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Conserved domains on  [gi|1859653128|ref|YP_009841410|]
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lipoprotein [Escherichia phage fp01]

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 ...
 21-252 1.85e-20

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.13  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  21 KRWGIGAAVGLVGLVLALNSYTVVQDGTVKTQTFLGKVDpSPVLPGFHIVNPFasFDT---FSTKDIALKLDKLQVPSQD 97
Cdd:COG0330     1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV-RTLEPGLHFKIPF--IDRvrkVDVREQVLDVPPQEVLTKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  98 KFKSTVDLTVMLQFDGSKAPINRInagtqdQALDKYVTEKLLSTIRE-FGKSvpKAQDLFDAKiQAQLQTAIQQEVEEYA 176
Cdd:COG0330    78 NNIVDVDAVVQYRITDPAKFLYNV------ENAEEALRQLAESALREvIGKM--TLDEVLSTG-RDEINAEIREELQEAL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 177 RPYGYTVKQVFLQDITLPPVI---MEQVQNTKV-REEQVNAAKAE----LARVEQEAQQKVKQAEADREARNNQAianER 248
Cdd:COG0330   149 DPYGIEVVDVEIKDIDPPEEVqdaMEDRMKAEReREAAILEAEGYreaaIIRAEGEAQRAIIEAEAYREAQILRA---EG 225


                  ....
gi 1859653128 249 DADA 252
Cdd:COG0330   226 EAEA 229
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 21-252 1.85e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.13  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  21 KRWGIGAAVGLVGLVLALNSYTVVQDGTVKTQTFLGKVDpSPVLPGFHIVNPFasFDT---FSTKDIALKLDKLQVPSQD 97
Cdd:COG0330     1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV-RTLEPGLHFKIPF--IDRvrkVDVREQVLDVPPQEVLTKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  98 KFKSTVDLTVMLQFDGSKAPINRInagtqdQALDKYVTEKLLSTIRE-FGKSvpKAQDLFDAKiQAQLQTAIQQEVEEYA 176
Cdd:COG0330    78 NNIVDVDAVVQYRITDPAKFLYNV------ENAEEALRQLAESALREvIGKM--TLDEVLSTG-RDEINAEIREELQEAL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 177 RPYGYTVKQVFLQDITLPPVI---MEQVQNTKV-REEQVNAAKAE----LARVEQEAQQKVKQAEADREARNNQAianER 248
Cdd:COG0330   149 DPYGIEVVDVEIKDIDPPEEVqdaMEDRMKAEReREAAILEAEGYreaaIIRAEGEAQRAIIEAEAYREAQILRA---EG 225


                  ....
gi 1859653128 249 DADA 252
Cdd:COG0330   226 EAEA 229
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 41-238 1.03e-18

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: 82.18  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  41 YTVVQDGTVKTQTFLGKVDPSPVL-PGFHIVNPFA-SFDTFSTKDIALKLdKLQVPSQDKFKSTVDLTVMLQFDGSKAPI 118
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLgEGLHFKIPWIqVVIIYDVRTQPREI-TLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 119 NRINAGTQdqaldkYVTEKLLSTIREFGKSVP---KAQDLFdaKIQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPP 195
Cdd:cd03401    80 LYQNLGPD------YEERVLPPIVREVLKAVVaqyTAEELY--TKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPD 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1859653128 196 VIMEQVQNTKVREEQVNAAKAELARVEQEAQQKVKQAEADREA 238
Cdd:cd03401   152 EYEKAIEAKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEA 194
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 62-225 9.49e-16

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: 73.89  E-value: 9.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  62 PVLPGFHIVNPF-ASFDTFSTKDIALKLDKLQVPSQDKFKSTVDLTVMLQFDGSKAPI---NRINAGTQDQALDKYVTEK 137
Cdd:pfam01145  20 VLEPGLHFIIPFiQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKlvqNVFGSDDLQELLRRVLESA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 138 LLSTIREFgksvpKAQDLFDAkiQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPPVIMEQVQNTKVREEQvnaAKAE 217
Cdd:pfam01145 100 LREIIARY-----TLEELLSN--REELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQE---AEAE 169


                  ....*...
gi 1859653128 218 LARVEQEA 225
Cdd:pfam01145 170 IARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 55-202 4.45e-04

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 39.95  E-value: 4.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128   55 LGKVDpSPVLPGFHIVNPFasfdTFSTKDIALKLDKLQVPSQ-----DKFKSTVDLTVMLQFDGSKAPINRINaGTQDQA 129
Cdd:smart00244  17 LGRVL-RVLGPGLHFLIPF----IDDVKKVDLRAQTDDVPPQetitkDNVKVSVDAVVYYRVLDPLRAVYRVL-DADYAV 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859653128  130 LDKYVTEKLLSTIREFgksvpKAQDLFDAKiQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPPVIMEQVQ 202
Cdd:smart00244  91 IEQLAQTTLRSVIGKR-----TLDELLTDQ-REKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAME 157
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 21-252 1.85e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.13  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  21 KRWGIGAAVGLVGLVLALNSYTVVQDGTVKTQTFLGKVDpSPVLPGFHIVNPFasFDT---FSTKDIALKLDKLQVPSQD 97
Cdd:COG0330     1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV-RTLEPGLHFKIPF--IDRvrkVDVREQVLDVPPQEVLTKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  98 KFKSTVDLTVMLQFDGSKAPINRInagtqdQALDKYVTEKLLSTIRE-FGKSvpKAQDLFDAKiQAQLQTAIQQEVEEYA 176
Cdd:COG0330    78 NNIVDVDAVVQYRITDPAKFLYNV------ENAEEALRQLAESALREvIGKM--TLDEVLSTG-RDEINAEIREELQEAL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 177 RPYGYTVKQVFLQDITLPPVI---MEQVQNTKV-REEQVNAAKAE----LARVEQEAQQKVKQAEADREARNNQAianER 248
Cdd:COG0330   149 DPYGIEVVDVEIKDIDPPEEVqdaMEDRMKAEReREAAILEAEGYreaaIIRAEGEAQRAIIEAEAYREAQILRA---EG 225


                  ....
gi 1859653128 249 DADA 252
Cdd:COG0330   226 EAEA 229
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 41-238 1.03e-18

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: 82.18  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  41 YTVVQDGTVKTQTFLGKVDPSPVL-PGFHIVNPFA-SFDTFSTKDIALKLdKLQVPSQDKFKSTVDLTVMLQFDGSKAPI 118
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLgEGLHFKIPWIqVVIIYDVRTQPREI-TLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 119 NRINAGTQdqaldkYVTEKLLSTIREFGKSVP---KAQDLFdaKIQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPP 195
Cdd:cd03401    80 LYQNLGPD------YEERVLPPIVREVLKAVVaqyTAEELY--TKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPD 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1859653128 196 VIMEQVQNTKVREEQVNAAKAELARVEQEAQQKVKQAEADREA 238
Cdd:cd03401   152 EYEKAIEAKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEA 194
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 62-225 9.49e-16

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: 73.89  E-value: 9.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  62 PVLPGFHIVNPF-ASFDTFSTKDIALKLDKLQVPSQDKFKSTVDLTVMLQFDGSKAPI---NRINAGTQDQALDKYVTEK 137
Cdd:pfam01145  20 VLEPGLHFIIPFiQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKlvqNVFGSDDLQELLRRVLESA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 138 LLSTIREFgksvpKAQDLFDAkiQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPPVIMEQVQNTKVREEQvnaAKAE 217
Cdd:pfam01145 100 LREIIARY-----TLEELLSN--REELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQE---AEAE 169


                  ....*...
gi 1859653128 218 LARVEQEA 225
Cdd:pfam01145 170 IARAEAEA 177
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 39-238 9.43e-08

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: 51.85  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  39 NSYTVVQDGTVKTQTFLGKVDPSpVLPGFHIVNPFAsfDTFSTKDIALK---LDKLQVPSQDKFKSTVDLTVMLQFDGSK 115
Cdd:cd13437     4 NPYKQVKQGSVGLVERFGKFYKT-VDPGLHKVNPCT--EKIIQVDMKTQvidLPRQSVMTKDNVSVTIDSVVYYRIIDPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 116 APINRINAgtqdqaLDKYVTEKLLSTIREF-GKSVpkAQDLFDAKIQAQLQtaIQQEVEEYARPYGYTVKQVFLQDITLP 194
Cdd:cd13437    81 KAIYRIDN------VKQALIERTQTTLRSViGERT--LQDLLEKREEIADE--IEEIVEEVAKEWGVYVESILIKDIVLS 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1859653128 195 PVIMEQVQntkvreeqvNAAKAelarvEQEAQQKVKQAEADREA 238
Cdd:cd13437   151 KDLQQSLS---------SAAKA-----KRIGESKIISAKADVES 180
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 65-250 1.41e-06

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: 48.74  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  65 PGFHIVNPFasFDTFStKDIALKLDKLQVPSQDKFKS--TVDLTVMLQFDGSKAPINR-----INAGTQDQAldkYVtek 137
Cdd:cd03407    22 PGLHFIIPP--IESVA-GRVSLRVQQLDVRVETKTKDnvFVTLVVSVQYRVVPEKVYDafyklTNPEQQIQS---YV--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 138 lLSTIRefgKSVPKA--QDLFDAKIQaqLQTAIQQEVEEYARPYGYTVKQVFLQDITLPPvimeqvqntKVRE--EQVNA 213
Cdd:cd03407    93 -FDVVR---ASVPKLtlDEVFESKDE--IAKAVKEELAKVMSEYGYEIVKTLVTDIEPDA---------SVKAamNEINA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1859653128 214 AKAELARVEQEAQ----QKVKQAEADREAR--NNQAIANERDA 250
Cdd:cd03407   158 AQRLREAAEEKAEaekiLQVKAAEAEAEAKrlQGVGIAEQRKA 200
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 158-243 2.02e-06

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: 48.28  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 158 AKIQAQLQTAIQQEVEEYArpYGYTVKQVFLQDITLPpvimEQVQN-----TKVREEQ---VNAAKAE----LARVEQEA 225
Cdd:cd03404   135 AEIAADVRELLQEILDRYD--LGIEIVQVQLQDADPP----EEVQDafddvNAARQDKerlINEAQAYanevIPRARGEA 208

                          90
                  ....*....|....*...
gi 1859653128 226 QQKVKQAEADREARNNQA 243
Cdd:cd03404   209 ARIIQEAEAYKAEVVARA 226
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 53-252 1.47e-04

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: 42.48  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  53 TFLGKVDPSPVLPGFHIVNPFA-SFDTFSTKDIALKLDKLQVPSQDKFKSTVDLTVM------LQFdgskapinRINAGT 125
Cdd:cd03405    14 LQFGKPVRVITEPGLHFKLPFIqNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARwritdpLRF--------YQSVGG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 126 QDQAldkyvtEKLLSTI------REFGKSvpKAQDLFDAKiQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPPVIME 199
Cdd:cd03405    86 EEGA------ESRLDDIvdsalrNEIGKR--TLAEVVSGG-RDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1859653128 200 QVQNtKVREEQVNAAKAELARVEQEAQQkvKQAEADREA--------RNNQAIANERDADA 252
Cdd:cd03405   157 SVYE-RMRAERERIAAEYRAEGEEEAEK--IRAEADRERtvilaeayREAEEIRGEGDAEA 214
PHB smart00244
prohibitin homologues; prohibitin homologues
 55-202 4.45e-04

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 39.95  E-value: 4.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128   55 LGKVDpSPVLPGFHIVNPFasfdTFSTKDIALKLDKLQVPSQ-----DKFKSTVDLTVMLQFDGSKAPINRINaGTQDQA 129
Cdd:smart00244  17 LGRVL-RVLGPGLHFLIPF----IDDVKKVDLRAQTDDVPPQetitkDNVKVSVDAVVYYRVLDPLRAVYRVL-DADYAV 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1859653128  130 LDKYVTEKLLSTIREFgksvpKAQDLFDAKiQAQLQTAIQQEVEEYARPYGYTVKQVFLQDITLPPVIMEQVQ 202
Cdd:smart00244  91 IEQLAQTTLRSVIGKR-----TLDELLTDQ-REKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAME 157
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 208-253 1.23e-03

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 37.80  E-value: 1.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1859653128 208 EEQVNAAKAELARVEQEAQQKVKQAEA---DREARNNQAIANERDADAK 253
Cdd:pfam16999  29 EREVEAAEAEAARILREAEAKAKALQAeyrQELAAETARIREEARARAE 77
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 65-288 4.99e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 38.05  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128  65 PGFHIVNPFasFDTFSTKDIALKLDKL-QVPSQDKFKstvdltVMLQFDGSKApINRinagtqdqaLDKyvtEKLLSTIR 143
Cdd:cd03406    32 PGYHLMLPF--LTTYESVQVTLQTDEVkNVPCGTSGG------VMIYFDRIEV-VNR---------LDK---ESVYDTVK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 144 EFGKSVPKA-----------Q------------DLFDaKIQAQLQTAIQQEVEEYArPyGYTVKQVFLQDITLPPVI--- 197
Cdd:cd03406    91 NYTVDYDKTwifdkihhelnQfcsvhtlqevyiDLFD-QIDENLKDALQADLNKMA-P-GLEIIAVRVTKPKIPEAIrrn 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859653128 198 ---MEQ--------VQNTKV--------REEQVNAAK--AELARVEQeaQQKVKQAEADR---EARNNQAIANERD-ADA 252
Cdd:cd03406   168 yeaMEAektklliaEQHQKVvekeaeteRKRAVIEAEkdAEVAKIQM--QQKIMEKEAEKkisEIEDEMHLAREKArADA 245

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1859653128 253 KLYAAKKEaeaNAALQRTITPEMirwkqLEVEMIRA 288
Cdd:cd03406   246 EYYRALRE---AEANKLKLTPEY-----LELKKYQA 273
 
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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