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Conserved domains on  [gi|1720364150|ref|XP_030101417|]
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flotillin-2 isoform X1 [Mus musculus]

Protein Classification

flotillin family protein( domain architecture ID 11455184)

flotillin family protein may act as a scaffolding protein within caveolar membranes, functionally participating in the formation of caveolae or caveolae-like vesicles

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
7-390 6.39e-74

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 236.69  E-value: 6.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   7 RLSLEVMTI-LCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQ 85
Cdd:COG2268    65 RMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  86 IYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEML 165
Cdd:COG2268   145 LNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 166 DVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILR 240
Cdd:COG2268   225 EAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQR---QLEIAEREREIELQEKEAER 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 241 TDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaekirkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKM 320
Cdd:COG2268   302 EEAELEADVRKPAEAEKQAAEAEA----------------------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAIL 359

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364150 321 ALVLEALPQIAAKISAPLTKVDEIVVLSGDNSK--VTSEVNRLLAELPASVHALTGVDLSKipLIKNATGAQ 390
Cdd:COG2268   360 LMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVAEALAPLLESLLEETGLDLPG--LLKGLTGAG 429
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
7-390 6.39e-74

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 236.69  E-value: 6.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   7 RLSLEVMTI-LCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQ 85
Cdd:COG2268    65 RMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  86 IYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEML 165
Cdd:COG2268   145 LNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 166 DVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILR 240
Cdd:COG2268   225 EAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQR---QLEIAEREREIELQEKEAER 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 241 TDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaekirkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKM 320
Cdd:COG2268   302 EEAELEADVRKPAEAEKQAAEAEA----------------------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAIL 359

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364150 321 ALVLEALPQIAAKISAPLTKVDEIVVLSGDNSK--VTSEVNRLLAELPASVHALTGVDLSKipLIKNATGAQ 390
Cdd:COG2268   360 LMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVAEALAPLLESLLEETGLDLPG--LLKGLTGAG 429
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 7-141 2.05e-59

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 189.25  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   7 RLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQI 86
Cdd:cd03399    11 RLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEI 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364150  87 YQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRD 141
Cdd:cd03399    91 YQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 24-151 2.41e-15

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: 73.51  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  24 TSEGVPLFVTGVAQVKIMTEKELLAVAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 103
Cdd:pfam01145  54 TKDGVPVNVDVTVIYRVNPDDPPKLVQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQE 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720364150 104 DVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAER 151
Cdd:pfam01145 130 ELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 50-232 7.63e-12

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 63.06  E-value: 7.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   50 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 129
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  130 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 207
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139

                          170       180
                   ....*....|....*....|....*
gi 1720364150  208 GAReqqkIRQEEIEIEVVQRKKQIA 232
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
PTZ00121 PTZ00121
MAEBL; Provisional
 149-321 1.63e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  149 AERDAGIReAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRK 228
Cdd:PTZ00121  1266 ARRQAAIK-AEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  229 KQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER----- 303
Cdd:PTZ00121  1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkade 1422

                          170
                   ....*....|....*...
gi 1720364150  304 MKLKAEAYQKYGDAAKMA 321
Cdd:PTZ00121  1423 AKKKAEEKKKADEAKKKA 1440
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 170-353 6.31e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.45  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 170 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 249
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 250 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 325
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218

                         170       180
                  ....*....|....*....|....*...
gi 1720364150 326 ALPQIAAKISAPLTKVDEIVVLSGDNSK 353
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
7-390 6.39e-74

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 236.69  E-value: 6.39e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   7 RLSLEVMTI-LCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQ 85
Cdd:COG2268    65 RMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  86 IYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEML 165
Cdd:COG2268   145 LNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 166 DVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILR 240
Cdd:COG2268   225 EAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQR---QLEIAEREREIELQEKEAER 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 241 TDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaekirkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKM 320
Cdd:COG2268   302 EEAELEADVRKPAEAEKQAAEAEA----------------------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAIL 359

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720364150 321 ALVLEALPQIAAKISAPLTKVDEIVVLSGDNSK--VTSEVNRLLAELPASVHALTGVDLSKipLIKNATGAQ 390
Cdd:COG2268   360 LMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVAEALAPLLESLLEETGLDLPG--LLKGLTGAG 429
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 7-141 2.05e-59

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 189.25  E-value: 2.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   7 RLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQI 86
Cdd:cd03399    11 RLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEI 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720364150  87 YQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRD 141
Cdd:cd03399    91 YQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 11-123 2.70e-19

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: 82.41  E-value: 2.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  11 EVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVAceqfLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDR 90
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFY----LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGR 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720364150  91 DQFAKLVREVAAPDVGRMGIEILSFTIKDVYDK 123
Cdd:cd02106    77 DEIAKAVKEDLEEDLENFGVVISDVDITSIEPP 109
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 24-151 2.41e-15

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: 73.51  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  24 TSEGVPLFVTGVAQVKIMTEKELLAVAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 103
Cdd:pfam01145  54 TKDGVPVNVDVTVIYRVNPDDPPKLVQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQE 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720364150 104 DVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAER 151
Cdd:pfam01145 130 ELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 50-232 7.63e-12

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 63.06  E-value: 7.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   50 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 129
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  130 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 207
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139

                          170       180
                   ....*....|....*....|....*
gi 1720364150  208 GAReqqkIRQEEIEIEVVQRKKQIA 232
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 24-163 9.29e-09

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 56.00  E-value: 9.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  24 TSEGVPLFVTGVAQVKIMTEKELLavaceqflgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIY-QDRDQFAKLVREVAA 102
Cdd:COG0330    75 TKDNNIVDVDAVVQYRITDPAKFL---------YNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQ 145

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720364150 103 PDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKE 163
Cdd:COG0330   146 EALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQ 206
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 276-350 1.04e-07

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: 50.01  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364150 276 QAEAEKIRKIGEAEAavIEAMGKAEAERMKLKAEAYQKYGD---AAKMAL-VLEALPQIAAKISAPLTKVDEIVVLSGD 350
Cdd:pfam15975   1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALSDeqiALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVD 77
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 253-354 2.36e-07

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 51.76  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 253 AEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALvLEALPQIAA 332
Cdd:COG0330   179 AEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRS-LEALEEVLS 257

                          90       100
                  ....*....|....*....|..
gi 1720364150 333 KISapltkvdEIVVLSGDNSKV 354
Cdd:COG0330   258 PNS-------KVIVLPPDGNGF 272
PTZ00121 PTZ00121
MAEBL; Provisional
 149-321 1.63e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  149 AERDAGIReAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRK 228
Cdd:PTZ00121  1266 ARRQAAIK-AEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  229 KQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER----- 303
Cdd:PTZ00121  1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkade 1422

                          170
                   ....*....|....*...
gi 1720364150  304 MKLKAEAYQKYGDAAKMA 321
Cdd:PTZ00121  1423 AKKKAEEKKKADEAKKKA 1440
PTZ00121 PTZ00121
MAEBL; Provisional
 148-364 1.76e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  148 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 218
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  219 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 298
Cdd:PTZ00121  1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720364150  299 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 364
Cdd:PTZ00121  1683 AEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00121 PTZ00121
MAEBL; Provisional
 147-343 1.81e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  147 AEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEE------- 219
Cdd:PTZ00121  1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaee 1651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  220 ---IEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAE----AEKIRKIGEAEAAV 292
Cdd:PTZ00121  1652 lkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKAEEENKIK 1731

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720364150  293 IEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDE 343
Cdd:PTZ00121  1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
PTZ00121 PTZ00121
MAEBL; Provisional
 139-321 3.13e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  139 QRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIAD--------SKRAFELQKSA-----FSEEVNIKTAEAQLAYE 205
Cdd:PTZ00121  1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkkaeeAKKADEAKKKAeeakkKADAAKKKAEEAKKAAE 1346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  206 LQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKI 285
Cdd:PTZ00121  1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720364150  286 GEAEAAVIEAMGKAE----AERMKLKAEAYQKYGDAAKMA 321
Cdd:PTZ00121  1427 AEEKKKADEAKKKAEeakkADEAKKKAEEAKKAEEAKKKA 1466
PTZ00121 PTZ00121
MAEBL; Provisional
 148-319 5.04e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 5.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  148 EAERDAGIREAECKKEMLDVKFMADTK-IADSKRAFELQKSafsEEV----NIKTAEAQLAYELQGAREQQKIRQEEIEI 222
Cdd:PTZ00121  1150 DAKRVEIARKAEDARKAEEARKAEDAKkAEAARKAEEVRKA---EELrkaeDARKAEAARKAEEERKAEEARKAEDAKKA 1226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  223 EVVQRKKQIAVEAQEILRTDKE-------------LIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQaEAEKIRKIGEAE 289
Cdd:PTZ00121  1227 EAVKKAEEAKKDAEEAKKAEEErnneeirkfeearMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKAD 1305

                          170       180       190
                   ....*....|....*....|....*....|
gi 1720364150  290 AAVIEAMGKAEAERMKLKAEAYQKYGDAAK 319
Cdd:PTZ00121  1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
PTZ00121 PTZ00121
MAEBL; Provisional
 147-344 1.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  147 AEAERD-AGIREAECKKEMLDVKFMADTKIADSKRAFELQKSafsEEVNiKTAEAQLAYELQGAREQQKIRQEEIEIEVV 225
Cdd:PTZ00121  1245 AEEERNnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA---EEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEA 1320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  226 QRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqAEAEKIRKIGE---AEAAVIEAMGKAEAE 302
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK------AEAAEKKKEEAkkkADAAKKKAEEKKKAD 1394

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720364150  303 RMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEI 344
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 170-353 6.31e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.45  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 170 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 249
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 250 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 325
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218

                         170       180
                  ....*....|....*....|....*...
gi 1720364150 326 ALPQIAAKISAPLTKVDEIVVLSGDNSK 353
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 22-120 7.35e-05

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). 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. 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. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 41.79  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  22 IETSEGVPLFVTGVAQVKImtEKELLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVA 101
Cdd:cd13434    15 ILTKDNVTVSVDAVVYYRV--VDPLKAVL-------NVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEIL 85

                          90
                  ....*....|....*....
gi 1720364150 102 APDVGRMGIEILSFTIKDV 120
Cdd:cd13434    86 DEATDPWGIKVERVEIKDI 104
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 171-319 1.03e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 171 ADTKIADSKRAFELQKSAfsEEVNIKTAEAQlayELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVR 250
Cdd:PRK09510   72 KSAKRAEEQRKKKEQQQA--EELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 251 RPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAE-RMKLKAEAYQKYGDAAK 319
Cdd:PRK09510  147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAK 216
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 251-313 1.25e-04

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: 43.25  E-value: 1.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364150 251 RPAEAEAHRiqqiAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 313
Cdd:cd03405   166 RERIAAEYR----AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224
PTZ00121 PTZ00121
MAEBL; Provisional
 134-343 1.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  134 QTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSA----FSEEVNIKTAEAQLAYELQGA 209
Cdd:PTZ00121  1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKK 1491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  210 REQQKIRQEEIEIEVVQRKK-QIAVEAQEILRTDKELIATVRRPAEA-----------EAHRIQQIAEGEKVKQVLLAQA 277
Cdd:PTZ00121  1492 AEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKK 1571

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364150  278 EAE-------KIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDE 343
Cdd:PTZ00121  1572 AEEdknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 5-153 2.49e-04

Slipin-3 (SLP-3), 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 vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 41.17  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150   5 LLRLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEkeLLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTVE 84
Cdd:cd08828    15 FIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSA--VKAVA-------NVNNVHIATFLLAQTTLRNVLGTQTLA 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720364150  85 QIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDA 153
Cdd:cd08828    86 QILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
PTZ00121 PTZ00121
MAEBL; Provisional
 147-360 4.15e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  147 AEAERDAGIREAECKKEMLDVKFMADTKIADS---KRAFELQKSafSEEVNIKTAEaqlayeLQGAREQQKIRQEEIEIE 223
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKA--EEENKIKAAE------EAKKAEEDKKKAEEAKKA 1683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  224 VVQRKKqiAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 303
Cdd:PTZ00121  1684 EEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364150  304 MKLKAEAYQKYGDAAKMALVLEALPQiaaKISAPLTKVDEIVVLSGDNSKVTSEVNR 360
Cdd:PTZ00121  1762 LKKEEEKKAEEIRKEKEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
PTZ00121 PTZ00121
MAEBL; Provisional
 139-319 5.15e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  139 QRDADIGVAEAERDAG-IREAECKKEMLDVKFMADTKIADS--------KRAFELQKSAfsEEVNIKTAEAQLAYELQGA 209
Cdd:PTZ00121  1342 KKAAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAakkkaeekKKADEAKKKA--EEDKKKADELKKAAAAKKK 1419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  210 REQQKIRQEEI-EIEVVQRKKQIAVEAQEILRTDKEliatvRRPAEAEAHRIQQIAEGEKVKQvllaqaEAEKIRKIGEA 288
Cdd:PTZ00121  1420 ADEAKKKAEEKkKADEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKKKAEEAKKADEAKK------KAEEAKKADEA 1488

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720364150  289 EAAVIEAmgKAEAERMKLKAEAYQKYGDAAK 319
Cdd:PTZ00121  1489 KKKAEEA--KKKADEAKKAAEAKKKADEAKK 1517
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-120 6.01e-04

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 38.99  E-value: 6.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720364150  58 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDV 120
Cdd:cd08829    45 GVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDI 107
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 253-335 1.15e-03

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: 40.19  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 253 AEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAA 332
Cdd:cd03404   182 ARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEVLS 261


                  ...
gi 1720364150 333 KIS 335
Cdd:cd03404   262 NAS 264
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 22-120 1.42e-03

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


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 39.83  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  22 IETSEGVPLFVTGVAQVKImtekellaVACEQFLgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVA 101
Cdd:cd13438    52 ILTADKVALRVNLVATYRV--------VDPVKAV-ETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAV 122

                          90
                  ....*....|....*....
gi 1720364150 102 APDVGRMGIEILSFTIKDV 120
Cdd:cd13438   123 KEAAAELGVEVLSVGVKDI 141
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 210-305 2.49e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 210 REQQKIRQEEIEIEVVQRKKqiaVEAQEILRTDKEliATVRRpaEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKigEAE 289
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRE---LERLQMERQQKN--ERVRQ--ELEAARKVKILEEERQRKIQQQKVEMEQIRA--EQE 430

                          90
                  ....*....|....*.
gi 1720364150 290 AAVIEAMGKAEAERMK 305
Cdd:pfam17380 431 EARQREVRRLEEERAR 446
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 30-120 4.09e-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: 259806  Cd Length: 217  Bit Score: 38.30  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  30 LFVTGVA-QVKIMTEKELLavacEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEqiyqdrdqFAKLVREVAAPDVGRM 108
Cdd:cd03408   117 LFLTEVVgTQGTFTTDEIE----EQLRSEIVQALKDAIAELSISGLDLALEANLDE--------LSAALKEKLAPEFEKY 184

                          90
                  ....*....|..
gi 1720364150 109 GIEILSFTIKDV 120
Cdd:cd03408   185 GLELTSFGIESI 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 191-344 5.56e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 191 EEVNIKTAEAQLAyELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRpAEAEAHRIQQIAEGEKVK 270
Cdd:COG1196   251 LEAELEELEAELA-ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAEL 328

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720364150 271 QVLLAQAEAEKIrkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEI 344
Cdd:COG1196   329 EEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 208-326 6.74e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.25  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 208 GAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAE-----AHRIQQIAEGEKVKQVLLAQAEAEKI 282
Cdd:PRK09510   73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEeaakqAALKQKQAEEAAAKAAAAAKAKAEAE 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1720364150 283 RKIGEAEAAVIEAMGKAEAE---RMKLKAEAYQKYGDAAKMALVLEA 326
Cdd:PRK09510  153 AKRAAAAAKKAAAEAKKKAEaeaAKKAAAEAKKKAEAEAAAKAAAEA 199
PRK11029 PRK11029
protease modulator HflC;
184-313 8.53e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 37.80  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150 184 LQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIE----------IEVVQ-RKKQIAVEAQ------EILRTDKELI 246
Cdd:PRK11029  155 LNSGSAGTEDEVATPAADDAIASAAERVEAETKGKVPVinpnsmaalgIEVVDvRIKQINLPTEvsdaiyNRMRAEREAV 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720364150 247 AtvRRpaeaeaHRIQQIAEGEKVKqvllAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 313
Cdd:PRK11029  235 A--RR------HRSQGQEEAEKLR----ATADYEVTRTLAEAERQGRIMRGEGDAEAAKLFADAFSQ 289
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 58-153 9.09e-03

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


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 36.84  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720364150  58 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAV 137
Cdd:cd13775    42 EVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAE 121

                          90
                  ....*....|....*.
gi 1720364150 138 VQRDADIGVAEAERDA 153
Cdd:cd13775   122 REKNARVILAEAEKEI 137
 
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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