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Conserved domains on  [gi|446678612|ref|WP_000755958|]
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SPFH domain-containing protein [Shigella flexneri]

Protein Classification

SPFH domain-containing protein( domain architecture ID 10471637)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Mycobacterium tuberculosis protease Rv3090

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  16101677|17766116|10542406|24782879|21501885

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 22-208 6.20e-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: 97.78  E-value: 6.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612   22 RVEPGNVGIKVNklgDDKGVGEVVGVGRYWTGWNTEVYIFPTfKQMKTYDEPFSFQMSDGTTIGYHIGVAYKVDPSKVTT 101
Cdd:pfam01145   2 IVPPGEVGVVTR---FGKLSRVLEPGLHFIIPFIQRVVTVDV-RVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  102 VFQTYRKGVDDitDTDLRQKITDALNRLASKMTTDKFIdGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVI 181
Cdd:pfam01145  78 LVQNVFGSDDL--QELLRRVLESALREIIARYTLEELL-SNREELAEEIKNALQEELAKYGVEIIDVQ-ITDIDPPPEIA 153

                         170       180
                  ....*....|....*....|....*..
gi 446678612  182 DSINAKVTANQKTlqcEQEVKQREAEA 208
Cdd:pfam01145 154 EAIEAKQTAEQEA---EAEIARAEAEA 177
growth_prot_Scy super family cl49463
polarized growth protein Scy;
193-239 7.81e-06

polarized growth protein Scy;


The actual alignment was detected with superfamily member NF041483:

Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 7.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 446678612  193 KTLQceqevKQREAEANMLRAEAAgqADAIRTKAQAEADAIRLRGEA 239
Cdd:NF041483  625 RTLQ-----AQAEQEAERLRTEAA--ADASAARAEGENVAVRLRSEA 664
 
Name Accession Description Interval E-value
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 22-208 6.20e-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: 97.78  E-value: 6.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612   22 RVEPGNVGIKVNklgDDKGVGEVVGVGRYWTGWNTEVYIFPTfKQMKTYDEPFSFQMSDGTTIGYHIGVAYKVDPSKVTT 101
Cdd:pfam01145   2 IVPPGEVGVVTR---FGKLSRVLEPGLHFIIPFIQRVVTVDV-RVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  102 VFQTYRKGVDDitDTDLRQKITDALNRLASKMTTDKFIdGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVI 181
Cdd:pfam01145  78 LVQNVFGSDDL--QELLRRVLESALREIIARYTLEELL-SNREELAEEIKNALQEELAKYGVEIIDVQ-ITDIDPPPEIA 153

                         170       180
                  ....*....|....*....|....*..
gi 446678612  182 DSINAKVTANQKTlqcEQEVKQREAEA 208
Cdd:pfam01145 154 EAIEAKQTAEQEA---EAEIARAEAEA 177
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 23-221 2.45e-22

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: 91.42  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  23 VEPGNVGIKVNKLGDDKGVGevvgvgrYWTG------WNTEVYIFPTfkQMKTYDEPFSFQMSDGTTIGYHIGVAYKVDP 96
Cdd:cd03401    4 VDAGEVGVVFRRGKGVKDEV-------LGEGlhfkipWIQVVIIYDV--RTQPREITLTVLSKDGQTVNIDLSVLYRPDP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  97 SKVTTVFQTYRkgvDDITDTDLRQKITDALNRLASKMTTDKFIdGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEY 176
Cdd:cd03401   75 EKLPELYQNLG---PDYEERVLPPIVREVLKAVVAQYTAEELY-TKREEVSAEIREALTERLAPFGIIVDDVL-ITNIDF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446678612 177 PPTVIDSINAKVTANQKTLQCEQEVKQREAEANMLRAEAAGQADA 221
Cdd:cd03401  150 PDEYEKAIEAKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEA 194
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 59-255 2.81e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 87.59  E-value: 2.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  59 YIFPTFKQMKTYD--------EPFSFQMSDGTTIGYHIGVAYKV-DPSKvttvfqtYRKGVDDITDTdLRQKITDALNRL 129
Cdd:COG0330   48 FKIPFIDRVRKVDvreqvldvPPQEVLTKDNNIVDVDAVVQYRItDPAK-------FLYNVENAEEA-LRQLAESALREV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612 130 ASKMTTDKFIDGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVIDSINAKVTANQKTLQC--------EQEV 201
Cdd:COG0330  120 IGKMTLDEVLSTGRDEINAEIREELQEALDPYGIEVVDVE-IKDIDPPEEVQDAMEDRMKAEREREAAileaegyrEAAI 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446678612 202 KQREAEANMLRAEAAGQADAIRTKAQAEADAIRLRGEALRQNPNVMELEAINKW 255
Cdd:COG0330  199 IRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEAL 252
PHB smart00244
prohibitin homologues; prohibitin homologues
 59-188 5.31e-11

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 59.60  E-value: 5.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612    59 YIFPTFKQMKTYDEPFSFQMSDGTTIGYHIGVAYkVDPSKVTTVFQTYrKGVDDITDTDLRQKITDALNRLASKMTTDKF 138
Cdd:smart00244  34 FIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA-VVYYRVLDPLRAV-YRVLDADYAVIEQLAQTTLRSVIGKRTLDEL 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 446678612   139 IDGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVIDSINAKV 188
Cdd:smart00244 112 LTDQREKISENIREELNEAAEAWGIKVEDVE-IKDIRLPEEIKEAMEAQQ 160
growth_prot_Scy NF041483
polarized growth protein Scy;
193-239 7.81e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 7.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 446678612  193 KTLQceqevKQREAEANMLRAEAAgqADAIRTKAQAEADAIRLRGEA 239
Cdd:NF041483  625 RTLQ-----AQAEQEAERLRTEAA--ADASAARAEGENVAVRLRSEA 664
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
192-263 1.05e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.32  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446678612 192 QKTLQCEQeVKQREAEANMLRAEAAGQADAIRTKAQAEADAIRLRGEALRQNPNVMELEAINKwngTLPQYM 263
Cdd:COG2268  303 EAELEADV-RKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIE---KLPEIA 370
growth_prot_Scy NF041483
polarized growth protein Scy;
190-239 2.35e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446678612  190 ANQKTLQCEQEVKQREAEANMLRAEAAGQADAIRTKA---------QAEADAIRLRGEA 239
Cdd:NF041483  584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAaerirtlqaQAEQEAERLRTEA 642
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 205-263 2.37e-04

Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.


Pssm-ID: 435047 [Multi-domain]  Cd Length: 121  Bit Score: 40.00  E-value: 2.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678612  205 EAEAnmlRAEAA-GQADAIRTKAQAEADAIRLRGEALRQN-PNVMELEAINKWNGTLPQYM 263
Cdd:pfam15975   1 EAEA---EADAIkLRAEAKRKKALAEAEGIRALNEAENALsDEQIALQVKLALLEALPEII 58
growth_prot_Scy NF041483
polarized growth protein Scy;
196-241 3.21e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 3.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446678612  196 QCEQEVKQREAEANMLRAEAAGQADAIRtkAQAEADAIRLRGEALR 241
Cdd:NF041483  521 QAEETLERTRAEAERLRAEAEEQAEEVR--AAAERAARELREETER 564
growth_prot_Scy NF041483
polarized growth protein Scy;
183-239 2.21e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446678612  183 SINAKVTANQKTLQCEQEVKQREAEANMLRAEAAGQADAIRTKA------------QAEADAIRLRGEA 239
Cdd:NF041483  381 SEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvELQEEARRLRGEA 449
growth_prot_Scy NF041483
polarized growth protein Scy;
196-239 5.31e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 38.27  E-value: 5.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446678612  196 QCEQEVKQREAEANMLRAEAAG------------QADAIRTKAQAEADAIRLRGEA 239
Cdd:NF041483  958 QAEQLIAEATGEAERLRAEAAEtvgsaqqhaeriRTEAERVKAEAAAEAERLRTEA 1013
 
Name Accession Description Interval E-value
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 22-208 6.20e-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: 97.78  E-value: 6.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612   22 RVEPGNVGIKVNklgDDKGVGEVVGVGRYWTGWNTEVYIFPTfKQMKTYDEPFSFQMSDGTTIGYHIGVAYKVDPSKVTT 101
Cdd:pfam01145   2 IVPPGEVGVVTR---FGKLSRVLEPGLHFIIPFIQRVVTVDV-RVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  102 VFQTYRKGVDDitDTDLRQKITDALNRLASKMTTDKFIdGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVI 181
Cdd:pfam01145  78 LVQNVFGSDDL--QELLRRVLESALREIIARYTLEELL-SNREELAEEIKNALQEELAKYGVEIIDVQ-ITDIDPPPEIA 153

                         170       180
                  ....*....|....*....|....*..
gi 446678612  182 DSINAKVTANQKTlqcEQEVKQREAEA 208
Cdd:pfam01145 154 EAIEAKQTAEQEA---EAEIARAEAEA 177
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 23-221 2.45e-22

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: 91.42  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  23 VEPGNVGIKVNKLGDDKGVGevvgvgrYWTG------WNTEVYIFPTfkQMKTYDEPFSFQMSDGTTIGYHIGVAYKVDP 96
Cdd:cd03401    4 VDAGEVGVVFRRGKGVKDEV-------LGEGlhfkipWIQVVIIYDV--RTQPREITLTVLSKDGQTVNIDLSVLYRPDP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  97 SKVTTVFQTYRkgvDDITDTDLRQKITDALNRLASKMTTDKFIdGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEY 176
Cdd:cd03401   75 EKLPELYQNLG---PDYEERVLPPIVREVLKAVVAQYTAEELY-TKREEVSAEIREALTERLAPFGIIVDDVL-ITNIDF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446678612 177 PPTVIDSINAKVTANQKTLQCEQEVKQREAEANMLRAEAAGQADA 221
Cdd:cd03401  150 PDEYEKAIEAKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEA 194
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 59-255 2.81e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 87.59  E-value: 2.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  59 YIFPTFKQMKTYD--------EPFSFQMSDGTTIGYHIGVAYKV-DPSKvttvfqtYRKGVDDITDTdLRQKITDALNRL 129
Cdd:COG0330   48 FKIPFIDRVRKVDvreqvldvPPQEVLTKDNNIVDVDAVVQYRItDPAK-------FLYNVENAEEA-LRQLAESALREV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612 130 ASKMTTDKFIDGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVIDSINAKVTANQKTLQC--------EQEV 201
Cdd:COG0330  120 IGKMTLDEVLSTGRDEINAEIREELQEALDPYGIEVVDVE-IKDIDPPEEVQDAMEDRMKAEREREAAileaegyrEAAI 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446678612 202 KQREAEANMLRAEAAGQADAIRTKAQAEADAIRLRGEALRQNPNVMELEAINKW 255
Cdd:COG0330  199 IRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEAL 252
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 57-239 1.99e-12

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: 65.20  E-value: 1.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  57 EVYIFPtfKQMKTYD-EPFSFQMSDGTTIGYHIGVAYKV-DPSKVTTVFQTyrkgvDDITDTDLRQKITDALNRLASKMT 134
Cdd:cd03405   37 NVRKFD--KRILTLDgPPEEVLTKDKKRLIVDSYARWRItDPLRFYQSVGG-----EEGAESRLDDIVDSALRNEIGKRT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612 135 TDKFIDGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVIDSInakvtanqktlqCEQEVKQREAEANMLRAE 214
Cdd:cd03405  110 LAEVVSGGRDELMEEILEQANEEAKEYGIEVVDVR-IKRIDLPEEVSESV------------YERMRAERERIAAEYRAE 176

                        170       180       190
                 ....*....|....*....|....*....|....
gi 446678612 215 AAGQADAIRTKA---------QAEADAIRLRGEA 239
Cdd:cd03405  177 GEEEAEKIRAEAdrertvilaEAYREAEEIRGEG 210
PHB smart00244
prohibitin homologues; prohibitin homologues
 59-188 5.31e-11

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 59.60  E-value: 5.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612    59 YIFPTFKQMKTYDEPFSFQMSDGTTIGYHIGVAYkVDPSKVTTVFQTYrKGVDDITDTDLRQKITDALNRLASKMTTDKF 138
Cdd:smart00244  34 FIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA-VVYYRVLDPLRAV-YRVLDADYAVIEQLAQTTLRSVIGKRTLDEL 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 446678612   139 IDGGKSELLDAALKDIQEEMTPIGIQVMSLSyVGKPEYPPTVIDSINAKV 188
Cdd:smart00244 112 LTDQREKISENIREELNEAAEAWGIKVEDVE-IKDIRLPEEIKEAMEAQQ 160
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 71-178 6.41e-10

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: 55.45  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  71 DEPFSFQMSDGTTIGYHIGVAYKV-DPSKVttvFQTYRKGVDDITDTDLRQKITDALNRLASKMTTDKFIDgGKSELLDA 149
Cdd:cd02106    7 VRVEPVGTADGVPVAVDLVVQFRItDYNAL---PAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIIS-GRDEIAKA 82

                         90       100
                 ....*....|....*....|....*....
gi 446678612 150 ALKDIQEEMTPIGIQVMSLSyVGKPEYPP 178
Cdd:cd02106   83 VKEDLEEDLENFGVVISDVD-ITSIEPPD 110
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 110-241 1.00e-08

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: 54.83  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612 110 VDDITDTdLRQKITDALNRLASKMTTDKFIDGGKSELLDAALKDIQEEMTP--IGIQVMSLSyVGKPEYPPTVIDSINAK 187
Cdd:cd03404  102 VRDPEET-LRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRydLGIEIVQVQ-LQDADPPEEVQDAFDDV 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446678612 188 VTANQktlQCEQEVKQREAEANMLRAEAAGQADAIRTKAQAEADAIRLR--GEALR 241
Cdd:cd03404  180 NAARQ---DKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARaeGDAAR 232
growth_prot_Scy NF041483
polarized growth protein Scy;
193-239 7.81e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 7.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 446678612  193 KTLQceqevKQREAEANMLRAEAAgqADAIRTKAQAEADAIRLRGEA 239
Cdd:NF041483  625 RTLQ-----AQAEQEAERLRTEAA--ADASAARAEGENVAVRLRSEA 664
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 90-242 4.03e-05

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: 44.11  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612  90 VAYKVDPSKVTTVFqtYRKgvdditdTDLRQKIT----DALNRLASKMTTD-KFIDggKSELLDAALKDIQEEMTPIGIQ 164
Cdd:cd03407   65 VQYRVVPEKVYDAF--YKL-------TNPEQQIQsyvfDVVRASVPKLTLDeVFES--KDEIAKAVKEELAKVMSEYGYE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446678612 165 VMSlSYVGKPEYPPTVIDSINaKVTANQktlqceqevkqREAEAnmlrAEAAGQADAIR--TKAQAEADAIRLRGEALRQ 242
Cdd:cd03407  134 IVK-TLVTDIEPDASVKAAMN-EINAAQ-----------RLREA----AEEKAEAEKILqvKAAEAEAEAKRLQGVGIAE 196
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
192-263 1.05e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.32  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446678612 192 QKTLQCEQeVKQREAEANMLRAEAAGQADAIRTKAQAEADAIRLRGEALRQNPNVMELEAINKwngTLPQYM 263
Cdd:COG2268  303 EAELEADV-RKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIE---KLPEIA 370
growth_prot_Scy NF041483
polarized growth protein Scy;
190-239 2.35e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 2.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446678612  190 ANQKTLQCEQEVKQREAEANMLRAEAAGQADAIRTKA---------QAEADAIRLRGEA 239
Cdd:NF041483  584 AEERLTAAEEALADARAEAERIRREAAEETERLRTEAaerirtlqaQAEQEAERLRTEA 642
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 205-263 2.37e-04

Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.


Pssm-ID: 435047 [Multi-domain]  Cd Length: 121  Bit Score: 40.00  E-value: 2.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446678612  205 EAEAnmlRAEAA-GQADAIRTKAQAEADAIRLRGEALRQN-PNVMELEAINKWNGTLPQYM 263
Cdd:pfam15975   1 EAEA---EADAIkLRAEAKRKKALAEAEGIRALNEAENALsDEQIALQVKLALLEALPEII 58
growth_prot_Scy NF041483
polarized growth protein Scy;
196-241 3.21e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 3.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446678612  196 QCEQEVKQREAEANMLRAEAAGQADAIRtkAQAEADAIRLRGEALR 241
Cdd:NF041483  521 QAEETLERTRAEAERLRAEAEEQAEEVR--AAAERAARELREETER 564
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 185-239 4.45e-04

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 38.96  E-value: 4.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446678612  185 NAKVTANQKTLQCEQEVKQ--REAEANM----------LRAEAAGQADAIRTKAQAEADAIRLRGEA 239
Cdd:pfam16999  23 AARKEAEREVEAAEAEAARilREAEAKAkalqaeyrqeLAAETARIREEARARAEAEAQAVRTRAEG 89
growth_prot_Scy NF041483
polarized growth protein Scy;
183-239 2.21e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446678612  183 SINAKVTANQKTLQCEQEVKQREAEANMLRAEAAGQADAIRTKA------------QAEADAIRLRGEA 239
Cdd:NF041483  381 SEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvELQEEARRLRGEA 449
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
198-240 2.93e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 2.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446678612 198 EQEVKQREAEANM-LRAEAagQADAIRTKAQAEADAIRLRGEAL 240
Cdd:COG2268  298 EAEREEAELEADVrKPAEA--EKQAAEAEAEAEAEAIRAKGLAE 339
growth_prot_Scy NF041483
polarized growth protein Scy;
196-239 5.31e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 38.27  E-value: 5.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446678612  196 QCEQEVKQREAEANMLRAEAAG------------QADAIRTKAQAEADAIRLRGEA 239
Cdd:NF041483  958 QAEQLIAEATGEAERLRAEAAEtvgsaqqhaeriRTEAERVKAEAAAEAERLRTEA 1013
 
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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