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Conserved domains on  [gi|161077236|ref|NP_652030|]
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prohibitin 2, isoform B [Drosophila melanogaster]

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 ...
 42-236 2.08e-95

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: 279.78  E-value: 2.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  42 LYTVEGGHRAIIFSRLGGIQSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPTGSKDLQMINISLRVLSRPDSLNLPYL 121
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 122 HKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAK 201
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161077236 202 QVAQQEAQRAVFFVERAKQEKQQKIVQAEGEAEAA 236
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 ...
 42-236 2.08e-95

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: 279.78  E-value: 2.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  42 LYTVEGGHRAIIFSRLGGIQSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPTGSKDLQMINISLRVLSRPDSLNLPYL 121
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 122 HKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAK 201
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161077236 202 QVAQQEAQRAVFFVERAKQEKQQKIVQAEGEAEAA 236
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 41-202 1.19e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 112.75  E-value: 1.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236    41 SLYTVEGGHRAIIFSRLGGIQsDIYSEGLHVRIPWFQYPIIYDIRSRPRKI-SSPTGSKDLQMINISLRVLSRpdSLN-L 118
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR--VLDpL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236   119 PYLHKQLgvDYDEKVLPSICNEVLKSVIAKFNASQLIT-QRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAA 197
Cdd:smart00244  78 RAVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 161077236   198 IEAKQ 202
Cdd:smart00244 156 MEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 39-278 1.58e-30

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 115.71  E-value: 1.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  39 SQSLYTVEGGHRAIIFsRLGGIQsDIYSEGLHVRIPWFQYPIIYDIRSRPRKI-SSPTGSKDLQMINISLRVLSRPDSLN 117
Cdd:COG0330   18 FSSVYIVPQGERGVVL-RFGKYV-RTLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVDVDAVVQYRITDPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 118 LPYLhkqlGVDYDEKVLPSICNEVLKSVIAKFNASQLI-TQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTA 196
Cdd:COG0330   96 KFLY----NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 197 AIEAKQVAQQEAQRAVF-------------------FVERAKQEKQQKIVQAEGEAEAAKMLGLAVKQNPAYLKLRKLRA 257
Cdd:COG0330  172 AMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEA 251

                        250       260
                 ....*....|....*....|.
gi 161077236 258 AQSIArtiASSQNKVYLSADS 278
Cdd:COG0330  252 LEEVL---SPNSKVIVLPPDG 269
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 43-222 7.84e-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: 98.16  E-value: 7.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236   43 YTVEGGHRAIIFsRLGGIqSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPT-GSKDLQMINISLRVLSRPDSLNLPYL 121
Cdd:pfam01145   1 IIVPPGEVGVVT-RFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  122 HKQL-GVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEA 200
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170       180
                  ....*....|....*....|..
gi 161077236  201 KQVAQQEAQRAvffVERAKQEK 222
Cdd:pfam01145 159 KQTAEQEAEAE---IARAEAEA 177
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 40-278 5.26e-09

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: 56.33  E-value: 5.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236   40 QSLYTVEGGHRAIIfSRLGGIQSD------IYSEGLHVRIPWFQYPIIYDIR-----SRPRKIssPTGSKDLQMINISLR 108
Cdd:TIGR01932  18 QPFFIIKEGERGII-TRFGKILKDnnhhvlVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRI--PTKEKKDIIIDTYIR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  109 vlSRPDSLNLPYLHKQLG-VDYDEKVLPSICNEVLKSVIAKFNASQLITQ-RQQVSLLIRKELVERA------------- 173
Cdd:TIGR01932  95 --WRIEDFKKYYLSTGGGtISAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNRGgkinkiamtitkg 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  174 ----------------RDFNIILDDVSLTELSFGKEYTAAI------EAKQVAQQ-----EAQRAVFFVER--------A 218
Cdd:TIGR01932 173 reilareisqiansqlKDIGIEVVDVRIKKINYSDELSESIynrmrsEREQIARMhrsqgEEKAEEILGKAeyevrkilS 252

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  219 KQEKQQKIVQAEGEAEAAKMLGLAVKQNPAYLKLrkLRAAQSIARTIASSQNKVYLSADS 278
Cdd:TIGR01932 253 EAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSF--WRSLEAYEKSFKDNQDEKVLSTDS 310
PRK11029 PRK11029
protease modulator HflC;
41-278 7.16e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 43.58  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  41 SLYTVEGGHRAIIFsRLGGIQSD------IYSEGLHVRIPWFQYPIIYDIRsrprkISSPTGSKD--LQMINISLRVLS- 111
Cdd:PRK11029  19 SVFVVKEGERGIVL-RFGKVLRDddnkplVYAPGLHFKIPFIETVKMLDAR-----IQTMDNQADrfVTKEKKDLIVDSy 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 112 ---RPDSLNLPYLHKQLG-VDYDEKVLPSICNEVLKSVIAKFNASQLIT-QRQQVSLLIRKEL----------VERARDF 176
Cdd:PRK11029  93 ikwRISDFSRYYLATGGGdISQAEVLLKRKFSDRLRSEIGRLDVKDIVTdSRGRLTLDVRDALnsgsagtedeVATPAAD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 177 NIILD-----------------------------DVSLTELSFGKEYTAAI------EAKQVA-------QQEAQR---- 210
Cdd:PRK11029 173 DAIASaaerveaetkgkvpvinpnsmaalgievvDVRIKQINLPTEVSDAIynrmraEREAVArrhrsqgQEEAEKlrat 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077236 211 AVFFVER--AKQEKQQKIVQAEGEAEAAKMLGLAVKQNPA-YLKLRKLRAAQSiarTIASSQNKVYLSADS 278
Cdd:PRK11029 253 ADYEVTRtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDfYAFIRSLRAYEN---SFSGNQDVMVLSPDS 320
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 42-236 2.08e-95

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: 279.78  E-value: 2.08e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  42 LYTVEGGHRAIIFSRLGGIQSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPTGSKDLQMINISLRVLSRPDSLNLPYL 121
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 122 HKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAK 201
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 161077236 202 QVAQQEAQRAVFFVERAKQEKQQKIVQAEGEAEAA 236
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 41-202 1.19e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 112.75  E-value: 1.19e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236    41 SLYTVEGGHRAIIFSRLGGIQsDIYSEGLHVRIPWFQYPIIYDIRSRPRKI-SSPTGSKDLQMINISLRVLSRpdSLN-L 118
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR--VLDpL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236   119 PYLHKQLgvDYDEKVLPSICNEVLKSVIAKFNASQLIT-QRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAA 197
Cdd:smart00244  78 RAVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 161077236   198 IEAKQ 202
Cdd:smart00244 156 MEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 39-278 1.58e-30

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 115.71  E-value: 1.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  39 SQSLYTVEGGHRAIIFsRLGGIQsDIYSEGLHVRIPWFQYPIIYDIRSRPRKI-SSPTGSKDLQMINISLRVLSRPDSLN 117
Cdd:COG0330   18 FSSVYIVPQGERGVVL-RFGKYV-RTLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVDVDAVVQYRITDPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 118 LPYLhkqlGVDYDEKVLPSICNEVLKSVIAKFNASQLI-TQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTA 196
Cdd:COG0330   96 KFLY----NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 197 AIEAKQVAQQEAQRAVF-------------------FVERAKQEKQQKIVQAEGEAEAAKMLGLAVKQNPAYLKLRKLRA 257
Cdd:COG0330  172 AMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEA 251

                        250       260
                 ....*....|....*....|.
gi 161077236 258 AQSIArtiASSQNKVYLSADS 278
Cdd:COG0330  252 LEEVL---SPNSKVIVLPPDG 269
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 43-222 7.84e-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: 98.16  E-value: 7.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236   43 YTVEGGHRAIIFsRLGGIqSDIYSEGLHVRIPWFQYPIIYDIRSRPRKISSPT-GSKDLQMINISLRVLSRPDSLNLPYL 121
Cdd:pfam01145   1 IIVPPGEVGVVT-RFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  122 HKQL-GVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEA 200
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170       180
                  ....*....|....*....|..
gi 161077236  201 KQVAQQEAQRAvffVERAKQEK 222
Cdd:pfam01145 159 KQTAEQEAEAE---IARAEAEA 177
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-261 6.13e-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: 69.82  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  41 SLYTVEGGHRAIIFsRLGGIQSDIYSEGLHVRIPWFQYPIIYDIR-----SRPRKIssPTgsKDLQMINISLRVLSR-PD 114
Cdd:cd03405    1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEV--LT--KDKKRLIVDSYARWRiTD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 115 SLNlpYLHKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLI-TQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKE 193
Cdd:cd03405   76 PLR--FYQSVGGEEGAESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 194 YTAAI------EAKQVAQQ-------EAQRAvffveRAKQEKQQKIVQA-----------EGEAEAAKMLGLAVKQNPA- 248
Cdd:cd03405  154 VSESVyermraERERIAAEyraegeeEAEKI-----RAEADRERTVILAeayreaeeirgEGDAEAARIYAEAYGKDPEf 228

                        250
                 ....*....|...
gi 161077236 249 YLKLRKLRAAQSI 261
Cdd:cd03405  229 YSFYRSLEAYRAS 241
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 40-278 5.26e-09

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: 56.33  E-value: 5.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236   40 QSLYTVEGGHRAIIfSRLGGIQSD------IYSEGLHVRIPWFQYPIIYDIR-----SRPRKIssPTGSKDLQMINISLR 108
Cdd:TIGR01932  18 QPFFIIKEGERGII-TRFGKILKDnnhhvlVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRI--PTKEKKDIIIDTYIR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  109 vlSRPDSLNLPYLHKQLG-VDYDEKVLPSICNEVLKSVIAKFNASQLITQ-RQQVSLLIRKELVERA------------- 173
Cdd:TIGR01932  95 --WRIEDFKKYYLSTGGGtISAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNRGgkinkiamtitkg 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  174 ----------------RDFNIILDDVSLTELSFGKEYTAAI------EAKQVAQQ-----EAQRAVFFVER--------A 218
Cdd:TIGR01932 173 reilareisqiansqlKDIGIEVVDVRIKKINYSDELSESIynrmrsEREQIARMhrsqgEEKAEEILGKAeyevrkilS 252

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  219 KQEKQQKIVQAEGEAEAAKMLGLAVKQNPAYLKLrkLRAAQSIARTIASSQNKVYLSADS 278
Cdd:TIGR01932 253 EAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSF--WRSLEAYEKSFKDNQDEKVLSTDS 310
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 92-192 1.72e-07

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: 48.90  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  92 SSPTGSKDLQMINISLRVLSRP-DSLNLPYLHKQLGVDYDEKVLPSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELV 170
Cdd:cd02106    9 VEPVGTADGVPVAVDLVVQFRItDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLE 88

                         90       100
                 ....*....|....*....|..
gi 161077236 171 ERARDFNIILDDVSLTELSFGK 192
Cdd:cd02106   89 EDLENFGVVISDVDITSIEPPD 110
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 141-263 1.76e-07

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


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 50.21  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 141 VLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIeAKQVaqqEAQRavffverakq 220
Cdd:cd08826   65 TLRSVVGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAM-ARQA---EAER---------- 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 161077236 221 EKQQKIVQAEGEAEAAKMLGLAVK---QNPAYLKLRKLRAAQSIAR 263
Cdd:cd08826  131 ERRAKIIKAEGELQAAEKLAEAAEilaKSPGALQLRYLQTLSEIAS 176
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-234 2.45e-07

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: 50.97  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  41 SLYTVEGGHRAIIFsRLGGIQSdIYSEGLHVRIPW-FQYPIIYDIrSRPRKISSPTG--------SKDLQMINISLRVLS 111
Cdd:cd03404   14 GFYTVDPGERGVVL-RFGKYVR-TVGPGLHWKLPFpIEVVEKVNV-TQVRSVEIGFRvpeeslmlTGDENIVDVDFVVQY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 112 R---PDSlnlpYLHKqlgVDYDEKVLPSICNEVLKSVIAKFNASQLIT-QRQQVSLLIRKELVERARDFN--IILDDVSL 185
Cdd:cd03404   91 RisdPVA----YLFN---VRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYDlgIEIVQVQL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161077236 186 TEL--------SFgKEYTAAIEAKQ---------------VAQQEAQRavfFVERAKQEKQQKIVQAEGEAE 234
Cdd:cd03404  164 QDAdppeevqdAF-DDVNAARQDKErlineaqayanevipRARGEAAR---IIQEAEAYKAEVVARAEGDAA 231
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 142-262 3.50e-07

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: 50.08  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 142 LKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFgkeyTAAIEAKQVAQQEAQRavffverakqE 221
Cdd:cd13435   79 LRNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSL----PDSLQRAMAAEAEAAR----------E 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 161077236 222 KQQKIVQAEGEAEAAKMLGLA---VKQNPAYLKLRKLRAAQSIA 262
Cdd:cd13435  145 ARAKVIAAEGEMKSSRALKEAsdiISASPSALQLRYLQTLSSIS 188
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 142-255 7.51e-06

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: 45.31  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 142 LKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAkqvaqqEAQravffverAKQE 221
Cdd:cd13775   58 LRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSR------EAQ--------AERE 123

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 161077236 222 KQQKIVQAEGEAEAAKMLGLAVK---QNPAYLKLRKL 255
Cdd:cd13775  124 KNARVILAEAEKEIAEMFVEAAEvyeNNPIALQLRAM 160
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 142-265 2.58e-05

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: 44.45  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 142 LKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAA----IEAKQVAQqeAQravffVER 217
Cdd:cd13438   95 LREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREIlnqvLEAEKRAQ--AN-----LIR 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 161077236 218 AKQEKQQkivqAEGEAEAAKMLglavKQNPAYLKLRKLRAAQSIARTI 265
Cdd:cd13438  168 AREETAA----TRSLLNAAKLM----EENPALLRLRELEALEKIAEKV 207
PRK11029 PRK11029
protease modulator HflC;
41-278 7.16e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 43.58  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  41 SLYTVEGGHRAIIFsRLGGIQSD------IYSEGLHVRIPWFQYPIIYDIRsrprkISSPTGSKD--LQMINISLRVLS- 111
Cdd:PRK11029  19 SVFVVKEGERGIVL-RFGKVLRDddnkplVYAPGLHFKIPFIETVKMLDAR-----IQTMDNQADrfVTKEKKDLIVDSy 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 112 ---RPDSLNLPYLHKQLG-VDYDEKVLPSICNEVLKSVIAKFNASQLIT-QRQQVSLLIRKEL----------VERARDF 176
Cdd:PRK11029  93 ikwRISDFSRYYLATGGGdISQAEVLLKRKFSDRLRSEIGRLDVKDIVTdSRGRLTLDVRDALnsgsagtedeVATPAAD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 177 NIILD-----------------------------DVSLTELSFGKEYTAAI------EAKQVA-------QQEAQR---- 210
Cdd:PRK11029 173 DAIASaaerveaetkgkvpvinpnsmaalgievvDVRIKQINLPTEVSDAIynrmraEREAVArrhrsqgQEEAEKlrat 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161077236 211 AVFFVER--AKQEKQQKIVQAEGEAEAAKMLGLAVKQNPA-YLKLRKLRAAQSiarTIASSQNKVYLSADS 278
Cdd:PRK11029 253 ADYEVTRtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDfYAFIRSLRAYEN---SFSGNQDVMVLSPDS 320
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 59-243 1.31e-03

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: 39.49  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236  59 GIQSDIYSEGLHVRIPWFQYpIIYDIRSRPRKISS--PTGSKD--LQMINISLRVLSRPDSLNLPYLHkqlgVDYDEKVL 134
Cdd:cd03407   14 GKFSRIAEPGLHFIIPPIES-VAGRVSLRVQQLDVrvETKTKDnvFVTLVVSVQYRVVPEKVYDAFYK----LTNPEQQI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 135 PSICNEVLKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVSLTELSFGKEYTAAIEAKQVAQQEAQRAVff 214
Cdd:cd03407   89 QSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAE-- 166

                        170       180
                 ....*....|....*....|....*....
gi 161077236 215 vERAKQEKQQKIVQAEGEAEAAKMLGLAV 243
Cdd:cd03407  167 -EKAEAEKILQVKAAEAEAEAKRLQGVGI 194
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 142-262 1.84e-03

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: 38.69  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077236 142 LKSVIAKFNASQLITQRQQVSLLIRKELVERARDFNIILDDVsltelsfgkeytaaiEAKQVA-QQEAQRAVFFVERAKQ 220
Cdd:cd03403   79 LRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERV---------------EIKDVRlPVQLQRAMAAEAEAAR 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 161077236 221 EKQQKIVQAEGEAEAAKML---GLAVKQNPAYLKLRKLRAAQSIA 262
Cdd:cd03403  144 EARAKVIAAEGEQNASRALkeaADVISESPAALQLRYLQTLNTIS 188
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
192-242 7.10e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 37.54  E-value: 7.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 161077236 192 KEYTAAIEAKQVAQQEAQRAVffVERAKQEKQQKIVQAEGEAEAAKMLGLA 242
Cdd:COG2268  290 REIELQEKEAEREEAELEADV--RKPAEAEKQAAEAEAEAEAEAIRAKGLA 338
 
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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