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Conserved domains on  [gi|1218458664|gb|OXH76104|]
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prohibitin-2 [Cryptococcus neoformans serotype A]

Protein Classification

prohibitin family protein( domain architecture ID 10130412)

prohibitin family protein similar to Homo sapiens prohibitin, a lipid raft-associated integral membrane protein that inhibits DNA synthesis and has a role in regulating proliferation

CATH:  3.30.479.30
Gene Ontology:  GO:0005743|GO:0035632|GO:0016020
PubMed:  31522117|17766116|10542406|16101677
SCOP:  4003722

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 65-259 8.62e-87

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: 258.60  E-value: 8.62e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  65 LFNVDGGHRAIKYSRLQGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNIASLTGTKDLQMVNITCRVLSRPSVNDLPTI 144
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 145 YRELGTDYDERVLPSIVNEVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAK 224
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1218458664 225 QVAQQIAQRAAFLVDQAIQEKQSIIVKAQGEARSA 259
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 65-259 8.62e-87

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: 258.60  E-value: 8.62e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  65 LFNVDGGHRAIKYSRLQGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNIASLTGTKDLQMVNITCRVLSRPSVNDLPTI 144
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 145 YRELGTDYDERVLPSIVNEVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAK 224
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1218458664 225 QVAQQIAQRAAFLVDQAIQEKQSIIVKAQGEARSA 259
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 64-225 1.47e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 115.84  E-value: 1.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664   64 SLFNVDGGHRAIKYSRLQGVKaDIYPEGTHLVLPWFEHPIIYDVRAKPRNI-ASLTGTKDLQMVNITCRVLSRpSVNDLP 142
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  143 TIYRELgtDYDERVLPSIVNEVLKSVVAQFNASQLIT-QREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAV 221
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 1218458664  222 EAKQ 225
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 50-301 1.88e-28

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 110.70  E-value: 1.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  50 AIGTLVVGAIALNYSLFNVDGGHRAIKYsRLqGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNI-ASLTGTKDLQMVNI 128
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RF-GKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 129 TCRVLSRpsVNDLPTIYRELgTDYDERVLPsIVNEVLKSVVAQFNASQLI-TQREMVSRLVRENLTRRARRFNLILDDVS 207
Cdd:COG0330    84 DAVVQYR--ITDPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 208 ITHVAFSPEFTHAVEAKQVAQQIAQRAAF-------------------LVDQAIQEKQSIIVKAQGEARSAELIGEAVKT 268
Cdd:COG0330   160 IKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSA 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1218458664 269 NKGFLQLRKLEAAREIAGtlaQSGNRVMLDAKS 301
Cdd:COG0330   240 APFVLFYRSLEALEEVLS---PNSKVIVLPPDG 269
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 68-235 2.40e-25

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: 99.70  E-value: 2.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  68 VDGGHRAIKYSrlQGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNIASLT-GTKDLQMVNITCRVLSRPSVNDLPTIYR 146
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 147 ELGT-DYDERVLPSIVNEVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAKQ 225
Cdd:pfam01145  81 NVFGsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170
                  ....*....|
gi 1218458664 226 VAQQIAQRAA 235
Cdd:pfam01145 161 TAEQEAEAEI 170
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 65-259 8.62e-87

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: 258.60  E-value: 8.62e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  65 LFNVDGGHRAIKYSRLQGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNIASLTGTKDLQMVNITCRVLSRPSVNDLPTI 144
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 145 YRELGTDYDERVLPSIVNEVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAK 224
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1218458664 225 QVAQQIAQRAAFLVDQAIQEKQSIIVKAQGEARSA 259
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 64-225 1.47e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 115.84  E-value: 1.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664   64 SLFNVDGGHRAIKYSRLQGVKaDIYPEGTHLVLPWFEHPIIYDVRAKPRNI-ASLTGTKDLQMVNITCRVLSRpSVNDLP 142
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  143 TIYRELgtDYDERVLPSIVNEVLKSVVAQFNASQLIT-QREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAV 221
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 1218458664  222 EAKQ 225
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 50-301 1.88e-28

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 110.70  E-value: 1.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  50 AIGTLVVGAIALNYSLFNVDGGHRAIKYsRLqGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNI-ASLTGTKDLQMVNI 128
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RF-GKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 129 TCRVLSRpsVNDLPTIYRELgTDYDERVLPsIVNEVLKSVVAQFNASQLI-TQREMVSRLVRENLTRRARRFNLILDDVS 207
Cdd:COG0330    84 DAVVQYR--ITDPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 208 ITHVAFSPEFTHAVEAKQVAQQIAQRAAF-------------------LVDQAIQEKQSIIVKAQGEARSAELIGEAVKT 268
Cdd:COG0330   160 IKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSA 239

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1218458664 269 NKGFLQLRKLEAAREIAGtlaQSGNRVMLDAKS 301
Cdd:COG0330   240 APFVLFYRSLEALEEVLS---PNSKVIVLPPDG 269
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 68-235 2.40e-25

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: 99.70  E-value: 2.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  68 VDGGHRAIKYSrlQGVKADIYPEGTHLVLPWFEHPIIYDVRAKPRNIASLT-GTKDLQMVNITCRVLSRPSVNDLPTIYR 146
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 147 ELGT-DYDERVLPSIVNEVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAKQ 225
Cdd:pfam01145  81 NVFGsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170
                  ....*....|
gi 1218458664 226 VAQQIAQRAA 235
Cdd:pfam01145 161 TAEQEAEAEI 170
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 106-213 1.16e-13

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: 66.23  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 106 DVRAKPRniasltGTKDLQMVNITCRVLSRPSV-NDLPTIYRELGTDYDERVLPSIVNEVLKSVVAQFNASQLITQREMV 184
Cdd:cd02106     6 DVRVEPV------GTADGVPVAVDLVVQFRITDyNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEI 79

                          90       100
                  ....*....|....*....|....*....
gi 1218458664 185 SRLVRENLTRRARRFNLILDDVSITHVAF 213
Cdd:cd02106    80 AKAVKEDLEEDLENFGVVISDVDITSIEP 108
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 64-284 3.58e-12

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: 65.20  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  64 SLFNVDGGHRAIKySRLQGVKADIYPEGTHLVLPWFEHPIIYDVR-----AKPRNIasLTGTKDLQMVNITCRVlsrpSV 138
Cdd:cd03405     1 SVFIVDETEQAVV-LQFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEV--LTKDKKRLIVDSYARW----RI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 139 NDLPTIYRELGTDYD-ERVLPSIVNEVLKSVVAQFNASQLI-TQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPE 216
Cdd:cd03405    74 TDPLRFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 217 FTHAV------EAKQVAQQI----AQRAAFLVDQAIQEKQSII---------VKAQGEARSAELIGEAVKTNKGFLQ-LR 276
Cdd:cd03405   154 VSESVyermraERERIAAEYraegEEEAEKIRAEADRERTVILaeayreaeeIRGEGDAEAARIYAEAYGKDPEFYSfYR 233


                  ....*...
gi 1218458664 277 KLEAAREI 284
Cdd:cd03405   234 SLEAYRAS 241
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 164-286 5.78e-07

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 48.66  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 164 VLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAveakqvaqqIAQRAaflvdQAIQ 243
Cdd:cd08826    65 TLRSVVGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRA---------MARQA-----EAER 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1218458664 244 EKQSIIVKAQGEARSAELIGEAVKT---NKGFLQLRKLEAAREIAG 286
Cdd:cd08826   131 ERRAKIIKAEGELQAAEKLAEAAEIlakSPGALQLRYLQTLSEIAS 176
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 91-286 1.57e-05

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: 45.07  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  91 GTHLVLPWFEHPIIYDVRAKPRNIASLTG-TKDLQMVNITCRVLSRPSvNDLPTIYRELGTDYDERVLPSIVnevLKSVV 169
Cdd:cd13435     8 GVFFVLPCIDNYCKVDLRTVSFDVPPQEVlTKDSVTVTVDAVVYYRIS-DPLNAVIQVANYSHSTRLLAATT---LRNVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 170 AQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAKQvaqqiaqraaflvdQAIQEKQSII 249
Cdd:cd13435    84 GTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEA--------------EAAREARAKV 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1218458664 250 VKAQGEARSAELIGEA---VKTNKGFLQLRKLEAAREIAG 286
Cdd:cd13435   150 IAAEGEMKSSRALKEAsdiISASPSALQLRYLQTLSSISG 189
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 62-287 1.51e-04

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: 42.22  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  62 NYSLFNVDGGHRAIkYSRLQGVKADIYPeGTHLVLPWFEHPIIYDVRAKPRNIASLTG-TKDLQMVNITCRVLSRpsVND 140
Cdd:cd13437     3 PNPYKQVKQGSVGL-VERFGKFYKTVDP-GLHKVNPCTEKIIQVDMKTQVIDLPRQSVmTKDNVSVTIDSVVYYR--IID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 141 LPT-IYRElgTDYDERVLpSIVNEVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTH 219
Cdd:cd13437    79 PYKaIYRI--DNVKQALI-ERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQ 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 220 AVEAKQVAQQIAqraaflvdqaiqekQSIIVKAQGEARSAELIGEA--VKTNKGFLQLRKLEAAREIAGT 287
Cdd:cd13437   156 SLSSAAKAKRIG--------------ESKIISAKADVESAKLMREAadILDSKAAMQIRYLETLQAIAKS 211
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 51-256 3.07e-03

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: 38.65  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664  51 IGTLVVGAIALNYSLFNVDGGHRAI-----KYSRLQGvkadiypEGTHLVLPW-FEHPIIYDVRA-------KPRNIASL 117
Cdd:cd03404     1 LILLLLLLVWLLSGFYTVDPGERGVvlrfgKYVRTVG-------PGLHWKLPFpIEVVEKVNVTQvrsveigFRVPEESL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 118 TGTKDLQMVNITCRVLSRpsVNDLptiyrelgTDY------DERVLPSIVNEVLKSVVAQFNASQLIT-QREMVSRLVRE 190
Cdd:cd03404    74 MLTGDENIVDVDFVVQYR--ISDP--------VAYlfnvrdPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 191 NLTRRARRFNL--ILDDVSITHV--------AFspeftHAV------------EAKQVAQQIAQRA----AFLVDQAIQE 244
Cdd:cd03404   144 LLQEILDRYDLgiEIVQVQLQDAdppeevqdAF-----DDVnaarqdkerlinEAQAYANEVIPRArgeaARIIQEAEAY 218

                         250
                  ....*....|..
gi 1218458664 245 KQSIIVKAQGEA 256
Cdd:cd03404   219 KAEVVARAEGDA 230
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
163-261 9.95e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 37.54  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218458664 163 EVLKSVVAQFNASQLITQREMVSRLVRENLTRRARRFNLILDDVSITHVAFSPEFTHAVEAKQVAQQIAQRAaflVDQAI 242
Cdd:COG2268   131 GALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDAR---IAEAE 207

                          90       100
                  ....*....|....*....|.
gi 1218458664 243 QEKQSIIVKAQG--EARSAEL 261
Cdd:COG2268   208 AERETEIAIAQAnrEAEEAEL 228
 
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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