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Conserved domains on  [gi|75271990|sp|Q9CAR7|]
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RecName: Full=Hypersensitive-induced response protein 2; Short=AtHIR2

Protein Classification

SPFH domain-containing protein( domain architecture ID 10130471)

uncharacterized stomatin, prohibitin, flotillin, HflK/C (SPFH) domain-containing protein similar to Streptococcus pneumoniae SPFH domain/Band 7 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 10-278 2.97e-155

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: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 433.55  E-value: 2.97e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  10 VDQSNVAIKETFGKFDEVLEPGCHCLPWClGSQVAGHLSLRVQQLDVRCETKTKDNVFVTVVASIQYRALAESAQDAFYK 89
Cdd:cd03407   2 VSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  90 LSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASR 169
Cdd:cd03407  81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 170 MREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVPGTSSKDVMDMVLVTQYFDTLKEI 249
Cdd:cd03407 161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEV 240

                       250       260
                ....*....|....*....|....*....
gi 75271990 250 GASSKSNSVFIPHGPGAVRDIASQIRDGL 278
Cdd:cd03407 241 GKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
 
Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 10-278 2.97e-155

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: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 433.55  E-value: 2.97e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  10 VDQSNVAIKETFGKFDEVLEPGCHCLPWClGSQVAGHLSLRVQQLDVRCETKTKDNVFVTVVASIQYRALAESAQDAFYK 89
Cdd:cd03407   2 VSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  90 LSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASR 169
Cdd:cd03407  81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 170 MREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVPGTSSKDVMDMVLVTQYFDTLKEI 249
Cdd:cd03407 161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEV 240

                       250       260
                ....*....|....*....|....*....
gi 75271990 250 GASSKSNSVFIPHGPGAVRDIASQIRDGL 278
Cdd:cd03407 241 GKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-273 4.47e-36

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 129.96  E-value: 4.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990   4 ALGCIQVDQSNVAIKETFGKFDEVLEPGCH-CLPWClgsQVAGHLSLRVQQLDVR-CETKTKDNVFVTVVASIQYRAlaE 81
Cdd:COG0330  18 FSSVYIVPQGERGVVLRFGKYVRTLEPGLHfKIPFI---DRVRKVDVREQVLDVPpQEVLTKDNNIVDVDAVVQYRI--T 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  82 SAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRA 160
Cdd:COG0330  93 DPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 161 MNEINAASRMREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVpgtsskDVMDMVLVT 240
Cdd:COG0330 173 MEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAY------SAAPFVLFY 246

                       250       260       270
                ....*....|....*....|....*....|....
gi 75271990 241 QYFDTLKEIgASSKSNSVFIPH-GPGAVRDIASQ 273
Cdd:COG0330 247 RSLEALEEV-LSPNSKVIVLPPdGNGFLKYLLKS 279
PHB smart00244
prohibitin homologues; prohibitin homologues
 10-165 7.01e-25

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 97.35  E-value: 7.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990     10 VDQSNVAIKETFGKFDEVLEPGCHCL-PWClgsQVAGHLSLRVQQLDVRC-ETKTKDNVFVTVVASIQYRaLAESAQDAF 87
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLiPFI---DDVKKVDLRAQTDDVPPqETITKDNVKVSVDAVVYYR-VLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75271990     88 YKLSNTRNQIQAYVFDVIRASVPKLDLDSTFE-QKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEIN 165
Cdd:smart00244  82 RVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 8-193 1.29e-22

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: 92.00  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990     8 IQVDQSNVAIKETFGKFDEVLEPGCHCLpWCLGSQVAgHLSLRVQQLDV-RCETKTKDNVFVTVVASIQYRALAESAQDA 86
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFI-IPFIQRVV-TVDVRVQTLEVsVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990    87 FYKL---SNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNE 163
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 75271990   164 INAASRMREAasekaeaekilQIKRAEGEA 193
Cdd:pfam01145 159 KQTAEQEAEA-----------EIARAEAEA 177
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 10-167 6.13e-04

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 40.46  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990    10 VDQSNVAIKETFGKFDEVLEPGCHCLP----WCLGSQVAghlslRVQQLDVRCETKTKDNVFVTVVASIQYRalAESAQD 85
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPpfieEVYPVNVT-----AVRNLRKQGLMLTGDENIVNVEMNVQYR--ITDPYK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990    86 AFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKTVETELEKAMSHY--GYEIVQTLIVDIEPDVHVKRAMN 162
Cdd:TIGR01933  77 YLFSVENPEDSLRQATDSALRGVIGDSTMDDILtEGRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFD 156


                  ....*
gi 75271990   163 EINAA 167
Cdd:TIGR01933 157 DVIIA 161
 
Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 10-278 2.97e-155

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: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 433.55  E-value: 2.97e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  10 VDQSNVAIKETFGKFDEVLEPGCHCLPWClGSQVAGHLSLRVQQLDVRCETKTKDNVFVTVVASIQYRALAESAQDAFYK 89
Cdd:cd03407   2 VSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  90 LSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASR 169
Cdd:cd03407  81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 170 MREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVPGTSSKDVMDMVLVTQYFDTLKEI 249
Cdd:cd03407 161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEV 240

                       250       260
                ....*....|....*....|....*....
gi 75271990 250 GASSKSNSVFIPHGPGAVRDIASQIRDGL 278
Cdd:cd03407 241 GKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-273 4.47e-36

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 129.96  E-value: 4.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990   4 ALGCIQVDQSNVAIKETFGKFDEVLEPGCH-CLPWClgsQVAGHLSLRVQQLDVR-CETKTKDNVFVTVVASIQYRAlaE 81
Cdd:COG0330  18 FSSVYIVPQGERGVVLRFGKYVRTLEPGLHfKIPFI---DRVRKVDVREQVLDVPpQEVLTKDNNIVDVDAVVQYRI--T 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  82 SAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRA 160
Cdd:COG0330  93 DPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 161 MNEINAASRMREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVpgtsskDVMDMVLVT 240
Cdd:COG0330 173 MEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAY------SAAPFVLFY 246

                       250       260       270
                ....*....|....*....|....*....|....
gi 75271990 241 QYFDTLKEIgASSKSNSVFIPH-GPGAVRDIASQ 273
Cdd:COG0330 247 RSLEALEEV-LSPNSKVIVLPPdGNGFLKYLLKS 279
PHB smart00244
prohibitin homologues; prohibitin homologues
 10-165 7.01e-25

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 97.35  E-value: 7.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990     10 VDQSNVAIKETFGKFDEVLEPGCHCL-PWClgsQVAGHLSLRVQQLDVRC-ETKTKDNVFVTVVASIQYRaLAESAQDAF 87
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLiPFI---DDVKKVDLRAQTDDVPPqETITKDNVKVSVDAVVYYR-VLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75271990     88 YKLSNTRNQIQAYVFDVIRASVPKLDLDSTFE-QKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEIN 165
Cdd:smart00244  82 RVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 8-193 1.29e-22

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: 92.00  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990     8 IQVDQSNVAIKETFGKFDEVLEPGCHCLpWCLGSQVAgHLSLRVQQLDV-RCETKTKDNVFVTVVASIQYRALAESAQDA 86
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFI-IPFIQRVV-TVDVRVQTLEVsVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990    87 FYKL---SNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNE 163
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 75271990   164 INAASRMREAasekaeaekilQIKRAEGEA 193
Cdd:pfam01145 159 KQTAEQEAEA-----------EIARAEAEA 177
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 50-154 2.60e-16

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: 73.17  E-value: 2.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  50 RVQQLDVRCET-KTKDNVFVTVVASIQYRALAESAQDAFYKLS---NTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIA 125
Cdd:cd02106   1 RPQFDDVRVEPvGTADGVPVAVDLVVQFRITDYNALPAFYLVDfvkDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                        90       100
                ....*....|....*....|....*....
gi 75271990 126 KTVETELEKAMSHYGYEIVQTLIVDIEPD 154
Cdd:cd02106  81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 8-261 3.00e-13

Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized.


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 67.25  E-value: 3.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990   8 IQVDQSNVAIKETFGKFDEVLEPGCHCL-PWClgSQVAgHLSLRVQQLDV-RCETKTKDNVFVTVVASIQYRALaeSAQD 85
Cdd:cd13437   7 KQVKQGSVGLVERFGKFYKTVDPGLHKVnPCT--EKII-QVDMKTQVIDLpRQSVMTKDNVSVTIDSVVYYRII--DPYK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  86 AFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEIN 165
Cdd:cd13437  82 AIYRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 166 AASRMREAasekaeaekilQIKRAEGEAESKYLsgmgiarQRQAiVDGLrnsvlafsesvpgtSSKDVMDMvlvtQYFDT 245
Cdd:cd13437 162 KAKRIGES-----------KIISAKADVESAKL-------MREA-ADIL--------------DSKAAMQI----RYLET 204

                       250
                ....*....|....*.
gi 75271990 246 LKEIGASSKSNSVFIP 261
Cdd:cd13437 205 LQAIAKSANSKVIFLP 220
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 7-195 1.25e-11

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: 62.15  E-value: 1.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990   7 CIQVDQSNVAIKETFGKF--DEVLEPGCH-CLPWclgSQVAGHLSLRVQQLDVRCETKTKDNVFVTVVASIQYRALAESA 83
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGvkDEVLGEGLHfKIPW---IQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  84 QDAF--YKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAM 161
Cdd:cd03401  78 PELYqnLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAI 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75271990 162 NEINAAS----RMREAASEKAEAEKILQIkRAEGEAES 195
Cdd:cd03401 158 EAKQVAEqeaeRAKFELEKAEQEAERKVI-EAEGEAEA 194
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 9-167 6.85e-11

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: 61.37  E-value: 6.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990   9 QVDQSNVAIKETFGKFDEVLEPGCHC-LPWCLGSQVAGHLSlRVQQLDVRCETK------TKDNVFVTVVASIQYRAlaE 81
Cdd:cd03404  17 TVDPGERGVVLRFGKYVRTVGPGLHWkLPFPIEVVEKVNVT-QVRSVEIGFRVPeeslmlTGDENIVDVDFVVQYRI--S 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  82 SAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKTVETELEKAMSHY--GYEIVQTLIVDIEPDVHVK 158
Cdd:cd03404  94 DPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLtEGRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQ 173


                ....*....
gi 75271990 159 RAMNEINAA 167
Cdd:cd03404 174 DAFDDVNAA 182
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 22-163 1.77e-10

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized.


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 59.47  E-value: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  22 GKFDEVLEPGCHcLPWCLGSQV-AGHLSLRVQQLDVRC-ETKTKDNVFVTVVASIQYR-----ALAESAQDAfyklsntR 94
Cdd:cd13438  13 GKLVRTLEPGRY-AFWKFGRKVqVELVDLREQLLEVSGqEILTADKVALRVNLVATYRvvdpvKAVETVDDP-------E 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75271990  95 NQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDI----EpdvhVKRAMNE 163
Cdd:cd13438  85 EQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIilpgE----IREILNQ 153
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 44-153 3.50e-09

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 53.25  E-value: 3.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  44 AGHLSLRVQQLDV-RCETKTKDNVFVTVVASIQYRALaeSAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKN 122
Cdd:cd08829   1 AYKVDLREQVLDIpPQEVITKDNVTVTVDAVLYYRVV--DPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSRE 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 75271990 123 DIAKTVETELEKAMSHYGYEIVQTLIVDIEP 153
Cdd:cd08829  79 EINAKLLEALDEATDPWGVKVTRVEIKDITP 109
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 49-151 9.50e-09

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. 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. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 52.19  E-value: 9.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  49 LRVQQLDV-RCETKTKDNVFVTVVASIQYRalAESAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKT 127
Cdd:cd13434   3 LRTQSVDVpPQEILTKDNVTVSVDAVVYYR--VVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                        90       100
                ....*....|....*....|....
gi 75271990 128 VETELEKAMSHYGYEIVQTLIVDI 151
Cdd:cd13434  81 LQEILDEATDPWGIKVERVEIKDI 104
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 10-167 6.13e-04

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 40.46  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990    10 VDQSNVAIKETFGKFDEVLEPGCHCLP----WCLGSQVAghlslRVQQLDVRCETKTKDNVFVTVVASIQYRalAESAQD 85
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPpfieEVYPVNVT-----AVRNLRKQGLMLTGDENIVNVEMNVQYR--ITDPYK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990    86 AFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKTVETELEKAMSHY--GYEIVQTLIVDIEPDVHVKRAMN 162
Cdd:TIGR01933  77 YLFSVENPEDSLRQATDSALRGVIGDSTMDDILtEGRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFD 156


                  ....*
gi 75271990   163 EINAA 167
Cdd:TIGR01933 157 DVIIA 161
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 47-167 7.08e-04

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 39.02  E-value: 7.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  47 LSLRVQQLDVRCETK-TKDNVFVTVVASIQYR-------ALAESAQDafykLSNTRNQIQAYVFDVI----RASVPKLDL 114
Cdd:cd03399  12 LSLETMTIDVKVEEVlTKDGIPVDVTAVAQVKvgsdpeeIAAAAERF----LGKSTEEIRELVKETLeghlRAIVGTMTV 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 75271990 115 DSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAA 167
Cdd:cd03399  88 EEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAA 140
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 47-259 9.59e-04

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 39.67  E-value: 9.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  47 LSLRVQQLDV-RCETKTKDNVFVTVVASIQYRAlaESAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIA 125
Cdd:cd13435  22 VDLRTVSFDVpPQEVLTKDSVTVTVDAVVYYRI--SDPLNAVIQVANYSHSTRLLAATTLRNVLGTRNLSELLTERETIS 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990 126 KTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASRmreaasekaeaekilqikraegEAESKYLSGMGIAR 205
Cdd:cd13435 100 HSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAR----------------------EARAKVIAAEGEMK 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75271990 206 QRQAivdgLRNSVLAFSESvPGTsskdvmdmvLVTQYFDTLKEIGASSKSNSVF 259
Cdd:cd13435 158 SSRA----LKEASDIISAS-PSA---------LQLRYLQTLSSISGEKNSTIIF 197
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 48-171 2.16e-03

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 38.26  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  48 SLRVQQLDV-RCETKTKDNVFVTVVASIQYRALaeSAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAK 126
Cdd:cd08826  10 DLRTVTLDVpPQEVITKDNVTVKVNAVVYFRVV--DPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEINK 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 75271990 127 TVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASRMR 171
Cdd:cd08826  88 RIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERER 132
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 66-171 4.27e-03

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: 259806  Cd Length: 217  Bit Score: 37.53  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75271990  66 VFVTVVASIQYRALAESAQDAFyklsntRNQIQAYVFDVI-RASVPKLDLDSTfEQKNDIAKTVETELEKAMSHYGYEIV 144
Cdd:cd03408 117 LFLTEVVGTQGTFTTDEIEEQL------RSEIVQALKDAIaELSISGLDLALE-ANLDELSAALKEKLAPEFEKYGLELT 189

                        90       100
                ....*....|....*....|....*..
gi 75271990 145 QTLIVDIEPDVHVKRAMNEINAASRMR 171
Cdd:cd03408 190 SFGIESISLPEEVQKRIDKRASMAALG 216
 
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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