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Conserved domains on  [gi|527498282|ref|NP_001268426|]
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prohibitin 1 isoform 2 [Homo sapiens]

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 ...
 27-141 3.45e-52

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: 164.22  E-value: 3.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 527498282 107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYT 115
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-141 3.45e-52

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: 164.22  E-value: 3.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 527498282 107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYT 115
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-141 1.09e-23

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 90.41  E-value: 1.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282    26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 527498282   105 RIFTSigEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLT 113
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-141 6.88e-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: 70.43  E-value: 6.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282   30 VDAGHRAVIFdRFrGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVASQLPRIFT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 527498282  109 SI-GEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLS 114
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-141 6.88e-15

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 69.48  E-value: 6.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282  12 FGLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNV 88
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR-TLEPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 527498282  89 NITLRILFRPVasQLPRIFTSIgEDYDERVLPsITTEILKSVVARFDAGELIT 141
Cdd:COG0330   82 DVDAVVQYRIT--DPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLS 130
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-141 3.45e-52

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: 164.22  E-value: 3.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 527498282 107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYT 115
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-141 1.09e-23

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 90.41  E-value: 1.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282    26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 527498282   105 RIFTSigEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLT 113
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-141 6.88e-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: 70.43  E-value: 6.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282   30 VDAGHRAVIFdRFrGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVASQLPRIFT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 527498282  109 SI-GEDYDERVLPSITTEILKSVVARFDAGELIT 141
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLS 114
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-141 6.88e-15

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 69.48  E-value: 6.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282  12 FGLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNV 88
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR-TLEPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 527498282  89 NITLRILFRPVasQLPRIFTSIgEDYDERVLPsITTEILKSVVARFDAGELIT 141
Cdd:COG0330   82 DVDAVVQYRIT--DPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLS 130
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 26-141 2.85e-05

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: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527498282  26 ALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFR--- 97
Cdd:cd03405    1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWRitd 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 527498282  98 PVasqlpRIFTSIGEDYD-ERVLPSITTEILKSVVARFDAGELIT 141
Cdd:cd03405   76 PL-----RFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVS 115
 
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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