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Conserved domains on  [gi|41152028|ref|NP_958454|]
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prohibitin [Danio rerio]

Protein Classification

SPFH_prohibitin domain-containing protein (domain architecture ID 10130412)

SPFH_prohibitin domain-containing protein

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 ...
26-220 2.61e-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: 269.38  E-value: 2.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  26 LYNVDAGHRAVIFDRFRGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVAGQLPRI 105
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 106 FTSIGEDYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVEMK 185
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 41152028 186 QVAQQEAERARFVVEKAEQQKQAAIISAEGDSQAA 220
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
26-220 2.61e-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: 269.38  E-value: 2.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  26 LYNVDAGHRAVIFDRFRGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVAGQLPRI 105
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 106 FTSIGEDYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVEMK 185
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 41152028 186 QVAQQEAERARFVVEKAEQQKQAAIISAEGDSQAA 220
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
25-186 2.58e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581  Cd Length: 160  Bit Score: 129.32  E-value: 2.58e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028     25 ALYNVDAGHRAVIFDRFRGVQDVVvGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVAGQLP 103
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVL-GPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    104 RIFTSigEDYDERVLPSITTEVLKSVVARFDAGELIT-QRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAV 182
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 41152028    183 EMKQ 186
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 ...
29-206 1.43e-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: 307341  Cd Length: 177  Bit Score: 112.04  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    29 VDAGHRAVIFdRFRGVQDVVvGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRpVAGQLPRIFT 107
Cdd:pfam01145   3 VPPGEVGVVT-RFGKLSRVL-GPGLHFIIPFIQSVVIVDVRVQTLDVSVQTvLTKDGVPVNVDATVIYR-VPDDPPKLVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   108 SI--GEDYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVEMK 185
Cdd:pfam01145  80 TVgfGSDDLQELIRQVVQSALREVIARYTLEELLSNREELAEEIKAALNEELSKYGVEIIDVQITDIDPPPEYREAIEAK 159
                         170       180
                  ....*....|....*....|.
gi 41152028   186 QVAQQEAERArfvVEKAEQQK 206
Cdd:pfam01145 160 QTAEQEAEAE---IARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
11-230 2.97e-27

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


Pssm-ID: 223407  Cd Length: 291  Bit Score: 108.30  E-value: 2.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  11 LGLALAIGGGVVNSALYNVDAGHRAVIFdRFRGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNV------PVITGSKDL 84
Cdd:COG0330   6 IIILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  85 QNVNITLRILFRPVAGQLPRIFTsigeDYDERVLPSITTEVLKSVVARFDAGELITQREL-VSRQVSEDLTERASTFGLI 163
Cdd:COG0330  85 VIVSVDAVVQYRVTDPQKAVYNV----ENAEAALRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIK 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152028 164 LDDVSLTHLTFGKEFTEAVEmKQVAQQEAERARfvVEKAEQQKQAAIISAEGDSQAALLIANSLAEA 230
Cdd:COG0330 161 VVDVEIKDIDPPEEVQAAME-KQMAAERDKRAE--ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
52-246 5.23e-06

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  Cd Length: 317  Bit Score: 46.70  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    52 GTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFRpvAGQLPRIFTSIGED---YDERVLPSITT 123
Cdd:TIGR01932  51 GLHFKIPFIEHVKIFDAKiqtmdGRPDRIP----TKEKKDIIIDTYIRWR--IEDFKKYYLSTGGGtisAAEVLIKRKID 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   124 EVLKSVVARFDAGELITQ-RELVSRQVSEDLTERAST-----------------------------FGLILDDVSLTHLT 173
Cdd:TIGR01932 125 DRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNRGGKinkiamtitkgreilareisqiansqlkdIGIEVVDVRIKKIN 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   174 FGKEFTEAV------EMKQVAQQ-------EAERARFVVEK------AEQQKQAAIISAEGDSQAALLIANSLAEAGDGL 234
Cdd:TIGR01932 205 YSDELSESIynrmrsEREQIARMhrsqgeeKAEEILGKAEYevrkilSEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFY 284
                         250
                  ....*....|..
gi 41152028   235 VELRKLEAAEDI 246
Cdd:TIGR01932 285 SFWRSLEAYEKS 296
PRK11029 PRK11029
FtsH protease regulator HflC; Provisional
180-244 3.02e-04

FtsH protease regulator HflC; Provisional


Pssm-ID: 182913  Cd Length: 334  Bit Score: 41.26  E-value: 3.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152028  180 EAVEMKQVAQ--QEAERARFVVEK------AEQQKQAAIISAEGDSQAALLIANSLAEAGDGLVELRKLEAAE 244
Cdd:PRK11029 232 EAVARRHRSQgqEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
26-220 2.61e-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: 269.38  E-value: 2.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  26 LYNVDAGHRAVIFDRFRGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVAGQLPRI 105
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 106 FTSIGEDYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVEMK 185
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 41152028 186 QVAQQEAERARFVVEKAEQQKQAAIISAEGDSQAA 220
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
25-186 2.58e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581  Cd Length: 160  Bit Score: 129.32  E-value: 2.58e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028     25 ALYNVDAGHRAVIFDRFRGVQDVVvGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVAGQLP 103
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVL-GPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    104 RIFTSigEDYDERVLPSITTEVLKSVVARFDAGELIT-QRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAV 182
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 41152028    183 EMKQ 186
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 ...
29-206 1.43e-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: 307341  Cd Length: 177  Bit Score: 112.04  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    29 VDAGHRAVIFdRFRGVQDVVvGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRpVAGQLPRIFT 107
Cdd:pfam01145   3 VPPGEVGVVT-RFGKLSRVL-GPGLHFIIPFIQSVVIVDVRVQTLDVSVQTvLTKDGVPVNVDATVIYR-VPDDPPKLVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   108 SI--GEDYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVEMK 185
Cdd:pfam01145  80 TVgfGSDDLQELIRQVVQSALREVIARYTLEELLSNREELAEEIKAALNEELSKYGVEIIDVQITDIDPPPEYREAIEAK 159
                         170       180
                  ....*....|....*....|.
gi 41152028   186 QVAQQEAERArfvVEKAEQQK 206
Cdd:pfam01145 160 QTAEQEAEAE---IARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
11-230 2.97e-27

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


Pssm-ID: 223407  Cd Length: 291  Bit Score: 108.30  E-value: 2.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  11 LGLALAIGGGVVNSALYNVDAGHRAVIFdRFRGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNV------PVITGSKDL 84
Cdd:COG0330   6 IIILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  85 QNVNITLRILFRPVAGQLPRIFTsigeDYDERVLPSITTEVLKSVVARFDAGELITQREL-VSRQVSEDLTERASTFGLI 163
Cdd:COG0330  85 VIVSVDAVVQYRVTDPQKAVYNV----ENAEAALRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIK 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152028 164 LDDVSLTHLTFGKEFTEAVEmKQVAQQEAERARfvVEKAEQQKQAAIISAEGDSQAALLIANSLAEA 230
Cdd:COG0330 161 VVDVEIKDIDPPEEVQAAME-KQMAAERDKRAE--ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
25-230 2.11e-18

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  Cd Length: 249  Bit Score: 81.77  E-value: 2.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  25 ALYNVDAGHRAVIFdRFRGVQDVVVGEGTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFR--- 96
Cdd:cd03405   1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWRitd 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  97 PVagqlpRIFTSIGEDYD-ERVLPSITTEVLKSVVARFDAGELI-TQRELVSRQVSEDLTERASTFGLILDDVSLTHLTF 174
Cdd:cd03405  76 PL-----RFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDL 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 41152028 175 GKEFTEAV--EMKQVAQQEAERARfvvekAEQQKQAAIISAEGDSQAALLIANSLAEA 230
Cdd:cd03405 151 PEEVSESVyeRMRAERERIAAEYR-----AEGEEEAEKIRAEADRERTVILAEAYREA 203
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
58-247 7.23e-10

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  Cd Length: 178  Bit Score: 56.75  E-value: 7.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  58 PWVQKPIIFDCRSRPRNVP---VITgsKDlqnvNITLR----ILFRPVAGQlpRIFTSIgEDYDERVLP-SITTevLKSV 129
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKvnavVYFRVVDPE--KAVLAV-EDYRYATSQlAQTT--LRSV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 130 VARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLtfgkEFTEavEMKQVAQQEAErarfvvekAEQQKQAA 209
Cdd:cd08826  70 VGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDV----DLPE--SMQRAMARQAE--------AERERRAK 135
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41152028 210 IISAEGDSQAalliANSLAEAGD------GLVELRKLEAAEDIA 247
Cdd:cd08826 136 IIKAEGELQA----AEKLAEAAEilakspGALQLRYLQTLSEIA 175
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
73-176 1.19e-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: 55.06  E-value: 1.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  73 RNVPVIT-GSKDLQNVNITLRILFRPV-AGQLPRIFTSIGEDYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVS 150
Cdd:cd02106   5 DDVRVEPvGTADGVPVAVDLVVQFRITdYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVK 84
                        90       100
                ....*....|....*....|....*.
gi 41152028 151 EDLTERASTFGLILDDVSLTHLTFGK 176
Cdd:cd02106  85 EDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
50-247 1.38e-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  Cd Length: 208  Bit Score: 56.62  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  50 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpVAGQLPRIFTSIGEDYDERVLPSITtevL 126
Cdd:cd13435   6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAATT---L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 127 KSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLthltfgKEFTEAVEMKQVAQQEAERARfvvekaeqQK 206
Cdd:cd13435  80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI------KDVSLPDSLQRAMAAEAEAAR--------EA 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 41152028 207 QAAIISAEGD--SQAALLIANSLAEAGDGLVELRKLEAAEDIA 247
Cdd:cd13435 146 RAKVIAAEGEmkSSRALKEASDIISASPSALQLRYLQTLSSIS 188
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
29-247 1.20e-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  Cd Length: 215  Bit Score: 53.69  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  29 VDAGHRAVIFdrFRGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNVPViTG----SKDlqnvNITLRILFRpVAGQL-- 102
Cdd:cd13438   1 VPPGERGLLY--RDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEV-SGqeilTAD----KVALRVNLV-ATYRVvd 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 103 PRIFTSIGEDYDErVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKefteav 182
Cdd:cd13438  73 PVKAVETVDDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPG------ 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152028 183 EMKQVAQQEAErarfvvekAEQQKQAAIISAEGDSQA--ALLIANSLAEAGDGLVELRKLEAAEDIA 247
Cdd:cd13438 146 EIREILNQVLE--------AEKRAQANLIRAREETAAtrSLLNAAKLMEENPALLRLRELEALEKIA 204
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) familyfamily; belonging to the ...
27-223 2.36e-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  Cd Length: 222  Bit Score: 53.00  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  27 YNVDAGHRAVIfDRFRGVQDVVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRPVAgqLP 103
Cdd:cd13437   7 KQVKQGSVGLV-ERFGKFYKTV-DPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYRIID--PY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 104 RIFTSIgEDYDERVLpSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVE 183
Cdd:cd13437  81 KAIYRI-DNVKQALI-ERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 41152028 184 MKQVAQQEAE----RARFVVEKAEQQKQAAIISaegDSQAALLI 223
Cdd:cd13437 159 SAAKAKRIGEskiiSAKADVESAKLMREAADIL---DSKAAMQI 199
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
35-240 6.99e-07

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  Cd Length: 269  Bit Score: 49.12  E-value: 6.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  35 AVIFDRFrGVQDVVVGEGTHFLIPWVQKpiIFD---CRSRPRNVPVITGSKDLQNVNITLRILFRPVAGQLPRIFTSIge 111
Cdd:cd03407   7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 112 DYDERVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAveMKQVaqQE 191
Cdd:cd03407  82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAA--MNEI--NA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 41152028 192 AERARF-VVEKAEQQKQAAIISAEGDsqaalliANSLAEAGDGLVELRKL 240
Cdd:cd03407 158 AQRLREaAEEKAEAEKILQVKAAEAE-------AEAKRLQGVGIAEQRKA 200
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
52-246 5.23e-06

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  Cd Length: 317  Bit Score: 46.70  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    52 GTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFRpvAGQLPRIFTSIGED---YDERVLPSITT 123
Cdd:TIGR01932  51 GLHFKIPFIEHVKIFDAKiqtmdGRPDRIP----TKEKKDIIIDTYIRWR--IEDFKKYYLSTGGGtisAAEVLIKRKID 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   124 EVLKSVVARFDAGELITQ-RELVSRQVSEDLTERAST-----------------------------FGLILDDVSLTHLT 173
Cdd:TIGR01932 125 DRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNRGGKinkiamtitkgreilareisqiansqlkdIGIEVVDVRIKKIN 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   174 FGKEFTEAV------EMKQVAQQ-------EAERARFVVEK------AEQQKQAAIISAEGDSQAALLIANSLAEAGDGL 234
Cdd:TIGR01932 205 YSDELSESIynrmrsEREQIARMhrsqgeeKAEEILGKAEYevrkilSEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFY 284
                         250
                  ....*....|..
gi 41152028   235 VELRKLEAAEDI 246
Cdd:TIGR01932 285 SFWRSLEAYEKS 296
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
11-230 3.44e-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  Cd Length: 266  Bit Score: 44.04  E-value: 3.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  11 LGLALAIGGGVVnSALYNVDAGHRAVIFdRFrGVQDVVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITG--------SK 82
Cdd:cd03404   1 LILLLLLLVWLL-SGFYTVDPGERGVVL-RF-GKYVRTVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlTG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  83 DLQNVNITLRILFRpvagqlpriftsIGEDYD--------ERVLPSITTEVLKSVVARFDAGELIT-QRELVSRQVSEDL 153
Cdd:cd03404  78 DENIVDVDFVVQYR------------ISDPVAylfnvrdpEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 154 TERASTF--GLILDDVSLTHLTFGKEFTEAVEMKQVAQQEAERARF--------VVEKAEQQKQAAIISAEGDSQAalLI 223
Cdd:cd03404 146 QEILDRYdlGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINeaqayaneVIPRARGEAARIIQEAEAYKAE--VV 223

                ....*..
gi 41152028 224 ANSLAEA 230
Cdd:cd03404 224 ARAEGDA 230
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
50-247 6.97e-05

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  Cd Length: 202  Bit Score: 42.54  E-value: 6.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  50 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRPvagQLPRIFTSIGEDYDE--RVLPSITte 124
Cdd:cd03403   6 GPGLFFILPCIDSYRKVDLRTVSFDVPpqeILT--KDSVTVAVDAVVYYRV---QNATIAVTNVENADRstRLLAQTT-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 125 vLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLthltfgKEFTEAVEMKQVAQQEAERARfvvekaeq 204
Cdd:cd03403  79 -LRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEI------KDVRLPVQLQRAMAAEAEAAR-------- 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 41152028 205 QKQAAIISAEGDSQAalliANSLAEAGDGLVE------LRKLEAAEDIA 247
Cdd:cd03403 144 EARAKVIAAEGEQNA----SRALKEAADVISEspaalqLRYLQTLNTIS 188
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
111-258 8.96e-05

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: 41.84  E-value: 8.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 111 EDYDERVLPSITTeVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLTHLTFGKEFTEAVEMKQVAQQ 190
Cdd:cd13775  44 EDYRAAVSLAAQT-ALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAER 122
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152028 191 EaerarfvvekaeqqKQAAIISAEGDSQaallIANSLAEAGdglvelrKLEAAEDIAFQLsRARNVTY 258
Cdd:cd13775 123 E--------------KNARVILAEAEKE----IAEMFVEAA-------EVYENNPIALQL-RAMNMLY 164
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
27-270 1.14e-04

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  Cd Length: 261  Bit Score: 42.39  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028    27 YNVDAGHRAVIFdRFrGVQDVVVGEGTHFLIPWVQKPIIFDC---RSRPRNVPVITGskDLQNVNITLRILFRPVAgqlP 103
Cdd:TIGR01933   2 YTIGEAERGVVL-RF-GKYHRTVDPGLNWKPPFIEEVYPVNVtavRNLRKQGLMLTG--DENIVNVEMNVQYRITD---P 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   104 RIFTsIGEDYDERVLPSITTEVLKSVVARFDAGELITQ-RELVSRQVSEDLTE--RASTFGLILDDVSLTHLTFGKEFTE 180
Cdd:TIGR01933  75 YKYL-FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEiiDNYDLGITVTDVNFQSARPPEEVKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028   181 AVEMKQVAQQ-------EAE------------RARFVVEKAEQQKQAAIISAEGDSQAALLIANSLAEAGDGLVELRKLE 241
Cdd:TIGR01933 154 AFDDVIIAREdeeryinEAEayanevvpkargDAQRIIEEARGYKERRINRAKGDVARFTKLLAEYKKAPDVTRERLYLE 233
                         250       260
                  ....*....|....*....|....*....
gi 41152028   242 AAEDIafqLSRARNVTYLPSGQGTLLQLP 270
Cdd:TIGR01933 234 TMEKV---LSNTRKVLLDDKKGNNLLYLP 259
PRK11029 PRK11029
FtsH protease regulator HflC; Provisional
180-244 3.02e-04

FtsH protease regulator HflC; Provisional


Pssm-ID: 182913  Cd Length: 334  Bit Score: 41.26  E-value: 3.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152028  180 EAVEMKQVAQ--QEAERARFVVEK------AEQQKQAAIISAEGDSQAALLIANSLAEAGDGLVELRKLEAAE 244
Cdd:PRK11029 232 EAVARRHRSQgqEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
45-221 4.25e-04

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


Pssm-ID: 225177  Cd Length: 548  Bit Score: 41.36  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028  45 QDVVVGeGTHFLIPWVQKPIIFDCRSRPRNVPVITG-SKDlqNVNITLRILFR-PVAGQLPRIFTSI---GEDYD----E 115
Cdd:COG2268  61 QKVVRG-GGAIVMPIFQTIERMSLTTIKLEVEIDNVyTKD--GMPLNVEAVAYvKIGDTFQDIATAAerfGGKGSredlE 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152028 116 RVLPSITTEVLKSVVARFDAGELITQRELVSRQVSEDLTERASTFGLILDDVSLT-------HLTFGKEFTEAVEMKQVA 188
Cdd:COG2268 138 QLAEDTLEGALRAVLAQMTVEELNEDRLGFAQVVQEVVGDDLSKMGLVLDSLAINdindtskENQDPNNYLDALGRRRIA 217
                       170       180       190
                ....*....|....*....|....*....|...
gi 41152028 189 QqeaERARFVVEKAEQQKQAAIISAEGDSQAAL 221
Cdd:COG2268 218 Q---VLQDAEIAENEAEKETEIAIAEANRDAKL 247
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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