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Conserved domains on  [gi|255725480|ref|XP_002547669|]
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predicted protein [Candida tropicalis MYA-3404]

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
TCDB:  8.A.21

Graphical summary

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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 ...
48-188 2.73e-39

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 135.35  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRsVHSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNID 127
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVR-KVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255725480 128 DVDFAINELCQTRMRTEIGNLKFDDVV-KNRNELNEKIKDFINSAsLENWGVECIRYEIKDI 188
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEA-LDPYGIEVVDVEIKDI 163
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
48-188 2.73e-39

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 135.35  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRsVHSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNID 127
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVR-KVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255725480 128 DVDFAINELCQTRMRTEIGNLKFDDVV-KNRNELNEKIKDFINSAsLENWGVECIRYEIKDI 188
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEA-LDPYGIEVVDVEIKDI 163
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
81-189 1.53e-38

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: 127.98  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  81 RSVHSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNEL 160
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80
                         90       100
                 ....*....|....*....|....*....
gi 255725480 161 NEKIKDFINSASlENWGVECIRYEIKDIS 189
Cdd:cd08829   81 NAKLLEALDEAT-DPWGVKVTRVEIKDIT 108
PHB smart00244
prohibitin homologues; prohibitin homologues
44-189 2.12e-28

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 103.89  E-value: 2.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480    44 ILNFVPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKAT 123
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKV-DLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255725480   124 YNIDDVDFA-INELCQTRMRTEIGNLKFDDVV-KNRNELNEKIKDFINSAsLENWGVECIRYEIKDIS 189
Cdd:smart00244  81 YRVLDADYAvIEQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEA-AEAWGIKVEDVEIKDIR 147
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
48-189 3.80e-24

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: 93.15  E-value: 3.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480   48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKIL--DTFKATYN 125
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255725480  126 I---DDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFINSAsLENWGVECIRYEIKDIS 189
Cdd:pfam01145  82 VfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEE-LAKYGVEIIDVQITDID 147
PRK11029 PRK11029
protease modulator HflC;
47-172 7.29e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 45.12  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  47 FVPQQ-QQWVIERMGKYNRTVKEGP-------HLIIPIFEKIRSVHSiKESVLEIQPHNCITIDQKDLIIDgvAFIK--I 116
Cdd:PRK11029  21 FVVKEgERGIVLRFGKVLRDDDNKPlvyapglHFKIPFIETVKMLDA-RIQTMDNQADRFVTKEKKDLIVD--SYIKwrI 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255725480 117 LDtFKATY------NIDDVDFAINELCQTRMRTEIGNLKFDDVVKN-RNELNEKIKDFINSAS 172
Cdd:PRK11029  98 SD-FSRYYlatgggDISQAEVLLKRKFSDRLRSEIGRLDVKDIVTDsRGRLTLDVRDALNSGS 159
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
48-188 2.73e-39

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 135.35  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRsVHSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNID 127
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVR-KVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255725480 128 DVDFAINELCQTRMRTEIGNLKFDDVV-KNRNELNEKIKDFINSAsLENWGVECIRYEIKDI 188
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEA-LDPYGIEVVDVEIKDI 163
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
81-189 1.53e-38

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: 127.98  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  81 RSVHSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNEL 160
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80
                         90       100
                 ....*....|....*....|....*....
gi 255725480 161 NEKIKDFINSASlENWGVECIRYEIKDIS 189
Cdd:cd08829   81 NAKLLEALDEAT-DPWGVKVTRVEIKDIT 108
PHB smart00244
prohibitin homologues; prohibitin homologues
44-189 2.12e-28

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 103.89  E-value: 2.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480    44 ILNFVPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKAT 123
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKV-DLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255725480   124 YNIDDVDFA-INELCQTRMRTEIGNLKFDDVV-KNRNELNEKIKDFINSAsLENWGVECIRYEIKDIS 189
Cdd:smart00244  81 YRVLDADYAvIEQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEA-AEAWGIKVEDVEIKDIR 147
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
48-189 3.10e-26

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: 100.00  E-value: 3.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNID 127
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255725480 128 DVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFINSASlENWGVECIRYEIKDIS 189
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVA-KEWGVYVESILIKDIV 148
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
48-189 3.80e-24

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: 93.15  E-value: 3.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480   48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKIL--DTFKATYN 125
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255725480  126 I---DDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFINSAsLENWGVECIRYEIKDIS 189
Cdd:pfam01145  82 VfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEE-LAKYGVEIIDVQITDID 147
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
86-189 8.31e-17

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: 72.22  E-value: 8.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  86 IKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIK 165
Cdd:cd13434    3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82
                         90       100
                 ....*....|....*....|....
gi 255725480 166 DFINSASLEnWGVECIRYEIKDIS 189
Cdd:cd13434   83 EILDEATDP-WGIKVERVEIKDII 105
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
75-188 3.07e-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 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: 72.55  E-value: 3.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  75 PIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVV 154
Cdd:cd08826    1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 255725480 155 KNRNELNEKIKDFINSASlENWGVECIRYEIKDI 188
Cdd:cd08826   80 SEREEINKRIQEIIDEQT-EPWGIKVTAVEIKDV 112
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
93-188 7.65e-13

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: 63.13  E-value: 7.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  93 IQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFINSAS 172
Cdd:cd08828   27 IPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQTLAQILAGREEIAHSIQSILDHAT 106
                         90
                 ....*....|....*.
gi 255725480 173 lENWGVECIRYEIKDI 188
Cdd:cd08828  107 -EKWGIKVARVEIKDV 121
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
48-188 1.83e-11

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 60.99  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLIIP-IFEKIRSVHSIKESVLEIQPHNC-----ITIDQKdlIIDgVAFI---KILD 118
Cdd:cd03404   18 VDPGERGVVLRFGKYVRTVGPGLHWKLPfPIEVVEKVNVTQVRSVEIGFRVPeeslmLTGDEN--IVD-VDFVvqyRISD 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255725480 119 TFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDV-VKNRNELNEKIKDFINsASLENW--GVECIRYEIKDI 188
Cdd:cd03404   95 PVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVlTEGRAEIAADVRELLQ-EILDRYdlGIEIVQVQLQDA 166
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
48-179 1.04e-10

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: 58.65  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKE-GPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDgvAFIK--ILDT---FK 121
Cdd:cd03405    5 VDETEQAVVLQFGKPVRVITEpGLHFKLPFIQNVRKF-DKRILTLDGPPEEVLTKDKKRLIVD--SYARwrITDPlrfYQ 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255725480 122 ATYNIDDVDFAINELCQTRMRTEIGNLKFDDVV-KNRNELNEKIKDFINSAsLENWGVE 179
Cdd:cd03405   82 SVGGEEGAESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEE-AKEYGIE 139
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
104-188 3.17e-09

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: 53.78  E-value: 3.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480 104 KDLI---IDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFINsASLENWGVEC 180
Cdd:cd13775   18 KDLVpvdVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIID-EKTTPWGITV 96

                 ....*...
gi 255725480 181 IRYEIKDI 188
Cdd:cd13775   97 QSVEIRDI 104
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
69-189 4.86e-09

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: 53.93  E-value: 4.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  69 GPHLIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEIGNL 148
Cdd:cd13435    8 GVFFVLPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTR 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 255725480 149 KFDDVVKNRNELNEKIKDFINSASlENWGVECIRYEIKDIS 189
Cdd:cd13435   87 NLSELLTERETISHSMQVTLDEAT-DPWGVQVERVEIKDVS 126
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
68-188 6.47e-09

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: 53.32  E-value: 6.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  68 EGPHL--IIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYNIDDVDFAINELCQTRMRTEI 145
Cdd:cd03403    5 KGPGLffILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVL 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 255725480 146 GNLKFDDVVKNRNELNEKIKDFINSASlENWGVECIRYEIKDI 188
Cdd:cd03403   84 GTKNLSEILSDRETISHQMQSTLDEAT-DPWGVKVERVEIKDV 125
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
48-188 3.10e-08

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: 51.82  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLIIPIFEKIRSVHSIKESVLEIqphNCITiDQKD---LIIDGVAFIKILDT--FKA 122
Cdd:cd03407    2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDV---RVET-KTKDnvfVTLVVSVQYRVVPEkvYDA 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255725480 123 TYNIDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFInSASLENWGVECIRYEIKDI 188
Cdd:cd03407   78 FYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEEL-AKVMSEYGYEIVKTLVTDI 142
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
48-188 8.71e-08

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: 50.27  E-value: 8.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKEGPHLI--IPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYN 125
Cdd:cd08827    7 VREYERAVIFRLGHLLQGRARGPGLFfyLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSS 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255725480 126 IDDVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFINSASLeNWGVECIRYEIKDI 188
Cdd:cd08827   86 FASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTC-RWGIKVERAEIKDV 147
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
88-189 3.63e-07

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: 46.59  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  88 ESVLEIQPHNCITIDQKDLIIDGVAFIKILDTF--KATYNIDDVDFAINELCQT---RMRTEIGNLKFDDVVKNRNELNE 162
Cdd:cd02106    2 PQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNalPAFYLVDFVKDIKADIRRKiadVLRAAIGRMTLDQIISGRDEIAK 81
                         90       100
                 ....*....|....*....|....*..
gi 255725480 163 KIKDFINSAsLENWGVECIRYEIKDIS 189
Cdd:cd02106   82 AVKEDLEED-LENFGVVISDVDITSIE 107
PRK11029 PRK11029
protease modulator HflC;
47-172 7.29e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 45.12  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  47 FVPQQ-QQWVIERMGKYNRTVKEGP-------HLIIPIFEKIRSVHSiKESVLEIQPHNCITIDQKDLIIDgvAFIK--I 116
Cdd:PRK11029  21 FVVKEgERGIVLRFGKVLRDDDNKPlvyapglHFKIPFIETVKMLDA-RIQTMDNQADRFVTKEKKDLIVD--SYIKwrI 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255725480 117 LDtFKATY------NIDDVDFAINELCQTRMRTEIGNLKFDDVVKN-RNELNEKIKDFINSAS 172
Cdd:PRK11029  98 SD-FSRYYlatgggDISQAEVLLKRKFSDRLRSEIGRLDVKDIVTDsRGRLTLDVRDALNSGS 159
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
58-189 2.10e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.09  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  58 RMGKYnRTVKEGPHLIIPIFEKIRSVhSIKESVLEIQPH-NCITIDQKDLIIDGVAFIKILDTFKATYN---------ID 127
Cdd:COG2268   42 RGGGY-KVVTGGGAFVLPVLHRAERM-SLSTMTIEVERTeGLITKDGIRVDVDAVFYVKVNSDPEDIANaaerflgrdPE 119
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255725480 128 DVDFAINELCQTRMRTEIGNLKFDDVVKNRNELNEKIKDFInSASLENWGVECIRYEIKDIS 189
Cdd:COG2268  120 EIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVA-GTDLAKNGLELESVAITDLE 180
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
72-189 2.80e-05

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: 42.11  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  72 LIIPIFEKIRSVhSIKESVLEIQPHNCITIDQKDLIIDGVAFIKILDTFKATYN---------IDDVDFAINELCQTRMR 142
Cdd:cd03399    1 FVIPFLQRVQRL-SLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAaaerflgksTEEIRELVKETLEGHLR 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 255725480 143 TEIGNLKFDDVVKNRNELNEKIKDFInSASLENWGVECIRYEIKDIS 189
Cdd:cd03399   80 AIVGTMTVEEIYQDREKFAEQVQEVA-EPDLAKMGLEIDSFNIKDIS 125
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
48-189 9.19e-04

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: 38.69  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255725480  48 VPQQQQWVIERMGKYNRTVKE-GPHLIIP------IFEKIRSVHSIKESVLEIQ--PhncitidqkdLIIDGVAFIKILD 118
Cdd:cd03402   13 VQPNEAAVLTLFGRYRGTVRRpGLRWVNPfyrkkrVSLRVRNFESEPLKVNDANgnP----------IEIAAVVVWRVVD 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255725480 119 TFKATYNIDDVDFAINELCQTRMRTEIGNLKFDDVVK-------NRNELNEKIKDFINSAsLENWGVECIRYEIKDIS 189
Cdd:cd03402   83 TAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFEDgepslrgNSDEVSEELRRELQER-LAVAGVEVIEARITHLA 159
 
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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