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Conserved domains on  [gi|487978515|ref|WP_002051299|]
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MULTISPECIES: SPFH domain-containing protein [Acinetobacter]

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 ...
 4-282 8.56e-74

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.42  E-value: 8.56e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   4 GTIIVLAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAV 83
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  84 LLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDWGITLKTVEI 162
Cdd:COG0330   81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 163 QDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQAAILEADGRLEASRRDAEA----QVVLAEASQKAIEMVTSAVgdk 238
Cdd:COG0330  161 KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAyreaQILRAEGEAEAFRIVAEAY--- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 487978515 239 eTPVAYLLGEQYVKAMQDMAkSSNAKTVVLPADVLNTIRGIMGK 282
Cdd:COG0330  238 -SAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-282 8.56e-74

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.42  E-value: 8.56e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   4 GTIIVLAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAV 83
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  84 LLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDWGITLKTVEI 162
Cdd:COG0330   81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 163 QDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQAAILEADGRLEASRRDAEA----QVVLAEASQKAIEMVTSAVgdk 238
Cdd:COG0330  161 KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAyreaQILRAEGEAEAFRIVAEAY--- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 487978515 239 eTPVAYLLGEQYVKAMQDMAkSSNAKTVVLPADVLNTIRGIMGK 282
Cdd:COG0330  238 -SAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 59-169 5.31e-49

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: 158.02  E-value: 5.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  59 AYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHI 138
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 487978515 139 KAKLKAAISDDISDWGITLKTVEIQDIQPSS 169
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 21-170 1.13e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 125.47  E-value: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515    21 KGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKA 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487978515   101 VYGIENYTWA-IQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSST 170
Cdd:smart00244  80 VYRVLDADYAvIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEE 151
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 24-196 5.85e-31

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: 113.57  E-value: 5.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   24 RIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAY--INLTTPEKAV 101
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIyrVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  102 Y---GIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQ 178
Cdd:pfam01145  80 QnvfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 487978515  179 AAAERQRRATVTRADGEK 196
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 23-253 7.51e-15

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: 72.43  E-value: 7.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   23 VRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRD-NAVLLMNAVAYiNLTTPEKAV 101
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVTAVRNLRKQGLMLTGDeNIVNVEMNVQY-RITDPYKYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  102 YGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDIS--DWGITLKTVEIQDIQPSStmqaameaq 178
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDnyDLGITVTDVNFQSARPPE--------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  179 aaAERQRRATVTRADGEKQAAILEAdgrleasrrDAEAQVVLAEASQKAIEMVTSAVGDKETPVAYLLGE---------Q 249
Cdd:TIGR01933 150 --EVKEAFDDVIIAREDEERYINEA---------EAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDvarftkllaE 218


                  ....
gi 487978515  250 YVKA 253
Cdd:TIGR01933 219 YKKA 222
PRK10930 PRK10930
FtsH protease activity modulator HflK;
4-167 1.32e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.97  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   4 GTIIVLAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVAyKVTTKDIVLDIPSQEVITRDNAV 83
Cdd:PRK10930  78 GRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVK-PVNVEAVRELAASGVMLTSDENV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  84 LL--MNaVAYiNLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDIS--DWGITLK 158
Cdd:PRK10930 157 VRveMN-VQY-RVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRpyDMGITLL 234


                 ....*....
gi 487978515 159 TVEIQDIQP 167
Cdd:PRK10930 235 DVNFQAARP 243
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-282 8.56e-74

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.42  E-value: 8.56e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   4 GTIIVLAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAV 83
Cdd:COG0330    2 KLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  84 LLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDWGITLKTVEI 162
Cdd:COG0330   81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 163 QDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQAAILEADGRLEASRRDAEA----QVVLAEASQKAIEMVTSAVgdk 238
Cdd:COG0330  161 KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAyreaQILRAEGEAEAFRIVAEAY--- 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 487978515 239 eTPVAYLLGEQYVKAMQDMAkSSNAKTVVLPADVLNTIRGIMGK 282
Cdd:COG0330  238 -SAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 59-169 5.31e-49

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: 158.02  E-value: 5.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  59 AYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHI 138
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 487978515 139 KAKLKAAISDDISDWGITLKTVEIQDIQPSS 169
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 26-271 2.81e-39

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: 136.59  E-value: 2.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  26 VPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIE 105
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 106 NYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSstmQAAMEAQAAAERQR 185
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLS---KDLQQSLSSAAKAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 186 RATvtradgekQAAILEADGRLEASRRDAEAQVVLAeaSQKAIEMvtsavgdketpvayllgeQYVKAMQDMAKSSNAKT 265
Cdd:cd13437  165 RIG--------ESKIISAKADVESAKLMREAADILD--SKAAMQI------------------RYLETLQAIAKSANSKV 216


                 ....*.
gi 487978515 266 VVLPAD 271
Cdd:cd13437  217 IFLPLD 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 53-210 4.36e-37

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: 129.56  E-value: 4.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  53 PYIDDVAyKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDAL 132
Cdd:cd08826    1 PFIDRMV-RVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 133 SSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQAA--ILEADGRLEAS 210
Cdd:cd08826   80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAekLAEAAEILAKS 159
PHB smart00244
prohibitin homologues; prohibitin homologues
 21-170 1.13e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 125.47  E-value: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515    21 KGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKA 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487978515   101 VYGIENYTWA-IQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSST 170
Cdd:smart00244  80 VYRVLDADYAvIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEE 151
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 24-196 5.85e-31

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: 113.57  E-value: 5.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   24 RIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAY--INLTTPEKAV 101
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIyrVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  102 Y---GIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQ 178
Cdd:pfam01145  80 QnvfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 487978515  179 AAAERQRRATVTRADGEK 196
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 25-271 2.92e-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: 2.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  25 IVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVAYKVTTKDIVLDIpSQEVITRDNA-VLLMNAVAYinLTTPEK---A 100
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDV-RVETKTKDNVfVTLVVSVQY--RVVPEKvydA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 101 VYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAA 180
Cdd:cd03407   78 FYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 181 AERQRRATVTRADGEKQAAILEADGRLEASRRDAEAqvvLAEASQ-------KAIEMVTSAVGD---KEtPVAYLLGEQY 250
Cdd:cd03407  158 AQRLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVG---IAEQRKaivdglrESIEDFQEAVPGvssKE-VMDLLLITQY 233

                        250       260
                 ....*....|....*....|.
gi 487978515 251 VKAMQDMAKSSNAKTVVLPAD 271
Cdd:cd03407  234 FDTLKEVGKSSKSSTVFLPHG 254
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 46-210 3.24e-29

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: 110.17  E-value: 3.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  46 PGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGE 125
Cdd:cd13435    7 PGVFFVLPCIDNY-CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 126 MDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQA--AILEA 203
Cdd:cd13435   86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSsrALKEA 165


                 ....*..
gi 487978515 204 DGRLEAS 210
Cdd:cd13435  166 SDIISAS 172
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 9-253 2.24e-26

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: 104.13  E-value: 2.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   9 LAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVAYKVTTKDI------VLDIPSQEVITRDNA 82
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQVrsveigFRVPEESLMLTGDEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  83 VLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDW--GITLKT 159
Cdd:cd03404   81 IVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 160 VEIQDIQPSSTMqaameaqaaaerqRRAT--VTRADGEKQAAILEAdgrlEASRRD------AEAQVVLAEASQKAIEMV 231
Cdd:cd03404  161 VQLQDADPPEEV-------------QDAFddVNAARQDKERLINEA----QAYANEviprarGEAARIIQEAEAYKAEVV 223

                        250       260
                 ....*....|....*....|..
gi 487978515 232 TSAVGDKETPVAYLlgEQYVKA 253
Cdd:cd03404  224 ARAEGDAARFLALL--AEYRKA 243
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 62-165 8.79e-24

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: 92.64  E-value: 8.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  62 VTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAK 141
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....
gi 487978515 142 LKAAISDDISDWGITLKTVEIQDI 165
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDI 104
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 46-223 1.06e-23

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: 95.31  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  46 PGLNFVIPYIDDVAyKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGE 125
Cdd:cd03403    7 PGLFFILPCIDSYR-KVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 126 MDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQaaileadg 205
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQN-------- 157

                        170
                 ....*....|....*...
gi 487978515 206 rleASRRDAEAQVVLAEA 223
Cdd:cd03403  158 ---ASRALKEAADVISES 172
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 46-198 2.78e-21

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: 87.78  E-value: 2.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  46 PGLNFVIPYIDdVAYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGE 125
Cdd:cd08828    3 PGLILVLPCTD-TFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487978515 126 MDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQA 198
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 67-199 8.15e-20

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: 84.21  E-value: 8.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  67 IVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAI 146
Cdd:cd13775    6 RTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDII 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 487978515 147 SDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAAAERQRRATVTRADGEKQAA 199
Cdd:cd13775   86 DEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIA 138
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 25-230 6.14e-18

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: 81.00  E-value: 6.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  25 IVPQGYKWIVQRLGK-YHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEK---A 100
Cdd:cd03405    4 IVDETEQAVVLQFGKpVRVITEPGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRfyqS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 101 VYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQA 179
Cdd:cd03405   83 VGGEEGAESRLDDIVDSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYERM 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487978515 180 AAERQRRATVTRADGEKQAAILEADgrleasrRDAEAQVVLAEASQKAIEM 230
Cdd:cd03405  163 RAERERIAAEYRAEGEEEAEKIRAE-------ADRERTVILAEAYREAEEI 206
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 23-199 3.14e-16

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: 75.69  E-value: 3.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  23 VRIVPQGYKWIVQRLGKYHS--TLNPGLNFVIPYIDdVAYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKA 100
Cdd:cd08827    4 VKVVREYERAVIFRLGHLLQgrARGPGLFFYLPCLD-VCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 101 VYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSSTMQAAMEAQAA 180
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170
                 ....*....|....*....
gi 487978515 181 AERQRRATVTRADGEKQAA 199
Cdd:cd08827  163 AQRQAKVKVIAAEGEKAAS 181
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 26-165 6.80e-16

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: 74.49  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  26 VPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDV-AYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGI 104
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVqVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487978515 105 ENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDI 165
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDI 141
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 23-253 7.51e-15

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: 72.43  E-value: 7.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   23 VRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVaYKVTTKDIVLDIPSQEVITRD-NAVLLMNAVAYiNLTTPEKAV 101
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVTAVRNLRKQGLMLTGDeNIVNVEMNVQY-RITDPYKYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  102 YGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDIS--DWGITLKTVEIQDIQPSStmqaameaq 178
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDnyDLGITVTDVNFQSARPPE--------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  179 aaAERQRRATVTRADGEKQAAILEAdgrleasrrDAEAQVVLAEASQKAIEMVTSAVGDKETPVAYLLGE---------Q 249
Cdd:TIGR01933 150 --EVKEAFDDVIIAREDEERYINEA---------EAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDvarftkllaE 218


                  ....
gi 487978515  250 YVKA 253
Cdd:TIGR01933 219 YKKA 222
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 23-227 2.32e-14

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: 69.85  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  23 VRIVPQGYKWIVQRLGKYHS--TLNPGLNFVIPYIDDV-AYKVTTKDIVLDIpsqEVITRDnavLLMnavayINLT---- 95
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKdeVLGEGLHFKIPWIQVViIYDVRTQPREITL---TVLSKD---GQT-----VNIDlsvl 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  96 ---TPEKAV-----YGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQP 167
Cdd:cd03401   70 yrpDPEKLPelyqnLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDF 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487978515 168 SstmqaameaqaaaerqrrATVTRADGEKQAA---ILEADGRLEASRRDAEAQVVLAEASQKA 227
Cdd:cd03401  150 P------------------DEYEKAIEAKQVAeqeAERAKFELEKAEQEAERKVIEAEGEAEA 194
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 46-166 2.58e-12

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: 62.80  E-value: 2.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  46 PGLNFVIPYIDDVAyKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGE 125
Cdd:cd13436    9 PGIVLILPCIDNFT-RVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTSLTNSLSK 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 487978515 126 MDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQ 166
Cdd:cd13436   88 KTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVK 128
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 68-167 6.48e-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: 55.45  E-value: 6.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  68 VLDIPSQEVITRDNAVLLMNAVAYINLTTPEKA-----VYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSSRDHIKAKL 142
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                         90       100
                 ....*....|....*....|....*
gi 487978515 143 KAAISDDISDWGITLKTVEIQDIQP 167
Cdd:cd02106   84 KEDLEEDLENFGVVISDVDITSIEP 108
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-227 5.29e-09

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 56.42  E-value: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   1 MPVGTIIVLAFLAFVAVTIF-----KGVRIVPQGYKWIVQ-RLGKYHSTLNpGLNFVIPYIDDVAYkVTTKDIVLDI-PS 73
Cdd:COG2268    1 METLGILIIIGVIVVVLLLLliilaRFYRKVPPNEALVITgRGGGYKVVTG-GGAFVLPVLHRAER-MSLSTMTIEVeRT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  74 QEVITRDNAVLLMNAVAYINLTTPEKAVY-GIENY----TWAIQNLVQT----SLRSIVGEMDLDDALSSRDHIKAKLKA 144
Cdd:COG2268   79 EGLITKDGIRVDVDAVFYVKVNSDPEDIAnAAERFlgrdPEEIEELAEEklegALRAVAAQMTVEELNEDREKFAEKVQE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515 145 AISDDISDWGITLKTVEIQDI-----------QPSSTMQAAMEAQAAAERQRRATVTRADGEKQAAILEAD-----GRLE 208
Cdd:COG2268  159 VAGTDLAKNGLELESVAITDLedennyldalgRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEqereiETAR 238

                        250
                 ....*....|....*....
gi 487978515 209 ASRRDAEAQVVLAEASQKA 227
Cdd:COG2268  239 IAEAEAELAKKKAEERREA 257
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 50-169 1.44e-07

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: 49.81  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  50 FVIPYIDDVAYkVTTKDIVLDIPSQEVITRDNAVLLMNAVAYINL-TTPEKAVYGIENY----TWAIQNLVQT----SLR 120
Cdd:cd03399    1 FVIPFLQRVQR-LSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVgSDPEEIAAAAERFlgksTEEIRELVKEtlegHLR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 487978515 121 SIVGEMDLDDALSSRDHIKAKLKAAISDDISDWGITLKTVEIQDIQPSS 169
Cdd:cd03399   80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDN 128
PRK10930 PRK10930
FtsH protease activity modulator HflK;
4-167 1.32e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.97  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515   4 GTIIVLAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKYHSTLNPGLNFVIPYIDDVAyKVTTKDIVLDIPSQEVITRDNAV 83
Cdd:PRK10930  78 GRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVK-PVNVEAVRELAASGVMLTSDENV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  84 LL--MNaVAYiNLTTPEKAVYGIENYTWAIQNLVQTSLRSIVGEMDLDDALSS-RDHIKAKLKAAISDDIS--DWGITLK 158
Cdd:PRK10930 157 VRveMN-VQY-RVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRpyDMGITLL 234


                 ....*....
gi 487978515 159 TVEIQDIQP 167
Cdd:PRK10930 235 DVNFQAARP 243
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 15-165 4.07e-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: 43.70  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487978515  15 VAVTIFKGVRIVPQGYKWIVQRLGKYHSTLN-PGLNFVIPYIddVAYKVTTKDIVLDIPSQEVITRDNAVLLMNAVAYIN 93
Cdd:cd03402    2 VGIILLGGFFVVQPNEAAVLTLFGRYRGTVRrPGLRWVNPFY--RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487978515  94 LTTPEKAVYGIENYTWAIQNLVQTSLRSIVG----EMDLDDALSSRDH---IKAKLKAAISDDISDWGITLKTVEIQDI 165
Cdd:cd03402   80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASrypyDSFEDGEPSLRGNsdeVSEELRRELQERLAVAGVEVIEARITHL 158
PRK11029 PRK11029
protease modulator HflC;
7-58 8.32e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 37.41  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 487978515   7 IVLAFLAFVAVTIFKGVRIVPQGYKWIVQRLGKY-----HSTL--NPGLNFVIPYIDDV 58
Cdd:PRK11029   4 SVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVlrdddNKPLvyAPGLHFKIPFIETV 62
 
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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