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Conserved domains on  [gi|221307584|ref|NP_001138303|]
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prohibitin-2 isoform 1 [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 ...
 40-235 8.43e-94

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: 275.55  E-value: 8.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  40 VFTVEGGHRAIFFNRiGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:cd03401    1 FYTVDAGEVGVVFRR-GKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 120 MYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA 199
Cdd:cd03401   80 LYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221307584 200 KQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAA 235
Cdd:cd03401  160 KQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 40-235 8.43e-94

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: 275.55  E-value: 8.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  40 VFTVEGGHRAIFFNRiGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:cd03401    1 FYTVDAGEVGVVFRR-GKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 120 MYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA 199
Cdd:cd03401   80 LYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221307584 200 KQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAA 235
Cdd:cd03401  160 KQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 39-201 2.74e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 122.38  E-value: 2.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584    39 SVFTVEGGHRAIFFNRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKIS-SPTGSKDLQMVNISLRVLSRpNAQEL 117
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   118 PSMYQRLglDYEERVLPSIVNEVLKSVVAKFNASQLIT-QRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAA 196
Cdd:smart00244  78 RAVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 221307584   197 VEAKQ 201
Cdd:smart00244 156 MEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 25-262 8.04e-31

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 116.48  E-value: 8.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  25 LLLGAGAVAYGVRESVFTVEGGHRAIFFnRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKI-SSPTGSKDLQMVN 103
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 104 ISLRVLSRPNaqELPSMYQRLGlDYEERVLPsIVNEVLKSVVAKFNASQLI-TQRAQVSLLIRRELTERAKDFSLILDDV 182
Cdd:COG0330   83 VDAVVQYRIT--DPAKFLYNVE-NAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 183 AITELSFSREYTAAVEAKQVAQQEAQRAQF-------------------LVEKAKQEQRQKIVQAEGEAEAAKMLGEALS 243
Cdd:COG0330  159 EIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYS 238

                        250
                 ....*....|....*....
gi 221307584 244 KNPGYIKLRKIRAAQNISK 262
Cdd:COG0330  239 AAPFVLFYRSLEALEEVLS 257
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-220 1.61e-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: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   41 FTVEGGHRAIFFNriGGVQQDTILAeGLHFRIPWFQYPIIYDIRARPRKISSPT-GSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:pfam01145   1 IIVPPGEVGVVTR--FGKLSRVLEP-GLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  120 MYQRL-GLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVE 198
Cdd:pfam01145  78 LVQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIE 157

                         170       180
                  ....*....|....*....|..
gi 221307584  199 AKQVAQQEAQRAqflVEKAKQE 220
Cdd:pfam01145 158 AKQTAEQEAEAE---IARAEAE 176
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 39-276 1.07e-10

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 61.34  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   39 SVFTVEGGHRAIFFnRIGGVQQD-----TILAEGLHFRIPWFQYPIIYDIR-----ARPRKIssPTGSKDLQMVNISlrv 108
Cdd:TIGR01932  19 PFFIIKEGERGIIT-RFGKILKDnnhhvLVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRI--PTKEKKDIIIDTY--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  109 lSRPNAQELPSMYQRLGLD---YEERVLPSIVNEVLKSVVAKFNASQLITQ-RAQVSLLIRRELTERA------------ 172
Cdd:TIGR01932  93 -IRWRIEDFKKYYLSTGGGtisAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNRGgkinkiamtitk 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  173 -----------------KDFSLILDDVAITELSFSREYTAAVEAKQVAQQEA----QRAQFLVEK--------------- 216
Cdd:TIGR01932 172 greilareisqiansqlKDIGIEVVDVRIKKINYSDELSESIYNRMRSEREQiarmHRSQGEEKAeeilgkaeyevrkil 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  217 AKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLrkIRAAQNISKTIATSQNRIYLTAD 276
Cdd:TIGR01932 252 SEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSF--WRSLEAYEKSFKDNQDEKVLSTD 309
PRK11029 PRK11029
protease modulator HflC;
39-277 1.73e-04

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 42.42  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  39 SVFTVEGGHRAIFFnRIGGVQQD-----TILAEGLHFRIPWFQYPIIYDIRARPR-----------------------KI 90
Cdd:PRK11029  19 SVFVVKEGERGIVL-RFGKVLRDddnkpLVYAPGLHFKIPFIETVKMLDARIQTMdnqadrfvtkekkdlivdsyikwRI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  91 SS------PTGSKDLQMVNIslrVLSRPNAQELPSMYQRLglDYEERV------LPSIVNEVLKS-------VVAKFNAS 151
Cdd:PRK11029  98 SDfsryylATGGGDISQAEV---LLKRKFSDRLRSEIGRL--DVKDIVtdsrgrLTLDVRDALNSgsagtedEVATPAAD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 152 QLITQRAQvsllirRELTERAKDFSLI-----------LDDVAITELSFSREYTAAVEAKQVAQQEA----QRAQFLVEK 216
Cdd:PRK11029 173 DAIASAAE------RVEAETKGKVPVInpnsmaalgieVVDVRIKQINLPTEVSDAIYNRMRAEREAvarrHRSQGQEEA 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307584 217 AK--------------QEQRQ-KIVQAEGEAEAAKMLGEALSKNPG-YIKLRKIRAAQNiskTIATSQNRIYLTADN 277
Cdd:PRK11029 247 EKlratadyevtrtlaEAERQgRIMRGEGDAEAAKLFADAFSQDPDfYAFIRSLRAYEN---SFSGNQDVMVLSPDS 320
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 40-235 8.43e-94

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: 275.55  E-value: 8.43e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  40 VFTVEGGHRAIFFNRiGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:cd03401    1 FYTVDAGEVGVVFRR-GKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 120 MYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA 199
Cdd:cd03401   80 LYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 221307584 200 KQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAA 235
Cdd:cd03401  160 KQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 39-201 2.74e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 122.38  E-value: 2.74e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584    39 SVFTVEGGHRAIFFNRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKIS-SPTGSKDLQMVNISLRVLSRpNAQEL 117
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   118 PSMYQRLglDYEERVLPSIVNEVLKSVVAKFNASQLIT-QRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAA 196
Cdd:smart00244  78 RAVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 221307584   197 VEAKQ 201
Cdd:smart00244 156 MEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 25-262 8.04e-31

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 116.48  E-value: 8.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  25 LLLGAGAVAYGVRESVFTVEGGHRAIFFnRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKI-SSPTGSKDLQMVN 103
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 104 ISLRVLSRPNaqELPSMYQRLGlDYEERVLPsIVNEVLKSVVAKFNASQLI-TQRAQVSLLIRRELTERAKDFSLILDDV 182
Cdd:COG0330   83 VDAVVQYRIT--DPAKFLYNVE-NAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 183 AITELSFSREYTAAVEAKQVAQQEAQRAQF-------------------LVEKAKQEQRQKIVQAEGEAEAAKMLGEALS 243
Cdd:COG0330  159 EIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYS 238

                        250
                 ....*....|....*....
gi 221307584 244 KNPGYIKLRKIRAAQNISK 262
Cdd:COG0330  239 AAPFVLFYRSLEALEEVLS 257
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-220 1.61e-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: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   41 FTVEGGHRAIFFNriGGVQQDTILAeGLHFRIPWFQYPIIYDIRARPRKISSPT-GSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:pfam01145   1 IIVPPGEVGVVTR--FGKLSRVLEP-GLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  120 MYQRL-GLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVE 198
Cdd:pfam01145  78 LVQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIE 157

                         170       180
                  ....*....|....*....|..
gi 221307584  199 AKQVAQQEAQRAqflVEKAKQE 220
Cdd:pfam01145 158 AKQTAEQEAEAE---IARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 39-246 3.38e-14

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: 70.59  E-value: 3.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  39 SVFTVEGGHRAIFFnRIGGVQQdTILAEGLHFRIPWFQYPIIYDIR-----ARPRKIssPTgsKDLQMVNISLRVLSRPN 113
Cdd:cd03405    1 SVFIVDETEQAVVL-QFGKPVR-VITEPGLHFKLPFIQNVRKFDKRiltldGPPEEV--LT--KDKKRLIVDSYARWRIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 114 AQELpsMYQRLGLDYE-ERVLPSIVNEVLKSVVAKFNASQLI-TQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSR 191
Cdd:cd03405   75 DPLR--FYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPE 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307584 192 EYTAAV------EAKQVAQQ----------------EAQRAQFLVEKAKQEQRQKivqAEGEAEAAKMLGEALSKNP 246
Cdd:cd03405  153 EVSESVyermraERERIAAEyraegeeeaekiraeaDRERTVILAEAYREAEEIR---GEGDAEAARIYAEAYGKDP 226
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 39-276 1.07e-10

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 61.34  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   39 SVFTVEGGHRAIFFnRIGGVQQD-----TILAEGLHFRIPWFQYPIIYDIR-----ARPRKIssPTGSKDLQMVNISlrv 108
Cdd:TIGR01932  19 PFFIIKEGERGIIT-RFGKILKDnnhhvLVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRI--PTKEKKDIIIDTY--- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  109 lSRPNAQELPSMYQRLGLD---YEERVLPSIVNEVLKSVVAKFNASQLITQ-RAQVSLLIRRELTERA------------ 172
Cdd:TIGR01932  93 -IRWRIEDFKKYYLSTGGGtisAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNRGgkinkiamtitk 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  173 -----------------KDFSLILDDVAITELSFSREYTAAVEAKQVAQQEA----QRAQFLVEK--------------- 216
Cdd:TIGR01932 172 greilareisqiansqlKDIGIEVVDVRIKKINYSDELSESIYNRMRSEREQiarmHRSQGEEKAeeilgkaeyevrkil 251

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  217 AKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLrkIRAAQNISKTIATSQNRIYLTAD 276
Cdd:TIGR01932 252 SEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSF--WRSLEAYEKSFKDNQDEKVLSTD 309
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 91-189 1.77e-09

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: 54.29  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  91 SSPTGSKDLQMVNISLRVLSRP-NAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELT 169
Cdd:cd02106    9 VEPVGTADGVPVAVDLVVQFRItDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLE 88

                         90       100
                 ....*....|....*....|
gi 221307584 170 ERAKDFSLILDDVAITELSF 189
Cdd:cd02106   89 EDLENFGVVISDVDITSIEP 108
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 140-261 4.02e-08

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: 52.13  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 140 VLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVeAKQVaqqEAQRaqflvekakq 219
Cdd:cd08826   65 TLRSVVGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAM-ARQA---EAER---------- 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 221307584 220 EQRQKIVQAEGEAEAAKMLGEA---LSKNPGYIKLRKIRAAQNIS 261
Cdd:cd08826  131 ERRAKIIKAEGELQAAEKLAEAaeiLAKSPGALQLRYLQTLSEIA 175
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 141-261 4.30e-08

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: 52.39  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 141 LKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSreytAAVEAKQVAQQEAQRaqflvekakqE 220
Cdd:cd13435   79 LRNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLP----DSLQRAMAAEAEAAR----------E 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 221307584 221 QRQKIVQAEGEAEAAKMLGEA---LSKNPGYIKLRKIRAAQNIS 261
Cdd:cd13435  145 ARAKVIAAEGEMKSSRALKEAsdiISASPSALQLRYLQTLSSIS 188
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 59-242 6.63e-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: 52.59  E-value: 6.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  59 QQDTILAEGLHFRIPWFQYpIIYDIRARPRKISS--PTGSKDLQMVNISLRVLSRPNAQELPSMYQRLglDYEERVLPSI 136
Cdd:cd03407   15 KFSRIAEPGLHFIIPPIES-VAGRVSLRVQQLDVrvETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL--TNPEQQIQSY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 137 VNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQflvEK 216
Cdd:cd03407   92 VFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAE---EK 168

                        170       180
                 ....*....|....*....|....*.
gi 221307584 217 AKQEQRQKIVQAEGEAEAAKMLGEAL 242
Cdd:cd03407  169 AEAEKILQVKAAEAEAEAKRLQGVGI 194
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 25-241 1.76e-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: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  25 LLLGAGAVAYGVrESVFTVEGGHRAIFFnRIGGVQqdTILAEGLHFRIPW-FQYPIIYDIrARPRKISSPTG-------- 95
Cdd:cd03404    1 LILLLLLLVWLL-SGFYTVDPGERGVVL-RFGKYV--RTVGPGLHWKLPFpIEVVEKVNV-TQVRSVEIGFRvpeeslml 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  96 SKDLQMVNISLRVlsrpnaqelpsMYQ-RLGLDY------EERVLPSIVNEVLKSVVAKFNASQLIT-QRAQVSLLIRRE 167
Cdd:cd03404   76 TGDENIVDVDFVV-----------QYRiSDPVAYlfnvrdPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVREL 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221307584 168 LTERAKDFSL--ILDDVAITELSFSREYTAAVEAKQVAQQEAQRaqfLVEKAKQEQRQKIVQAEGeaEAAKMLGEA 241
Cdd:cd03404  145 LQEILDRYDLgiEIVQVQLQDADPPEEVQDAFDDVNAARQDKER---LINEAQAYANEVIPRARG--EAARIIQEA 215
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 40-258 3.32e-05

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 44.31  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584   40 VFTVEGGHRAIFFnRIGgvQQDTILAEGLHFRIPWFQYPIIYDIRA-RPRKISSPTGSKDLQMVNISLRVLSRPNAqelP 118
Cdd:TIGR01933   1 IYTIGEAERGVVL-RFG--KYHRTVDPGLNWKPPFIEEVYPVNVTAvRNLRKQGLMLTGDENIVNVEMNVQYRITD---P 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  119 SMYqRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQ-RAQVSLLIRRELTE--RAKDFSLILDDVAITELSFSREYTA 195
Cdd:TIGR01933  75 YKY-LFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEiiDNYDLGITVTDVNFQSARPPEEVKE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221307584  196 AVEAKQVAQQEAQRaqfLVEKAKQEQRQKIVQAEGEAEaaKMLGEALsknpGYiKLRKIRAAQ 258
Cdd:TIGR01933 154 AFDDVIIAREDEER---YINEAEAYANEVVPKARGDAQ--RIIEEAR----GY-KERRINRAK 206
PRK11029 PRK11029
protease modulator HflC;
39-277 1.73e-04

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 42.42  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  39 SVFTVEGGHRAIFFnRIGGVQQD-----TILAEGLHFRIPWFQYPIIYDIRARPR-----------------------KI 90
Cdd:PRK11029  19 SVFVVKEGERGIVL-RFGKVLRDddnkpLVYAPGLHFKIPFIETVKMLDARIQTMdnqadrfvtkekkdlivdsyikwRI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  91 SS------PTGSKDLQMVNIslrVLSRPNAQELPSMYQRLglDYEERV------LPSIVNEVLKS-------VVAKFNAS 151
Cdd:PRK11029  98 SDfsryylATGGGDISQAEV---LLKRKFSDRLRSEIGRL--DVKDIVtdsrgrLTLDVRDALNSgsagtedEVATPAAD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 152 QLITQRAQvsllirRELTERAKDFSLI-----------LDDVAITELSFSREYTAAVEAKQVAQQEA----QRAQFLVEK 216
Cdd:PRK11029 173 DAIASAAE------RVEAETKGKVPVInpnsmaalgieVVDVRIKQINLPTEVSDAIYNRMRAEREAvarrHRSQGQEEA 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221307584 217 AK--------------QEQRQ-KIVQAEGEAEAAKMLGEALSKNPG-YIKLRKIRAAQNiskTIATSQNRIYLTADN 277
Cdd:PRK11029 247 EKlratadyevtrtlaEAERQgRIMRGEGDAEAAKLFADAFSQDPDfYAFIRSLRAYEN---SFSGNQDVMVLSPDS 320
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 48-261 1.77e-04

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: 41.80  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584  48 RAIFFnRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKIS-SPTGSKDLQMVNISLrvlsrpnaqelpSMYQRLgl 126
Cdd:cd08827   12 RAVIF-RLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPfHMIVTKDLVCTEIDA------------ICYYRI-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 127 dyeervlpSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA---KQVA 203
Cdd:cd08827   77 --------ENASVCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERaeiKDVN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221307584 204 QQEAQRAQFLVEKAKQEQRQ-KIVQAEGE---AEAAKMLGEALSKNPGYIKLRKIRAAQNIS 261
Cdd:cd08827  149 LPPELQHSFAVEAEAQRQAKvKVIAAEGEkaaSEALKAAAESLSGSPLAMQLRYLHTLQSLR 210
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 141-261 7.92e-04

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: 39.84  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 141 LKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSreytaaveakqvaqQEAQRAQFLVEKAKQE 220
Cdd:cd03403   79 LRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLP--------------VQLQRAMAAEAEAARE 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 221307584 221 QRQKIVQAEGEAEAAKMLGEA---LSKNPGYIKLRKIRAAQNIS 261
Cdd:cd03403  145 ARAKVIAAEGEQNASRALKEAadvISESPAALQLRYLQTLNTIS 188
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 141-254 2.53e-03

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: 37.99  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 141 LKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFslilddvAITELSfsreytaaVEAKQVA-QQEAQRAQFLVEKAKQ 219
Cdd:cd13775   58 LRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW-------GITVQS--------VEIRDIIiPKELQDAMSREAQAER 122

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 221307584 220 EQRQKIVQAEGEAEAAKMLGEA---LSKNPGYIKLRKI 254
Cdd:cd13775  123 EKNARVILAEAEKEIAEMFVEAaevYENNPIALQLRAM 160
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
139-236 3.49e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 139 EVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQfLVEKAK 218
Cdd:COG2268  131 GALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARI-AEAEAE 209

                         90
                 ....*....|....*...
gi 221307584 219 QEQRQKIVQAEGEAEAAK 236
Cdd:COG2268  210 RETEIAIAQANREAEEAE 227
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 140-263 5.47e-03

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: 37.59  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 140 VLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSreytaaveakqvaqQEAQRAQFLVEKAKQ 219
Cdd:cd13437  100 TLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLS--------------KDLQQSLSSAAKAKR 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 221307584 220 EQRQKIVQAEGEAEAAKMLGEA---LSKNPGyIKLRKIRAAQNISKT 263
Cdd:cd13437  166 IGESKIISAKADVESAKLMREAadiLDSKAA-MQIRYLETLQAIAKS 211
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 141-264 5.87e-03

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


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 37.13  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221307584 141 LKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAA----VEAKQVAQqeAQraqflVEK 216
Cdd:cd13438   95 LREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREIlnqvLEAEKRAQ--AN-----LIR 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 221307584 217 AkqeqRQKIVQAEGEAEAAKMLGEalskNPGYIKLRKIRAAQNISKTI 264
Cdd:cd13438  168 A----REETAATRSLLNAAKLMEE----NPALLRLRELEALEKIAEKV 207
 
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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