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Conserved domains on  [gi|757599719|ref|WP_042847363|]
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MULTISPECIES: SPFH domain-containing protein [Enterobacterales]

Protein Classification

SPFH domain-containing protein( domain architecture ID 11417211)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Homo sapiens mitochondrial stomatin-like protein 2, and Escherichia coli protein QmcA

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  16101677|17766116|10542406|21501885|24782879
TCDB:  8.A.21

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 3-294 2.04e-73

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.03  E-value: 2.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   3 GLISLAVVVVFLGITLYQCVRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAM 82
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  83 TQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETL-TNRDELAARLRQSMDVQMVDWGLSLRTVDI 161
Cdd:COG0330   81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 162 QDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREATaletlanGQFKASSKL 241
Cdd:COG0330  161 KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAE-------GEAEAFRIV 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 757599719 242 AEALtieggrEAMSFQLANNYIETLSVLAtSPNAKVVAMPADLAQSVGGLINA 294
Cdd:COG0330  234 AEAY------SAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 3-294 2.04e-73

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.03  E-value: 2.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   3 GLISLAVVVVFLGITLYQCVRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAM 82
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  83 TQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETL-TNRDELAARLRQSMDVQMVDWGLSLRTVDI 161
Cdd:COG0330   81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 162 QDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREATaletlanGQFKASSKL 241
Cdd:COG0330  161 KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAE-------GEAEAFRIV 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 757599719 242 AEALtieggrEAMSFQLANNYIETLSVLAtSPNAKVVAMPADLAQSVGGLINA 294
Cdd:COG0330  234 AEAY------SAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-168 1.04e-43

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: 145.31  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  58 AYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDEL 137
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 757599719 138 AARLRQSMDVQMVDWGLSLRTVDIQDITPSD 168
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 20-178 9.18e-39

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 133.94  E-value: 9.18e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719    20 QCVRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKA 99
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   100 AYGVDNFN-TAVRNLVMTTIRNAVGGMELDETLT-NRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQ 177
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 757599719   178 A 178
Cdd:smart00244 160 Q 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 23-195 8.23e-33

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: 119.35  E-value: 8.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   23 RIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVA--DPKKAA 100
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  101 YGV---DNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQ 177
Cdd:pfam01145  80 QNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 757599719  178 AAAVRERKATEELAAGNK 195
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 22-224 1.34e-18

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: 83.22  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   22 VRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKdqmiEVKGIEA----ITKDNAMTQVNAICFIRVADPK 97
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVT----AVRNLRKqglmLTGDENIVNVEMNVQYRITDPY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   98 KAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLT-NRDELAARLRQSMDVQM--VDWGLSLRTVDIQDITPSDSMLKSM 174
Cdd:TIGR01933  76 KYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTeGRSQIREDTKERLNEIIdnYDLGITVTDVNFQSARPPEEVKEAF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 757599719  175 EKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREA 224
Cdd:TIGR01933 156 DDVIIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRA 205
PRK10930 PRK10930
FtsH protease activity modulator HflK;
1-224 6.33e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 53.29  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   1 MIGLISLAVVVVFLGITLYQcvriVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIAYRMSAKDQMIEVKGIeAITKDN 80
Cdd:PRK10930  80 VVGIAAAAVVIIWAASGFYT----IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGV-MLTSDE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  81 AMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTN-----RDELAARLRQSmdVQMVDWGLS 155
Cdd:PRK10930 155 NVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgrtviRSDTQRELEET--IRPYDMGIT 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757599719 156 LRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREA 224
Cdd:PRK10930 233 LLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEA 301
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 3-294 2.04e-73

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.03  E-value: 2.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   3 GLISLAVVVVFLGITLYQCVRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAM 82
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  83 TQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETL-TNRDELAARLRQSMDVQMVDWGLSLRTVDI 161
Cdd:COG0330   81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 162 QDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREATaletlanGQFKASSKL 241
Cdd:COG0330  161 KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAE-------GEAEAFRIV 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 757599719 242 AEALtieggrEAMSFQLANNYIETLSVLAtSPNAKVVAMPADLAQSVGGLINA 294
Cdd:COG0330  234 AEAY------SAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-168 1.04e-43

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: 145.31  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  58 AYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDEL 137
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 757599719 138 AARLRQSMDVQMVDWGLSLRTVDIQDITPSD 168
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 20-178 9.18e-39

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 133.94  E-value: 9.18e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719    20 QCVRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKA 99
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   100 AYGVDNFN-TAVRNLVMTTIRNAVGGMELDETLT-NRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQ 177
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 757599719   178 A 178
Cdd:smart00244 160 Q 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 23-195 8.23e-33

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: 119.35  E-value: 8.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   23 RIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVA--DPKKAA 100
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  101 YGV---DNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQ 177
Cdd:pfam01145  80 QNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 757599719  178 AAAVRERKATEELAAGNK 195
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 74-203 3.84e-32

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: 117.62  E-value: 3.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  74 EAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWG 153
Cdd:cd08826   22 EVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEINKRIQEIIDEQTEPWG 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 757599719 154 LSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQ 203
Cdd:cd08826  102 IKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAE 151
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 25-283 7.29e-31

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: 115.40  E-value: 7.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  25 VPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVD 104
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 105 NFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMekqAAAVRER 184
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSL---SSAAKAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 185 KATEelaagnknAAIMEAQGKKEAMILDAEAkqqsavreATALETLAngqfkassklaealtieggreAMSFQlannYIE 264
Cdd:cd13437  165 RIGE--------SKIISAKADVESAKLMREA--------ADILDSKA---------------------AMQIR----YLE 203

                        250
                 ....*....|....*....
gi 757599719 265 TLSVLATSPNAKVVAMPAD 283
Cdd:cd13437  204 TLQAIAKSANSKVIFLPLD 222
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 24-283 5.16e-30

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: 114.60  E-value: 5.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  24 IVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIAYRMSAKDQMIEVKgIEAITKDNAMTQVNAICFIRVADPK--KAAY 101
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVPEKvyDAFY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 102 GVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQAAAV 181
Cdd:cd03407   80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 182 RERKATEELAAGNKNAAIMEAQGKKEAMILDAE--AKQQSAVRE--ATALETLANGQFKASSKlaealtieggrEAMSFQ 257
Cdd:cd03407  160 RLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVgiAEQRKAIVDglRESIEDFQEAVPGVSSK-----------EVMDLL 228

                        250       260
                 ....*....|....*....|....*.
gi 757599719 258 LANNYIETLSVLATSPNAKVVAMPAD 283
Cdd:cd03407  229 LITQYFDTLKEVGKSSKSSTVFLPHG 254
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 8-226 5.49e-27

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: 106.44  E-value: 5.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   8 AVVVVFLGITLYQCVRIVPQADQWVVERLGKYHTTLNPGLNILIPFLD--------------NIAYRMSAKDQMievkgi 73
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIevvekvnvtqvrsvEIGFRVPEESLM------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  74 eaITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTN-RDELAARLRQSMDVQMVDW 152
Cdd:cd03404   75 --LTGDENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRY 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757599719 153 --GLSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREATA 226
Cdd:cd03404  153 dlGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEG 228
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 66-164 7.53e-27

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: 101.50  E-value: 7.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  66 QMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSM 145
Cdd:cd13434    6 QSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEIL 85

                         90
                 ....*....|....*....
gi 757599719 146 DVQMVDWGLSLRTVDIQDI 164
Cdd:cd13434   86 DEATDPWGIKVERVEIKDI 104
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 45-284 2.91e-25

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: 100.15  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  45 PGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGG 124
Cdd:cd13435    7 PGVFFVLPCIDNY-CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 125 MELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATeelaagnknaaIMEAQG 204
Cdd:cd13435   86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAK-----------VIAAEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 205 kkeamildaEAKQQSAVREATALetlangqfkassklaealtIEGGREAMSFQlannYIETLSVLATSPNAKVV-AMPAD 283
Cdd:cd13435  155 ---------EMKSSRALKEASDI-------------------ISASPSALQLR----YLQTLSSISGEKNSTIIfPLPME 202


                 .
gi 757599719 284 L 284
Cdd:cd13435  203 L 203
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 74-200 3.40e-22

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); 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.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 91.15  E-value: 3.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  74 EAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWG 153
Cdd:cd13775   14 QTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 757599719 154 LSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIM 200
Cdd:cd13775   94 ITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEM 140
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 22-208 1.69e-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: 84.49  E-value: 1.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  22 VRIVPQADQWVVERLGKYHT--TLNPGLNILIPFLDNIaYRMSAKDQMIEVKgIEAITKDNAMTQVNAICFIRVaDPKKA 99
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKdeVLGEGLHFKIPWIQVV-IIYDVRTQPREIT-LTVLSKDGQTVNIDLSVLYRP-DPEKL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 100 A-----YGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSM 174
Cdd:cd03401   78 PelyqnLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAI 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 757599719 175 E-KQAAAVRERKATEEL--AAGNKNAAIMEAQGKKEA 208
Cdd:cd03401  158 EaKQVAEQEAERAKFELekAEQEAERKVIEAEGEAEA 194
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 45-231 5.08e-19

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 83.37  E-value: 5.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  45 PGLNILIPFLDNIAyRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGG 124
Cdd:cd03403    7 PGLFFILPCIDSYR-KVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 125 MELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAaimeAQG 204
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNA----SRA 161

                        170       180
                 ....*....|....*....|....*..
gi 757599719 205 KKEAMILDAEAKQQSAVREATALETLA 231
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTIS 188
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 21-220 6.46e-19

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: 84.08  E-value: 6.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  21 CVRIVPQADQWVVERLGK-YHTTLNPGLNILIPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKK- 98
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKpVRVITEPGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  99 --AAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTN-RDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSME 175
Cdd:cd03405   80 yqSVGGEEGAESRLDDIVDSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 757599719 176 KQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSA 220
Cdd:cd03405  160 ERMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYREAE 204
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 22-224 1.34e-18

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: 83.22  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   22 VRIVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIaYRMSAKdqmiEVKGIEA----ITKDNAMTQVNAICFIRVADPK 97
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVT----AVRNLRKqglmLTGDENIVNVEMNVQYRITDPY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   98 KAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLT-NRDELAARLRQSMDVQM--VDWGLSLRTVDIQDITPSDSMLKSM 174
Cdd:TIGR01933  76 KYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTeGRSQIREDTKERLNEIIdnYDLGITVTDVNFQSARPPEEVKEAF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 757599719  175 EKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREA 224
Cdd:TIGR01933 156 DDVIIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRA 205
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 37-202 1.22e-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: 79.89  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  37 GKYHTTLNPGLNILIPFLDNI-AYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVM 115
Cdd:cd13438   13 GKLVRTLEPGRYAFWKFGRKVqVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEEQLYLALQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 116 TTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSM------EKQAAAVRERkATEE 189
Cdd:cd13438   93 LALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILnqvleaEKRAQANLIR-AREE 171

                        170
                 ....*....|....*.
gi 757599719 190 LAAGN--KNAA-IMEA 202
Cdd:cd13438  172 TAATRslLNAAkLMEE 187
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 45-197 1.25e-16

Slipin-3 (SLP-3), 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 vertebrates. 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 slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 75.45  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  45 PGLNILIPFLDNIAyRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGG 124
Cdd:cd08828    3 PGLILVLPCTDTFI-KVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757599719 125 MELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNA 197
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 21-198 1.04e-14

Podocin, 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 vertebrates. 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. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 71.84  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  21 CVRIVPQADQWVVERLGKY--HTTLNPGLNILIPFLDnIAYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKK 98
Cdd:cd08827    3 CVKVVREYERAVIFRLGHLlqGRARGPGLFFYLPCLD-VCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  99 AAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQA 178
Cdd:cd08827   82 CLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEA 161

                        170       180
                 ....*....|....*....|
gi 757599719 179 AAVRERKATEELAAGNKNAA 198
Cdd:cd08827  162 EAQRQAKVKVIAAEGEKAAS 181
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 37-163 1.14e-11

Stomatin-like protein 1 (SLP-1), 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 animals. 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. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 61.26  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  37 GKYHTTLNPGLNILIPFLDNIAyRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMT 116
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFT-RVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 757599719 117 TIRNAVGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQD 163
Cdd:cd13436   80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSD 126
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 66-168 2.14e-10

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: 56.99  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  66 QMIEVKGIEAITKDNAMTQVNAICFIRVADPKKA-----AYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTNRDELAAR 140
Cdd:cd02106    3 QFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKA 82

                         90       100
                 ....*....|....*....|....*...
gi 757599719 141 LRQSMDVQMVDWGLSLRTVDIQDITPSD 168
Cdd:cd02106   83 VKEDLEEDLENFGVVISDVDITSIEPPD 110
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 4-226 2.56e-10

HflC 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. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 60.18  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719    4 LISLAVVVVFLGITLYQCVRIVPQADQWVVERLGKYHTTLN-------PGLNILIPFLDNIaYRMSAKDQMIEVKGIEAI 76
Cdd:TIGR01932   2 RKIGIVVIVLLIVVLFQPFFIIKEGERGIITRFGKILKDNNhhvlvyePGLHFKIPFIEHV-KIFDAKIQTMDGRPDRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   77 TKDNAMTQVNAICFIRVADPKK--AAYGVDNFNTA---VRNLVMTTIRNAVGGMELDETLTN------------------ 133
Cdd:TIGR01932  81 TKEKKDIIIDTYIRWRIEDFKKyyLSTGGGTISAAevlIKRKIDDRLRSEIGVLGLKEIVRSsndqldtlvsklalnrgg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  134 ------------RDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIME 201
Cdd:TIGR01932 161 kinkiamtitkgREILAREISQIANSQLKDIGIEVVDVRIKKINYSDELSESIYNRMRSEREQIARMHRSQGEEKAEEIL 240

                         250       260
                  ....*....|....*....|....*
gi 757599719  202 AQGKKEAMILDAEAKQQSAVREATA 226
Cdd:TIGR01932 241 GKAEYEVRKILSEAYRTARIIKGEG 265
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 51-182 1.68e-08

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: 52.51  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  51 IPFLDNIaYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIRV-ADPKKAAYGVDNFNT----AVRNLVMTTI----RNA 121
Cdd:cd03399    3 IPFLQRV-QRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVgSDPEEIAAAAERFLGksteEIRELVKETLeghlRAI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599719 122 VGGMELDETLTNRDELAARLRQSMDVQMVDWGLSLRTVDIQDITPSDSMLKSM-EKQAAAVR 182
Cdd:cd03399   82 VGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLgRKQAAEVK 143
PRK10930 PRK10930
FtsH protease activity modulator HflK;
1-224 6.33e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 53.29  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   1 MIGLISLAVVVVFLGITLYQcvriVPQADQWVVERLGKYHTTLNPGLNILIPFLDNIAYRMSAKDQMIEVKGIeAITKDN 80
Cdd:PRK10930  80 VVGIAAAAVVIIWAASGFYT----IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGV-MLTSDE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  81 AMTQVNAICFIRVADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELDETLTN-----RDELAARLRQSmdVQMVDWGLS 155
Cdd:PRK10930 155 NVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgrtviRSDTQRELEET--IRPYDMGIT 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757599719 156 LRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVREA 224
Cdd:PRK10930 233 LLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEA 301
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
2-253 9.37e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 52.95  E-value: 9.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719   2 IGLISLAVVVVFLGITLYQCVRIVPQADQWVVE-RLGKYHTTLNpGLNILIPFLDNIAyRMSAKDQMIEVKGIE-AITKD 79
Cdd:COG2268    8 IIIGVIVVVLLLLLIILARFYRKVPPNEALVITgRGGGYKVVTG-GGAFVLPVLHRAE-RMSLSTMTIEVERTEgLITKD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  80 NAMTQVNAICFIRVA-DPKKAAYGVDNFNT----AVRNLVMTT----IRNAVGGMELDETLTNRDELAARLRQSMDVQMV 150
Cdd:COG2268   86 GIRVDVDAVFYVKVNsDPEDIANAAERFLGrdpeEIEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719 151 DWGLSLRTVDIQDITPSDSMLKSMEKQAAAVRERKATEELAAGNKNAAIMEAQGKKEAMILDAEAKQQSAVR---EATAL 227
Cdd:COG2268  166 KNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETAriaEAEAE 245

                        250       260
                 ....*....|....*....|....*.
gi 757599719 228 ETLANGQFKASSKLAEALTIEGGREA 253
Cdd:COG2268  246 LAKKKAEERREAETARAEAEAAYEIA 271
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 14-181 1.72e-05

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: 259800  Cd Length: 231  Bit Score: 45.24  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  14 LGITLYQCVRIVPQADQWVVERLGKYHTTLN-PGLNILIPFLdnIAYRMSAKDQMIEVKGIEAITKDNAMTQVNAICFIR 92
Cdd:cd03402    2 VGIILLGGFFVVQPNEAAVLTLFGRYRGTVRrPGLRWVNPFY--RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599719  93 VADPKKAAYGVDNFNTAVRNLVMTTIRNAVGGMELD------ETL-TNRDELAARLRQSMDVQMVDWGLSLRTVDIQDIT 165
Cdd:cd03402   80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDsfedgePSLrGNSDEVSEELRRELQERLAVAGVEVIEARITHLA 159

                        170       180
                 ....*....|....*....|
gi 757599719 166 PS----DSMLKsmEKQAAAV 181
Cdd:cd03402  160 YApeiaQAMLQ--RQQASAI 177
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 240-306 4.57e-05

C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal extension of the Band_7 family, pfam01145. It is found in proteins fro bacteria to fungi, plants and mammals.


Pssm-ID: 465062  Cd Length: 63  Bit Score: 40.54  E-value: 4.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757599719  240 KLAEALTIEGGREAMSFQLANNYIETLSVLATSPNAKVVamPADLAqSVGGLInaGSLMSVGSAVSK 306
Cdd:pfam16200   2 KVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVIL--PANLG-DVSSMV--AQAMSIYKKVNK 63
 
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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