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Conserved domains on  [gi|15242123|ref|NP_199970|]
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SPFH/Band 7/PHB domain-containing membrane-associated protein family [Arabidopsis thaliana]

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 ...
 11-280 8.85e-165

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: 458.20  E-value: 8.85e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  11 CIEQASVGVVERWGRFEHIAEPGCHFFNPLaGQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASADDAFY 90
Cdd:cd03407   1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  91 ELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQ 170
Cdd:cd03407  80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 171 RLQLASVYKGEAEKILQVKRAEAEAEAKYLGGVGVARQRQAITDGLRENILNFSDKVEGTSAKEVMDLIMITQYFDTIRD 250
Cdd:cd03407 160 RLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKE 239

                       250       260       270
                ....*....|....*....|....*....|
gi 15242123 251 LGNSSKNTTVFLPHGPGHVRDISDQIRNGM 280
Cdd:cd03407 240 VGKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
 
Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 11-280 8.85e-165

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: 458.20  E-value: 8.85e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  11 CIEQASVGVVERWGRFEHIAEPGCHFFNPLaGQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASADDAFY 90
Cdd:cd03407   1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  91 ELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQ 170
Cdd:cd03407  80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 171 RLQLASVYKGEAEKILQVKRAEAEAEAKYLGGVGVARQRQAITDGLRENILNFSDKVEGTSAKEVMDLIMITQYFDTIRD 250
Cdd:cd03407 160 RLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKE 239

                       250       260       270
                ....*....|....*....|....*....|
gi 15242123 251 LGNSSKNTTVFLPHGPGHVRDISDQIRNGM 280
Cdd:cd03407 240 VGKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-275 2.39e-40

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 141.52  E-value: 2.39e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  12 IEQASVGVVERWGRFEHIAEPGCHFFNPLAGQwlAGVLSTRIKSLDV-KIETKTKDNVFVQLVCSIQYRVVkaSADDAFY 90
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDR--VRKVDVREQVLDVpPQEVLTKDNNIVDVDAVVQYRIT--DPAKFLY 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  91 ELQNPKEQIQAYVFDVVRALVPMMTLDALF-EQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAA 169
Cdd:COG0330 100 NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKA 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 170 QRLQLASVYKGEAEKILQVKRAEAEAEAKYLGGVGVARQRQAITDGLRENILNFSDkvegtsAKEVMDLIMITQYFDTIR 249
Cdd:COG0330 180 EREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAE------AYSAAPFVLFYRSLEALE 253

                       250       260
                ....*....|....*....|....*.
gi 15242123 250 DLGNSSKNTTVFLPHGPGHVRDISDQ 275
Cdd:COG0330 254 EVLSPNSKVIVLPPDGNGFLKYLLKS 279
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 12-184 4.51e-26

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: 101.24  E-value: 4.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    12 IEQASVGVVERWGRFEHIAEPGCHFFNPlagqWLAGVL--STRIKSLDVK-IETKTKDNVFVQLVCSIQYRVVKASADDA 88
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIP----FIQRVVtvDVRVQTLEVSvQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    89 FYEL---QNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNE 165
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*....
gi 15242123   166 INAAQRLQLASVYKGEAEK 184
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 12-167 1.01e-17

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 78.47  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123     12 IEQASVGVVERWGRFEHIAEPGCHFFNPlagqWLAGV--LSTRIKSLDVK-IETKTKDNVFVQLVCSIQYRVVkASADDA 88
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLIP----FIDDVkkVDLRAQTDDVPpQETITKDNVKVSVDAVVYYRVL-DPLRAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123     89 FYELQNPKEQIQAYVFDVVRALVPMMTLDALFE-QKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEIN 167
Cdd:smart00244  81 YRVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 12-233 2.28e-10

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: 59.72  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    12 IEQASVGVVERWGRFEHIAEPGCHFFNPLAgQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASadDAFYE 91
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFI-EEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPY--KYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    92 LQNPKEQIQAYVFDVVRALVPMMTLDA-LFEQKGEVAKSVLEELEKVMGAYGYSIEhILMVDI---IPDPSVRKAMNEIN 167
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDiLTEGRSQIREDTKERLNEIIDNYDLGIT-VTDVNFqsaRPPEEVKEAFDDVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123   168 AAQR-----LQLASVY--------KGEAEKILQ---------VKRAEAEAE------AKYLGGVGVARQRQAItDGLREn 219
Cdd:TIGR01933 160 IAREdeeryINEAEAYanevvpkaRGDAQRIIEeargykerrINRAKGDVArftkllAEYKKAPDVTRERLYL-ETMEK- 237

                         250
                  ....*....|....
gi 15242123   220 ILNFSDKVEGTSAK 233
Cdd:TIGR01933 238 VLSNTRKVLLDDKK 251
PRK10930 PRK10930
FtsH protease activity modulator HflK;
12-196 1.10e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 43.28  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123   12 IEQASVGVVERWGRFEHIAEPGCHfFNPLAGQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASAddAFYE 91
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLN-WKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEK--YLFS 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123   92 LQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKS-VLEELEKVMGAYGYSIEhILMVDII---PDPSVRKAMNEIN 167
Cdd:PRK10930 177 VTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSdTQRELEETIRPYDMGIT-LLDVNFQaarPPEEVKAAFDDAI 255

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15242123  168 AA-----QRLQLASVY--------KGEAEKILQVKRA-------EAEAE 196
Cdd:PRK10930 256 AAreneqQYIREAEAYtnevqpraNGQAQRILEEARAykaqtilEAQGE 304
 
Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 11-280 8.85e-165

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: 458.20  E-value: 8.85e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  11 CIEQASVGVVERWGRFEHIAEPGCHFFNPLaGQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASADDAFY 90
Cdd:cd03407   1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  91 ELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQ 170
Cdd:cd03407  80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 171 RLQLASVYKGEAEKILQVKRAEAEAEAKYLGGVGVARQRQAITDGLRENILNFSDKVEGTSAKEVMDLIMITQYFDTIRD 250
Cdd:cd03407 160 RLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKE 239

                       250       260       270
                ....*....|....*....|....*....|
gi 15242123 251 LGNSSKNTTVFLPHGPGHVRDISDQIRNGM 280
Cdd:cd03407 240 VGKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-275 2.39e-40

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 141.52  E-value: 2.39e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  12 IEQASVGVVERWGRFEHIAEPGCHFFNPLAGQwlAGVLSTRIKSLDV-KIETKTKDNVFVQLVCSIQYRVVkaSADDAFY 90
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDR--VRKVDVREQVLDVpPQEVLTKDNNIVDVDAVVQYRIT--DPAKFLY 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  91 ELQNPKEQIQAYVFDVVRALVPMMTLDALF-EQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAA 169
Cdd:COG0330 100 NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKA 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 170 QRLQLASVYKGEAEKILQVKRAEAEAEAKYLGGVGVARQRQAITDGLRENILNFSDkvegtsAKEVMDLIMITQYFDTIR 249
Cdd:COG0330 180 EREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAE------AYSAAPFVLFYRSLEALE 253

                       250       260
                ....*....|....*....|....*.
gi 15242123 250 DLGNSSKNTTVFLPHGPGHVRDISDQ 275
Cdd:COG0330 254 EVLSPNSKVIVLPPDGNGFLKYLLKS 279
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 12-184 4.51e-26

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: 101.24  E-value: 4.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    12 IEQASVGVVERWGRFEHIAEPGCHFFNPlagqWLAGVL--STRIKSLDVK-IETKTKDNVFVQLVCSIQYRVVKASADDA 88
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIP----FIQRVVtvDVRVQTLEVSvQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    89 FYEL---QNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNE 165
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*....
gi 15242123   166 INAAQRLQLASVYKGEAEK 184
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAEA 177
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 12-263 1.40e-25

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: 101.15  E-value: 1.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  12 IEQASVGVVERWGRFEHIAEPGCHFFNPLAGQWLagVLSTRIKSLDVKIET-KTKDNVFVQLVCSIQYRVVkaSADDAFY 90
Cdd:cd13437   9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKII--QVDMKTQVIDLPRQSvMTKDNVSVTIDSVVYYRII--DPYKAIY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  91 ELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQ 170
Cdd:cd13437  85 RIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAK 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 171 RLqlasvykGEAeKILQvkrAEAEAEAKYLggvgvarQRQAitdglrENILNfsdkvegtsAKEVMDLimitQYFDTIRD 250
Cdd:cd13437 165 RI-------GES-KIIS---AKADVESAKL-------MREA------ADILD---------SKAAMQI----RYLETLQA 207

                       250
                ....*....|...
gi 15242123 251 LGNSSKNTTVFLP 263
Cdd:cd13437 208 IAKSANSKVIFLP 220
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 12-199 1.80e-19

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: 84.10  E-value: 1.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  12 IEQASVGVVERWGRF--EHIAEPGCHFFNPLAGQWLagVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASADDAF 89
Cdd:cd03401   4 VDAGEVGVVFRRGKGvkDEVLGEGLHFKIPWIQVVI--IYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPELY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  90 YELQNPKEQ--IQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEIN 167
Cdd:cd03401  82 QNLGPDYEErvLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAKQ 161

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15242123 168 AAQrlQLASVYKGEAEKILQ---VKRAEAEAEAKY 199
Cdd:cd03401 162 VAE--QEAERAKFELEKAEQeaeRKVIEAEGEAEA 194
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 52-157 8.32e-19

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: 79.72  E-value: 8.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  52 RIKSLDVKIET-KTKDNVFVQLVCSIQYRVVKASADDAFYEL---QNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVA 127
Cdd:cd02106   1 RPQFDDVRVEPvGTADGVPVAVDLVVQFRITDYNALPAFYLVdfvKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                        90       100       110
                ....*....|....*....|....*....|
gi 15242123 128 KSVLEELEKVMGAYGYSIEHILMVDIIPDP 157
Cdd:cd02106  81 KAVKEDLEEDLENFGVVISDVDITSIEPPD 110
PHB smart00244
prohibitin homologues; prohibitin homologues
 12-167 1.01e-17

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 78.47  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123     12 IEQASVGVVERWGRFEHIAEPGCHFFNPlagqWLAGV--LSTRIKSLDVK-IETKTKDNVFVQLVCSIQYRVVkASADDA 88
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLIP----FIDDVkkVDLRAQTDDVPpQETITKDNVKVSVDAVVYYRVL-DPLRAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123     89 FYELQNPKEQIQAYVFDVVRALVPMMTLDALFE-QKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEIN 167
Cdd:smart00244  81 YRVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 17-197 7.25e-17

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: 77.19  E-value: 7.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  17 VGVVERWGRFEHIAEPGCHFFNPLAGQWLAGVLSTRIKSLDVK-IETKTKDNVFVQLVCSIQYRVVKASAddAFYELQNP 95
Cdd:cd13438   6 RGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSgQEILTADKVALRVNLVATYRVVDPVK--AVETVDDP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  96 KEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQRlqla 175
Cdd:cd13438  84 EEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEK---- 159

                       170       180
                ....*....|....*....|..
gi 15242123 176 svyKGEAekilQVKRAEAEAEA 197
Cdd:cd13438 160 ---RAQA----NLIRAREETAA 174
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 12-256 6.54e-16

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: 75.63  E-value: 6.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  12 IEQASVGVVERWGRFEHIAEPGCHFFNPLAGQWLAGVLSTRIKSLDVKIETK------TKDNVFVQLVCSIQYRVvkASA 85
Cdd:cd03404  18 VDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRVPeeslmlTGDENIVDVDFVVQYRI--SDP 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  86 DDAFYELQNPKEQIQAYVFDVVRALVPMMTLD-ALFEQKGEVAKSVLEELEKVMGAY--GYSIEHILMVDIIPDPSVRKA 162
Cdd:cd03404  96 VAYLFNVRDPEETLRQAAESALREVVGSRTLDdVLTEGRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQDA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123 163 MNEINAAQ----RLQL-ASVY--------KGEAEKILQvkraEAEAEAkylggvgVARQRQAITDGLR-ENILNfsdkvE 228
Cdd:cd03404 176 FDDVNAARqdkeRLINeAQAYanevipraRGEAARIIQ----EAEAYK-------AEVVARAEGDAARfLALLA-----E 239

                       250       260
                ....*....|....*....|....*....
gi 15242123 229 GTSAKEVMDLIMitqYFDTIRD-LGNSSK 256
Cdd:cd03404 240 YRKAPEVTRERL---YLETMEEvLSNASK 265
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 51-154 1.32e-10

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: 57.20  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  51 TRIKSLDV-KIETKTKDNVFVQLVCSIQYRVVkaSADDAFYELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKS 129
Cdd:cd13434   3 LRTQSVDVpPQEILTKDNVTVSVDAVVYYRVV--DPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                        90       100
                ....*....|....*....|....*
gi 15242123 130 VLEELEKVMGAYGYSIEHILMVDII 154
Cdd:cd13434  81 LQEILDEATDPWGIKVERVEIKDII 105
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 12-233 2.28e-10

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: 59.72  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    12 IEQASVGVVERWGRFEHIAEPGCHFFNPLAgQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASadDAFYE 91
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFI-EEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPY--KYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    92 LQNPKEQIQAYVFDVVRALVPMMTLDA-LFEQKGEVAKSVLEELEKVMGAYGYSIEhILMVDI---IPDPSVRKAMNEIN 167
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDiLTEGRSQIREDTKERLNEIIDNYDLGIT-VTDVNFqsaRPPEEVKEAFDDVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123   168 AAQR-----LQLASVY--------KGEAEKILQ---------VKRAEAEAE------AKYLGGVGVARQRQAItDGLREn 219
Cdd:TIGR01933 160 IAREdeeryINEAEAYanevvpkaRGDAQRIIEeargykerrINRAKGDVArftkllAEYKKAPDVTRERLYL-ETMEK- 237

                         250
                  ....*....|....
gi 15242123   220 ILNFSDKVEGTSAK 233
Cdd:TIGR01933 238 VLSNTRKVLLDDKK 251
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 50-193 2.10e-07

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: 49.82  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  50 STRIKSLDV-KIETKTKDNVFVQLVCSIQYRVVkaSADDAFYELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAK 128
Cdd:cd08826  10 DLRTVTLDVpPQEVITKDNVTVKVNAVVYFRVV--DPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEINK 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242123 129 SVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQRLQLASVYKGEAEKILQVKRAEA 193
Cdd:cd08826  88 RIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA 152
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 46-157 1.12e-06

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: 46.31  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  46 AGVLSTRIKSLDV-KIETKTKDNVFVQLVCSIQYRVVKASadDAFYELQNPKEQIQAYVFDVVRALVPMMTLDALFEQKG 124
Cdd:cd08829   1 AYKVDLREQVLDIpPQEVITKDNVTVTVDAVLYYRVVDPY--KASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSRE 78

                        90       100       110
                ....*....|....*....|....*....|...
gi 15242123 125 EVAKSVLEELEKVMGAYGYSIEHILMVDIIPDP 157
Cdd:cd08829  79 EINAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 13-207 1.28e-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: 45.56  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  13 EQAsvgVVERWGRFEH-IAEPGCHFFNPLAGQwlAGVLSTRIKSLDV---KIETKTKDNVFVQLVcsIQYRVVkasaDDA 88
Cdd:cd03405   9 EQA---VVLQFGKPVRvITEPGLHFKLPFIQN--VRKFDKRILTLDGppeEVLTKDKKRLIVDSY--ARWRIT----DPL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  89 -FYE----LQNPKEQIQAYVFDVVRALVPMMTL-DALFEQKGEVAKSVLEELEKVMGAYGysiehILMVDI------IPD 156
Cdd:cd03405  78 rFYQsvggEEGAESRLDDIVDSALRNEIGKRTLaEVVSGGRDELMEEILEQANEEAKEYG-----IEVVDVrikridLPE 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242123 157 pSVRKAMNEINAAQRLQLASVY----KGEAEKI-------LQVKRAEAEAEAKYLGGVGVAR 207
Cdd:cd03405 153 -EVSESVYERMRAERERIAAEYraegEEEAEKIraeadreRTVILAEAYREAEEIRGEGDAE 213
PRK10930 PRK10930
FtsH protease activity modulator HflK;
12-196 1.10e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 43.28  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123   12 IEQASVGVVERWGRFEHIAEPGCHfFNPLAGQWLAGVLSTRIKSLDVKIETKTKDNVFVQLVCSIQYRVVKASAddAFYE 91
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLN-WKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEK--YLFS 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123   92 LQNPKEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKS-VLEELEKVMGAYGYSIEhILMVDII---PDPSVRKAMNEIN 167
Cdd:PRK10930 177 VTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSdTQRELEETIRPYDMGIT-LLDVNFQaarPPEEVKAAFDDAI 255

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15242123  168 AA-----QRLQLASVY--------KGEAEKILQVKRA-------EAEAE 196
Cdd:PRK10930 256 AAreneqQYIREAEAYtnevqpraNGQAQRILEEARAykaqtilEAQGE 304
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 116-217 5.55e-03

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 36.17  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123    116 LDALFEQKGEVaKSVLEELEKVMGAYGYSIEHILMVdIIPDPSVRKAMNEINAAqrlqlasvYKGEAEKI-LQVKRAEAE 194
Cdd:smart00503   3 LDEFFEKVEEI-RANIQKISQNVAELQKLHEELLTP-PDADKELREKLERLIDD--------IKRLAKEIrAKLKELEKE 72

                           90       100
                   ....*....|....*....|...
gi 15242123    195 AEAKYLGGVGVARQRQAITDGLR 217
Cdd:smart00503  73 NLENRASGSASDRTRKAQTEKLR 95
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
96-199 7.84e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 37.54  E-value: 7.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242123  96 KEQIQAYVFDVVRALVPMMTLDALFEQKGEVAKSVLEELEKVMGAYGYSIEHILMVDIIPDPSVRKAMNEINAAQRLQLA 175
Cdd:COG2268 122 EELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDA 201

                        90       100
                ....*....|....*....|....
gi 15242123 176 SVYKGEAEKILQVKRAEAEAEAKY 199
Cdd:COG2268 202 RIAEAEAERETEIAIAQANREAEE 225
 
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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