|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
6-368 |
2.72e-70 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 226.68 E-value: 2.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 6 RCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLV 85
Cdd:COG2268 77 RTEGLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 86 REVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT---- 161
Cdd:COG2268 157 QEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReiet 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 162 -KIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRP 240
Cdd:COG2268 237 aRIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 241 AEAEAHRIQQIAegekvkqvllaqaeaekirkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAA 320
Cdd:COG2268 314 AEAEKQAAEAEA----------------------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034598930 321 KIAAPLTKVDEIVVLSGDNSK--VTSEVNRLLAELPASVHALTGVDLSKI 368
Cdd:COG2268 372 AAAKPLEKIDKITIIDGGNGGngAGSAVAEALAPLLESLLEETGLDLPGL 421
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
1-129 |
3.10e-56 |
|
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: 180.78 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 1 MTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQ 80
Cdd:cd03399 17 MTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEIYQDREK 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034598930 81 FAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRD 129
Cdd:cd03399 97 FAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
12-139 |
3.44e-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: 72.74 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 12 TAEGVALTVTGVAQVKIMTEKELLAVAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 91
Cdd:pfam01145 54 TKDGVPVNVDVTVIYRVNPDDPPKLVQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQE 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034598930 92 DVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAER 139
Cdd:pfam01145 130 ELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
38-220 |
1.48e-11 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 61.91 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 38 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 117
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 118 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 195
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139
|
170 180
....*....|....*....|....*
gi 1034598930 196 GAReqqkIRQEEIEIEVVQRKKQIA 220
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-352 |
1.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 136 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 206
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 207 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 286
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598930 287 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 352
Cdd:PTZ00121 1683 AEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
158-341 |
2.37e-04 |
|
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: 42.91 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 158 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 237
Cdd:TIGR02794 59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 238 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 313
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218
|
170 180
....*....|....*....|....*...
gi 1034598930 314 ALPQIAAKIAAPLTKVDEIVVLSGDNSK 341
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
6-368 |
2.72e-70 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 226.68 E-value: 2.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 6 RCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLV 85
Cdd:COG2268 77 RTEGLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 86 REVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT---- 161
Cdd:COG2268 157 QEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReiet 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 162 -KIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRP 240
Cdd:COG2268 237 aRIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 241 AEAEAHRIQQIAegekvkqvllaqaeaekirkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAA 320
Cdd:COG2268 314 AEAEKQAAEAEA----------------------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034598930 321 KIAAPLTKVDEIVVLSGDNSK--VTSEVNRLLAELPASVHALTGVDLSKI 368
Cdd:COG2268 372 AAAKPLEKIDKITIIDGGNGGngAGSAVAEALAPLLESLLEETGLDLPGL 421
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
1-129 |
3.10e-56 |
|
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: 180.78 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 1 MTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQ 80
Cdd:cd03399 17 MTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEIYQDREK 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034598930 81 FAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRD 129
Cdd:cd03399 97 FAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
1-111 |
8.90e-21 |
|
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: 86.26 E-value: 8.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 1 MTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVAceqfLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQ 80
Cdd:cd02106 3 QFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFY----LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDE 78
|
90 100 110
....*....|....*....|....*....|.
gi 1034598930 81 FAKLVREVAAPDVGRMGIEILSFTIKDVYDK 111
Cdd:cd02106 79 IAKAVKEDLEEDLENFGVVISDVDITSIEPP 109
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
12-139 |
3.44e-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: 72.74 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 12 TAEGVALTVTGVAQVKIMTEKELLAVAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 91
Cdd:pfam01145 54 TKDGVPVNVDVTVIYRVNPDDPPKLVQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQE 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034598930 92 DVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAER 139
Cdd:pfam01145 130 ELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
38-220 |
1.48e-11 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 61.91 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 38 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 117
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 118 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 195
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139
|
170 180
....*....|....*....|....*
gi 1034598930 196 GAReqqkIRQEEIEIEVVQRKKQIA 220
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
12-151 |
2.36e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 54.85 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 12 TAEGVALTVTGVAQVKIMTEKELLavaceqflgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIY-QDRDQFAKLVREVAA 90
Cdd:COG0330 75 TKDNNIVDVDAVVQYRITDPAKFL---------YNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQ 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034598930 91 PDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKE 151
Cdd:COG0330 146 EALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQ 206
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
264-338 |
2.29e-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: 49.24 E-value: 2.29e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034598930 264 QAEAEKIRKIGEAEAavIEAMGKAEAERMKLKAEAYQKYGD---AAKMAL-VLEALPQIAAKIAAPLTKVDEIVVLSGD 338
Cdd:pfam15975 1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALSDeqiALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVD 77
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
241-342 |
4.47e-07 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 50.61 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 241 AEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALvLEALPQIAA 320
Cdd:COG0330 179 AEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRS-LEALEEVLS 257
|
90 100
....*....|....*....|..
gi 1034598930 321 kiaapltKVDEIVVLSGDNSKV 342
Cdd:COG0330 258 -------PNSKVIVLPPDGNGF 272
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-352 |
1.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 136 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 206
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 207 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 286
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034598930 287 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 352
Cdd:PTZ00121 1683 AEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
137-309 |
3.26e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 137 AERDAGIReAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRK 216
Cdd:PTZ00121 1266 ARRQAAIK-AEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 217 KQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER----- 291
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkade 1422
|
170
....*....|....*...
gi 1034598930 292 MKLKAEAYQKYGDAAKMA 309
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKA 1440
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-348 |
3.32e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 135 AEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEE------- 207
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaee 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 208 ---IEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAE----AEKIRKIGEAEAAV 280
Cdd:PTZ00121 1652 lkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKAEEENKIK 1731
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034598930 281 IEAMGKAEAERMKLKAEAYQKYGDAAKMAlvleALPQIAAKIAAPLTKVDEIVVLSG---DNSKVTSEVNR 348
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIA----HLKKEEEKKAEEIRKEKEAVIEEEldeEDEKRRMEVDK 1798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-309 |
6.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 127 QRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIAD--------SKRAFELQKSA-----FSEEVNIKTAEAQLAYE 193
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkkaeeAKKADEAKKKAeeakkKADAAKKKAEEAKKAAE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 194 LQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKI 273
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034598930 274 GEAEAAVIEAMGKAE----AERMKLKAEAYQKYGDAAKMA 309
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEeakkADEAKKKAEEAKKAEEAKKKA 1466
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-307 |
1.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 136 EAERDAGIREAECKKEMLDVKFMADTK-IADSKRAFELQKSafsEEV----NIKTAEAQLAYELQGAREQQKIRQEEIEI 210
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKkAEAARKAEEVRKA---EELrkaeDARKAEAARKAEEERKAEEARKAEDAKKA 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 211 EVVQRKKQIAVEAQEILRTDKE-------------LIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQaEAEKIRKIGEAE 277
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEErnneeirkfeearMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKAD 1305
|
170 180 190
....*....|....*....|....*....|
gi 1034598930 278 AAVIEAMGKAEAERMKLKAEAYQKYGDAAK 307
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-332 |
1.56e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 135 AEAERD-AGIREAECKKEMLDVKFMADTKIADSKRAFELQKSafsEEVNiKTAEAQLAYELQGAREQQKIRQEEIEIEVV 213
Cdd:PTZ00121 1245 AEEERNnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA---EEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 214 QRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqAEAEKIRKIGE---AEAAVIEAMGKAEAE 290
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK------AEAAEKKKEEAkkkADAAKKKAEEKKKAD 1394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034598930 291 RMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEI 332
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-332 |
1.65e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 136 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQR 215
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 216 KKqiaveAQEILRTDKEliatVRRPAEAEAhriqqiaEGEKVKQVLLAQAEAEKIRKigeAEAAVIEAMGKAEAERMKLK 295
Cdd:PTZ00121 1418 KK-----ADEAKKKAEE----KKKADEAKK-------KAEEAKKADEAKKKAEEAKK---AEEAKKKAEEAKKADEAKKK 1478
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034598930 296 AEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEI 332
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| SPFH_SLPs |
cd13434 |
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ... |
5-108 |
5.30e-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: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 5 PRCEdVETAEGVALTVTGVAQVKImtEKELLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKL 84
Cdd:cd13434 11 PPQE-ILTKDNVTVSVDAVVYYRV--VDPLKAVL-------NVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80
|
90 100
....*....|....*....|....
gi 1034598930 85 VREVAAPDVGRMGIEILSFTIKDV 108
Cdd:cd13434 81 LQEILDEATDPWGIKVERVEIKDI 104
|
|
| SPFH_eoslipins_u2 |
cd13438 |
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ... |
12-108 |
1.00e-04 |
|
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: 42.91 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 12 TAEGVALTVTGVAQVKImtekellaVACEQFLgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 91
Cdd:cd13438 54 TADKVALRVNLVATYRV--------VDPVKAV-ETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKE 124
|
90
....*....|....*..
gi 1034598930 92 DVGRMGIEILSFTIKDV 108
Cdd:cd13438 125 AAAELGVEVLSVGVKDI 141
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
239-301 |
1.77e-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: 42.48 E-value: 1.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034598930 239 RPAEAEAHRiqqiAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 301
Cdd:cd03405 166 RERIAAEYR----AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224
|
|
| SPFH_SLP-3 |
cd08828 |
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ... |
8-141 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 8 EDVETAEGVALTVTGVAQVKIMTEkeLLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVRE 87
Cdd:cd08828 30 QEILTKDSVTTQVDGVVYYRIQSA--VKAVA-------NVNNVHIATFLLAQTTLRNVLGTQTLAQILAGREEIAHSIQS 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034598930 88 VAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDA 141
Cdd:cd08828 101 ILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
158-341 |
2.37e-04 |
|
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: 42.91 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 158 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 237
Cdd:TIGR02794 59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 238 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 313
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218
|
170 180
....*....|....*....|....*...
gi 1034598930 314 ALPQIAAKIAAPLTKVDEIVVLSGDNSK 341
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-331 |
4.44e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 122 QTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSA----FSEEVNIKTAEAQLAYELQGA 197
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 198 REQQKIRQEEIEIEVVQRKK-QIAVEAQEILRTDKELIATVRRPAEA-----------EAHRIQQIAEGEKVKQVLLAQA 265
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKK 1571
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034598930 266 EAE-------KIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDE 331
Cdd:PTZ00121 1572 AEEdknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
159-324 |
6.70e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 159 ADTKIADSKRAFELQKSAfsEEVNIKTAEAQlayELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVR 238
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQA--EELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 239 RPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAE-RMKLKAEAYQKYGDAAKMALVLEALPQ 317
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
....*..
gi 1034598930 318 IAAKIAA 324
Cdd:PRK09510 227 AAKAAAE 233
|
|
| SPFH_paraslipin |
cd08829 |
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ... |
46-108 |
6.71e-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: 6.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034598930 46 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDV 108
Cdd:cd08829 45 GVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDI 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-348 |
9.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 135 AEAERDAGIREAECKKEMLDVKFMADTKIADS---KRAFELQKSafSEEVNIKTAEaqlayeLQGAREQQKIRQEEIEIE 211
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKA--EEENKIKAAE------EAKKAEEDKKKAEEAKKA 1683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 212 VVQRKKqiAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 291
Cdd:PTZ00121 1684 EEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034598930 292 MKLKAEAYQKYGDAAKMALVLEALPQiaaKIAAPLTKVDEIVVLSGDNSKVTSEVNR 348
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| SPFH_HflK |
cd03404 |
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
241-318 |
1.59e-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: 39.80 E-value: 1.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034598930 241 AEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQI 318
Cdd:cd03404 182 ARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
198-293 |
3.82e-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: 39.34 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034598930 198 REQQKIRQEEIEIEVVQRKKqiaVEAQEILRTDKEliATVRRpaEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKigEAE 277
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRE---LERLQMERQQKN--ERVRQ--ELEAARKVKILEEERQRKIQQQKVEMEQIRA--EQE 430
|
90
....*....|....*.
gi 1034598930 278 AAVIEAMGKAEAERMK 293
Cdd:pfam17380 431 EARQREVRRLEEERAR 446
|
|
| |
