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Conserved domains on  [gi|77736091|ref|NP_001029744|]
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prohibitin [Bos taurus]

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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 ...
27-221 6.61e-90

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  Cd Length: 195  Bit Score: 267.46  E-value: 6.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 77736091 187 QVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
13-231 8.69e-26

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


:

Pssm-ID: 223407 [Multi-domain]  Cd Length: 291  Bit Score: 102.91  E-value: 8.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  13 GLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNV------PVITGSKDLQ 86
Cdd:COG0330   7 IILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDNV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  87 NVNITLRILFRPVAsqlPRIFTSIGEDYDERvLPSITTEILKSVVARFDAGELITQREL-VSRQVSDDLTERAATFGLIL 165
Cdd:COG0330  86 IVSVDAVVQYRVTD---PQKAVYNVENAEAA-LRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77736091 166 DDVSLTHLTFGKEFTEAVEAKQVAQQEAERArfvVEKAEQQKKAAIISAEGDSKAAELIANSLATA 231
Cdd:COG0330 162 VDVEIKDIDPPEEVQAAMEKQMAAERDKRAE---ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
27-221 6.61e-90

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  Cd Length: 195  Bit Score: 267.46  E-value: 6.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 77736091 187 QVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
26-187 5.36e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581  Cd Length: 160  Bit Score: 124.70  E-value: 5.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091     26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091    105 RIFTSigEDYDERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 77736091    184 EAKQ 187
Cdd:smart00244 157 EAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
28-207 2.71e-29

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: 250396  Cd Length: 176  Bit Score: 110.14  E-value: 2.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091    28 YNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVASQLPrI 106
Cdd:pfam01145   1 VIVPPGEVGVVT-RFGKVSR-VLGPGLHFKLPFIQTITVVDTRLQTLEVTVQTvLTKDGVPVNVDVTVQYRVEDPPKL-V 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091   107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:pfam01145  78 ANVTGEDDLQELLRPLVESALREVIARYTLDELLSNREEIAQEVKEALNEELEKYGIEIEDVQITDIDLPPEIEEAIEEK 157
                         170       180
                  ....*....|....*....|.
gi 77736091   187 QVAQQEAERARfvVEKAEQQK 207
Cdd:pfam01145 158 QAAEQEAEEAE--IERAEAEA 176
PRK11029 PRK11029
FtsH protease regulator HflC; Provisional
181-245 4.33e-03

FtsH protease regulator HflC; Provisional


Pssm-ID: 182913  Cd Length: 334  Bit Score: 36.64  E-value: 4.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77736091  181 EAVEAKQVAQ--QEAERARFVVEK------AEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAE 245
Cdd:PRK11029 232 EAVARRHRSQgqEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
13-231 8.69e-26

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


Pssm-ID: 223407 [Multi-domain]  Cd Length: 291  Bit Score: 102.91  E-value: 8.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  13 GLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNV------PVITGSKDLQ 86
Cdd:COG0330   7 IILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDNV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  87 NVNITLRILFRPVAsqlPRIFTSIGEDYDERvLPSITTEILKSVVARFDAGELITQREL-VSRQVSDDLTERAATFGLIL 165
Cdd:COG0330  86 IVSVDAVVQYRVTD---PQKAVYNVENAEAA-LRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77736091 166 DDVSLTHLTFGKEFTEAVEAKQVAQQEAERArfvVEKAEQQKKAAIISAEGDSKAAELIANSLATA 231
Cdd:COG0330 162 VDVEIKDIDPPEEVQAAMEKQMAAERDKRAE---ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
53-247 1.89e-05

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: 44.01  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091    53 GTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFRpvASQLPRIFTSIGED---YDERVLPSITT 124
Cdd:TIGR01932  51 GLHFKIPFIEHVKIFDAKiqtmdGRPDRIP----TKEKKDIIIDTYIRWR--IEDFKKYYLSTGGGtisAAEVLIKRKID 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091   125 EILKSVVARFDAGELITQ------------------------------RELVSRQVSDDLTERAATFGLILDDVSLTHLT 174
Cdd:TIGR01932 125 DRLRSEIGVLGLKEIVRSsndqldtlvsklalnrggkinkiamtitkgREILAREISQIANSQLKDIGIEVVDVRIKKIN 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091   175 FGKEFTEAV------EAKQVAQQ-------EAERARFVVEK------AEQQKKAAIISAEGDSKAAELIANSLATAGDGL 235
Cdd:TIGR01932 205 YSDELSESIynrmrsEREQIARMhrsqgeeKAEEILGKAEYevrkilSEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFY 284
                         250
                  ....*....|..
gi 77736091   236 IELRKLEAAEDI 247
Cdd:TIGR01932 285 SFWRSLEAYEKS 296
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
27-221 6.61e-90

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  Cd Length: 195  Bit Score: 267.46  E-value: 6.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 77736091 187 QVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
26-187 5.36e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581  Cd Length: 160  Bit Score: 124.70  E-value: 5.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091     26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091    105 RIFTSigEDYDERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 77736091    184 EAKQ 187
Cdd:smart00244 157 EAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
28-207 2.71e-29

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: 250396  Cd Length: 176  Bit Score: 110.14  E-value: 2.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091    28 YNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVASQLPrI 106
Cdd:pfam01145   1 VIVPPGEVGVVT-RFGKVSR-VLGPGLHFKLPFIQTITVVDTRLQTLEVTVQTvLTKDGVPVNVDVTVQYRVEDPPKL-V 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091   107 FTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:pfam01145  78 ANVTGEDDLQELLRPLVESALREVIARYTLDELLSNREEIAQEVKEALNEELEKYGIEIEDVQITDIDLPPEIEEAIEEK 157
                         170       180
                  ....*....|....*....|.
gi 77736091   187 QVAQQEAERARfvVEKAEQQK 207
Cdd:pfam01145 158 QAAEQEAEEAE--IERAEAEA 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
26-227 2.28e-16

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: 74.83  E-value: 2.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  26 ALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFR--- 97
Cdd:cd03405   1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWRitd 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  98 PVasqlpRIFTSIGEDYD-ERVLPSITTEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDDVSLTHLTF 175
Cdd:cd03405  76 PL-----RFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDL 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77736091 176 GKEFTEAV------EAKQVAQQ--------------EAERARfVVEKAEQQKKAAIISAEGDSKAAELIANS 227
Cdd:cd03405 151 PEEVSESVyermraERERIAAEyraegeeeaekiraEADRER-TVILAEAYREAEEIRGEGDAEAARIYAEA 221
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
51-248 1.14e-09

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 55.47  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  51 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpVASQLPRIFTSIGEDYDERVLPSITteiL 127
Cdd:cd13435   6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAATT---L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 128 KSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAkqvaqqEAERARfvvekaeqQK 207
Cdd:cd13435  80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAA------EAEAAR--------EA 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 77736091 208 KAAIISAEGDSKAAELI--ANSLATAGDGLIELRKLEAAEDIA 248
Cdd:cd13435 146 RAKVIAAEGEMKSSRALkeASDIISASPSALQLRYLQTLSSIS 188
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
74-177 7.79e-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  Cd Length: 110  Bit Score: 51.60  E-value: 7.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  74 RNVPVIT-GSKDLQNVNITLRILFRPV-ASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVS 151
Cdd:cd02106   5 DDVRVEPvGTADGVPVAVDLVVQFRITdYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVK 84
                        90       100
                ....*....|....*....|....*.
gi 77736091 152 DDLTERAATFGLILDDVSLTHLTFGK 177
Cdd:cd02106  85 EDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
30-248 1.76e-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. 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: 52.15  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  30 VDAGHRAVIFdrFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPViTG----SKDlqnvNITLRILFRpVASQL-- 103
Cdd:cd13438   1 VPPGERGLLY--RDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEV-SGqeilTAD----KVALRVNLV-ATYRVvd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 104 PRIFTSIGEDYDErVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKE----F 179
Cdd:cd13438  73 PVKAVETVDDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEireiL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 77736091 180 TEAVEAKQVAQQEAERARfvvEKAEQQKKAAiisaegdsKAAELIANSLAtagdgLIELRKLEAAEDIA 248
Cdd:cd13438 152 NQVLEAEKRAQANLIRAR---EETAATRSLL--------NAAKLMEENPA-----LLRLRELEALEKIA 204
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
59-248 5.32e-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: 50.21  E-value: 5.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  59 PWVQKPIIFDCRSRPRNVP---VITgsKDlqnvNITLR----ILFRPVASQlpRIFTSIgEDYDERVLP-SITTeiLKSV 130
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKvnavVYFRVVDPE--KAVLAV-EDYRYATSQlAQTT--LRSV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 131 VARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVeAKQVaqqEAERarfvvekaeqQKKAA 210
Cdd:cd08826  70 VGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAM-ARQA---EAER----------ERRAK 135
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 77736091 211 IISAEGDSKAAElianSLATAGD------GLIELRKLEAAEDIA 248
Cdd:cd08826 136 IIKAEGELQAAE----KLAEAAEilakspGALQLRYLQTLSEIA 175
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) familyfamily; belonging to the ...
28-248 7.43e-08

Alloslipin, a subgroup of the stomatin-like proteins (slipins) familyfamily; 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: 50.69  E-value: 7.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  28 YNVDAGHRAVIfDRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRPVASQlp 104
Cdd:cd13437   7 KQVKQGSVGLV-ERFGKFYKTV-DPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYRIIDPY-- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 105 RIFTSIgEDYDERVLP-SITTeiLKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTE-- 181
Cdd:cd13437  81 KAIYRI-DNVKQALIErTQTT--LRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQsl 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 77736091 182 --AVEAKQVAQQEAERARFVVEKAEQQKKAAIISaegDSKAAelianslatagdglIELRKLEAAEDIA 248
Cdd:cd13437 158 ssAAKAKRIGESKIISAKADVESAKLMREAADIL---DSKAA--------------MQIRYLETLQAIA 209
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
36-241 7.43e-06

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


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 44.88  E-value: 7.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  36 AVIFDRFrGVQDIVVGEGTHFLIPWVQKpiIFD---CRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIge 112
Cdd:cd03407   7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 113 DYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQE 192
Cdd:cd03407  82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRL 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 77736091 193 AERArfvVEKAEQQKKAAIISAEGDSKAAELianslatAGDGLIELRKL 241
Cdd:cd03407 162 REAA---EEKAEAEKILQVKAAEAEAEAKRL-------QGVGIAEQRKA 200
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
13-231 2.32e-05

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: 43.27  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  13 GLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITG--------SKD 84
Cdd:cd03404   1 LILLLLLLVWLLSGFYTVDPGERGVVL-RFGKYVR-TVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlTGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  85 LQNVNITLRILFRpvasqlpriftsIGEDYD--------ERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSDDLT 155
Cdd:cd03404  79 ENIVDVDFVVQYR------------ISDPVAylfnvrdpEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 156 ERAATF--GLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARF--------VVEKAEQQKKAAIISAEGDskAAELIA 225
Cdd:cd03404 147 EILDRYdlGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINeaqayaneVIPRARGEAARIIQEAEAY--KAEVVA 224

                ....*.
gi 77736091 226 NSLATA 231
Cdd:cd03404 225 RAEGDA 230
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
51-248 3.18e-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: 39.46  E-value: 3.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  51 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpvaSQLPRIFTSIGEDYDE--RVLPSITte 125
Cdd:cd03403   6 GPGLFFILPCIDSYRKVDLRTVSFDVPpqeILT--KDSVTVAVDAVVYYR---VQNATIAVTNVENADRstRLLAQTT-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 126 iLKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLthltfgKEFTEAVEAKQVAQQEAERARfvvekaeq 205
Cdd:cd03403  79 -LRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEI------KDVRLPVQLQRAMAAEAEAAR-------- 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 77736091 206 QKKAAIISAEGDSKAAELI--ANSLATAGDGLIELRKLEAAEDIA 248
Cdd:cd03403 144 EARAKVIAAEGEQNASRALkeAADVISESPAALQLRYLQTLNTIS 188
PRK11029 PRK11029
FtsH protease regulator HflC; Provisional
181-245 4.33e-03

FtsH protease regulator HflC; Provisional


Pssm-ID: 182913  Cd Length: 334  Bit Score: 36.64  E-value: 4.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77736091  181 EAVEAKQVAQ--QEAERARFVVEK------AEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAE 245
Cdd:PRK11029 232 EAVARRHRSQgqEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
112-259 6.47e-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  Cd Length: 177  Bit Score: 35.29  E-value: 6.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 112 EDYDERVLPSITTEiLKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKqvAQq 191
Cdd:cd13775  44 EDYRAAVSLAAQTA-LRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSRE--AQ- 119
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77736091 192 eaerarfvvekAEQQKKAAIISAEGDSKAAELianslatagdgLIELRKLEAAEDIAYQLsRSRNITY 259
Cdd:cd13775 120 -----------AEREKNARVILAEAEKEIAEM-----------FVEAAEVYENNPIALQL-RAMNMLY 164
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
13-231 8.69e-26

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


Pssm-ID: 223407 [Multi-domain]  Cd Length: 291  Bit Score: 102.91  E-value: 8.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  13 GLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNV------PVITGSKDLQ 86
Cdd:COG0330   7 IILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDNV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  87 NVNITLRILFRPVAsqlPRIFTSIGEDYDERvLPSITTEILKSVVARFDAGELITQREL-VSRQVSDDLTERAATFGLIL 165
Cdd:COG0330  86 IVSVDAVVQYRVTD---PQKAVYNVENAEAA-LRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 77736091 166 DDVSLTHLTFGKEFTEAVEAKQVAQQEAERArfvVEKAEQQKKAAIISAEGDSKAAELIANSLATA 231
Cdd:COG0330 162 VDVEIKDIDPPEEVQAAMEKQMAAERDKRAE---ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
53-247 1.89e-05

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: 44.01  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091    53 GTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFRpvASQLPRIFTSIGED---YDERVLPSITT 124
Cdd:TIGR01932  51 GLHFKIPFIEHVKIFDAKiqtmdGRPDRIP----TKEKKDIIIDTYIRWR--IEDFKKYYLSTGGGtisAAEVLIKRKID 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091   125 EILKSVVARFDAGELITQ------------------------------RELVSRQVSDDLTERAATFGLILDDVSLTHLT 174
Cdd:TIGR01932 125 DRLRSEIGVLGLKEIVRSsndqldtlvsklalnrggkinkiamtitkgREILAREISQIANSQLKDIGIEVVDVRIKKIN 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091   175 FGKEFTEAV------EAKQVAQQ-------EAERARFVVEK------AEQQKKAAIISAEGDSKAAELIANSLATAGDGL 235
Cdd:TIGR01932 205 YSDELSESIynrmrsEREQIARMhrsqgeeKAEEILGKAEYevrkilSEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFY 284
                         250
                  ....*....|..
gi 77736091   236 IELRKLEAAEDI 247
Cdd:TIGR01932 285 SFWRSLEAYEKS 296
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
46-223 7.42e-04

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


Pssm-ID: 225177 [Multi-domain]  Cd Length: 548  Bit Score: 39.43  E-value: 7.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091  46 QDIVVGeGTHFLIPWVQKPIIFDCRSRPRNVPVITG-SKDlqNVNITLRILFR-PVASQLPRIFTSI---GEDYD----E 116
Cdd:COG2268  61 QKVVRG-GGAIVMPIFQTIERMSLTTIKLEVEIDNVyTKD--GMPLNVEAVAYvKIGDTFQDIATAAerfGGKGSredlE 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77736091 117 RVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLT-------HLTFGKEFTEAVEAKQVA 189
Cdd:COG2268 138 QLAEDTLEGALRAVLAQMTVEELNEDRLGFAQVVQEVVGDDLSKMGLVLDSLAINdindtskENQDPNNYLDALGRRRIA 217
                       170       180       190
                ....*....|....*....|....*....|....
gi 77736091 190 qQEAERARFVVEKAEQQKKAAIISAEGDSKAAEL 223
Cdd:COG2268 218 -QVLQDAEIAENEAEKETEIAIAEANRDAKLVEL 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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