AAPFVLFYRS 248
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 186-278 8.74e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 186 ELMEAEKTKLLIAAQKQKVVE--KEAETERKRAVIEAEKIAQVAKIRF--QQKVMEK-----ETEKRISEIEDAAFLARE 256
Cdd:PRK09510  102 RLKQLEKERLAAQEQKKQAEEaaKQAALKQKQAEEAAAKAAAAAKAKAeaEAKRAAAaakkaAAEAKKKAEAEAAKKAAA 181

                          90       100
                  ....*....|....*....|..
gi 1868070931 257 KAKADAEYYAAHKYATSNKVTA 278
Cdd:PRK09510  182 EAKKKAEAEAAAKAAAEAKKKA 203
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 25-275 2.90e-180

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: 498.36  E-value: 2.90e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  25 IHRIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFD 104
Cdd:cd03406     8 IHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRLDKESVYD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 105 IVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNVMAPGLTIQAVRVTKPKIPEAIRRN 184
Cdd:cd03406    88 TVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKIPEAIRRN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 185 FELMEAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEY 264
Cdd:cd03406   168 YEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADAEY 247

                         250
                  ....*....|.
gi 1868070931 265 YAAHKYATSNK 275
Cdd:cd03406   248 YRALREAEANK 258
PHB smart00244
prohibitin homologues; prohibitin homologues
 25-189 5.28e-29

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 108.52  E-value: 5.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931   25 IHRIEEGHLAVYYRGGALLTsPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAvfD 104
Cdd:smart00244   3 IKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR--A 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  105 IVRNYTADYdkTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRRN 184
Cdd:smart00244  80 VYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAE--AWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 1868070931  185 FELME 189
Cdd:smart00244 156 MEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 27-209 6.80e-27

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: 103.56  E-value: 6.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  27 RIEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNmLAPYAVFDIV 106
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYR-VNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 107 RNY-TADYDKTLIFNKIHHELNQFCSAHTLQEVYIElFDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRRNf 185
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELA--KYGVEIIDVQITDIDPPPEIAEA- 155

                         170       180
                  ....*....|....*....|....
gi 1868070931 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 4.16e-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: 88.96  E-value: 4.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  67 TLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVyIELFDQI 146
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1868070931 147 DENLKQALQKDLNVMapGLTIQAVRVTKPKIPE 179
Cdd:cd02106    80 AKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 25-225 5.46e-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: 71.78  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  25 IHRIEEGHLAV-YYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKnVPCGTSGGVMIYIDrIEVVNMLAPYAVF 103
Cdd:cd03401     1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTVNID-LSVLYRPDPEKLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 104 DIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELfDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRR 183
Cdd:cd03401    79 ELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKR-EEVSAEIREALTERLA--PFGIIVDDVLITNIDFPDEYEK 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1868070931 184 NFE-LMEAEktkllIAAQKQKVVEKEAETERKRAVIEAEKIAQ 225
Cdd:cd03401   156 AIEaKQVAE-----QEAERAKFELEKAEQEAERKVIEAEGEAE 193
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 28-270 6.59e-15

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 73.34  E-value: 6.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  28 IEEGHLAVYYRGGALlTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDrievvnMLAPYAVFDIVR 107
Cdd:COG0330    24 VPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVD------AVVQYRITDPAK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 108 NY--TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNvmAPGLTIQAVRVTKPKIPEAIRRNF 185
Cdd:COG0330    97 FLynVENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALD--PYGIEVVDVEIKDIDPPEEVQDAM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 186 E-LMEAE----KTKLLIAAQKQKVVEKeAETERKRAVIEAEKIAQVAKIRfqqkvmeketekriSEIEDAAFLAREKAKA 260
Cdd:COG0330   174 EdRMKAErereAAILEAEGYREAAIIR-AEGEAQRAIIEAEAYREAQILR--------------AEGEAEAFRIVAEAYS 238

                         250
                  ....*....|
gi 1868070931 261 DAEYYAAHKY 270
Cdd:COG0330   239 AAPFVLFYRS 248
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 28-266 6.91e-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: 46.33  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  28 IEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYID-----RIEvvnmlapyav 102
Cdd:cd03405     5 VDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDsyarwRIT---------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 103 fDIVRNYTA----DYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNVMapGLTIQAVRVTKPKIP 178
Cdd:cd03405    75 -DPLRFYQSvggeEGAESRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKRIDLP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 179 EAIRRN-FELMEAEKTKllIAAQ-----KQKVVEKEAETERKRAVIEAEKIAQVAKIRfqqkvmeKETEKRISEIEDAAF 252
Cdd:cd03405   152 EEVSESvYERMRAERER--IAAEyraegEEEAEKIRAEADRERTVILAEAYREAEEIR-------GEGDAEAARIYAEAY 222

                         250
                  ....*....|....
gi 1868070931 253 larekaKADAEYYA 266
Cdd:cd03405   223 ------GKDPEFYS 230
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 168-263 2.25e-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: 42.80  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 168 QAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAEtERKRAVIEAEKiaqvakirfQQKVMEKETEKRisei 247
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEER---------KRKLLEKEMEER---- 525

                          90
                  ....*....|....*.
gi 1868070931 248 EDAAFLAREKAKADAE 263
Cdd:pfam17380 526 QKAIYEEERRREAEEE 541
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
189-267 4.35e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 189 EAEKTKLLIAAQKQKVVEKEAETERK--RAVIEAEKIAQVAKIRFQQKV------MEKETEKRISEIEDAAFLAREKA-- 258
Cdd:COG2268   231 EREIETARIAEAEAELAKKKAEERREaeTARAEAEAAYEIAEANAEREVqrqleiAEREREIELQEKEAEREEAELEAdv 310

                          90
                  ....*....|.
gi 1868070931 259 --KADAEYYAA 267
Cdd:COG2268   311 rkPAEAEKQAA 321
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 25-241 7.27e-04

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: 40.19  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931  25 IHRIEEGHLAVYYRGGALlTSPSGPGYHIMLPFIttFRSVQTTlQTDEVKNVPCGTSG---GVMIYIDR-IEVVNMLAPY 100
Cdd:cd03404    15 FYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFP--IEVVEKV-NVTQVRSVEIGFRVpeeSLMLTGDEnIVDVDFVVQY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 101 AVFDIVrNY---TADYDKTLIfNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNVMAPGLTIQAVRVTKPKI 177
Cdd:cd03404    91 RISDPV-AYlfnVRDPEETLR-QAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDADP 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868070931 178 PEAIRRNFElmEAEKtklliAAQKQKVVEKEAETERK----RAVIEAEKIAQVAKIRFQQKVMEKETE 241
Cdd:cd03404   169 PEEVQDAFD--DVNA-----ARQDKERLINEAQAYANevipRARGEAARIIQEAEAYKAEVVARAEGD 229
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 186-278 8.74e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 186 ELMEAEKTKLLIAAQKQKVVE--KEAETERKRAVIEAEKIAQVAKIRF--QQKVMEK-----ETEKRISEIEDAAFLARE 256
Cdd:PRK09510  102 RLKQLEKERLAAQEQKKQAEEaaKQAALKQKQAEEAAAKAAAAAKAKAeaEAKRAAAaakkaAAEAKKKAEAEAAKKAAA 181

                          90       100
                  ....*....|....*....|..
gi 1868070931 257 KAKADAEYYAAHKYATSNKVTA 278
Cdd:PRK09510  182 EAKKKAEAEAAAKAAAEAKKKA 203
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 189-272 2.71e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 189 EAEKTKLLIAAQKQKvveKEAETERKRAVIEAEKIAQVAKIR----FQQKVMEKETEKRISEIEDAAFLAREKAKADAEY 264
Cdd:PRK09510  164 AAEAKKKAEAEAAKK---AAAEAKKKAEAEAAAKAAAEAKKKaeaeAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240


                  ....*...
gi 1868070931 265 YAAHKYAT 272
Cdd:PRK09510  241 AAAAKAAE 248
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 190-271 2.92e-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: 36.65  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 190 AEKTKLLiaAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQkvMEKETEKRISEiEDAAFLAREKAKADAEYYAAHK 269
Cdd:pfam16999  11 AEREAAL--DQQIEAARKEAEREVEAAEAEAARILREAEAKAKA--LQAEYRQELAA-ETARIREEARARAEAEAQAVRT 85


                  ..
gi 1868070931 270 YA 271
Cdd:pfam16999  86 RA 87
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 189-283 7.52e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 189 EAEKTKLLIAAQKQKVVEKEAETERKRAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAH 268
Cdd:COG3883   137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216

                          90
                  ....*....|....*
gi 1868070931 269 KYATSNKVTALYATS 283
Cdd:COG3883   217 AAAAAAAAAAAAAAA 231
PTZ00491 PTZ00491
major vault protein; Provisional
 189-263 8.07e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 37.69  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868070931 189 EAEKTKLL--------IAAQKQKVVEKEAETERKRavIEAEKIAQVAKIRFQQKVMEKETE------KRISEIEDA---A 251
Cdd:PTZ00491  695 EEQRTKLLelqaesaaVESSGQSRAEALAEAEARL--IEAEAEVEQAELRAKALRIEAEAEleklrkRQELELEYEqaqN 772

                          90
                  ....*....|..
gi 1868070931 252 FLAREKAKADAE 263
Cdd:PTZ00491  773 ELEIAKAKELAD 784
 
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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