|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2-339 |
1.31e-65 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 213.58 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 2 LAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDY 81
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 82 LHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQAD 156
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 157 LAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAes 236
Cdd:COG2268 266 AAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 237 vrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVtg 316
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398
|
330 340
....*....|....*....|...
gi 1622929039 317 eVLDILTRLPESVERLTGVSISQ 339
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLPG 420
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
1-96 |
3.68e-41 |
|
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: 141.10 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 1 MLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 80
Cdd:cd03399 50 EIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNG 129
|
90
....*....|....*.
gi 1622929039 81 YLHSLGKARTAQVQKD 96
Cdd:cd03399 130 YLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
5-187 |
3.62e-17 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 77.70 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 5 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 84
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 85 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVA 164
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141
|
170 180
....*....|....*....|...
gi 1622929039 165 KTKQqieeQRVQVQVVERAQQVA 187
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
23-106 |
8.49e-11 |
|
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: 60.03 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 23 ETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEA 102
Cdd:pfam01145 94 RVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARA 173
|
....
gi 1622929039 103 EAKR 106
Cdd:pfam01145 174 EAEA 177
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
97-269 |
3.14e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 97 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 176
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 177 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLI--MQAEAEAESVRMRGEAEaf 246
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLekVEEEARHEAAVLIKEIE-- 179
|
170 180
....*....|....*....|....*
gi 1622929039 247 aigARARAEAEQMAKK--AEAFQLY 269
Cdd:PRK12704 180 ---EEAKEEADKKAKEilAQAIQRC 201
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
160-264 |
1.12e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 40.97 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 160 QLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEiaRREKELEARVRKP-AEAERYKLERLA---EAEKSQliMQAEAEAE 235
Cdd:NF012221 1670 GKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGE--QNQANAEQDIDDAkADAEKRKDDALAkqnEAQQAE--SDANAAAN 1745
|
90 100
....*....|....*....|....*....
gi 1622929039 236 SVRMRGEAEAFAIGARArAEAEQMAKKAE 264
Cdd:NF012221 1746 DAQSRGEQDASAAENKA-NQAQADAKGAK 1773
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
87-274 |
5.97e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 38.65 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 164
Cdd:NF041483 432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 165 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAE 235
Cdd:NF041483 497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622929039 236 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 274
Cdd:NF041483 577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2-339 |
1.31e-65 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 213.58 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 2 LAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDY 81
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 82 LHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQAD 156
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 157 LAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAes 236
Cdd:COG2268 266 AAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 237 vrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVtg 316
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398
|
330 340
....*....|....*....|...
gi 1622929039 317 eVLDILTRLPESVERLTGVSISQ 339
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLPG 420
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
1-96 |
3.68e-41 |
|
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: 141.10 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 1 MLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 80
Cdd:cd03399 50 EIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNG 129
|
90
....*....|....*.
gi 1622929039 81 YLHSLGKARTAQVQKD 96
Cdd:cd03399 130 YLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
5-187 |
3.62e-17 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 77.70 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 5 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 84
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 85 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVA 164
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141
|
170 180
....*....|....*....|...
gi 1622929039 165 KTKQqieeQRVQVQVVERAQQVA 187
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
23-106 |
8.49e-11 |
|
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: 60.03 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 23 ETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEA 102
Cdd:pfam01145 94 RVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARA 173
|
....
gi 1622929039 103 EAKR 106
Cdd:pfam01145 174 EAEA 177
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
148-309 |
5.47e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 53.30 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 148 VNTRRAQ--ADLAYQLQVAKTKQQIEEQRVQVQVVERAQQV--AVQEQEIARREKElearvrkpaeaeryKLERLAEAEK 223
Cdd:COG0330 129 LSTGRDEinAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdAMEDRMKAERERE--------------AAILEAEGYR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 224 SQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLdMLLEKLPQVAEeisgpltSANKITLVS 303
Cdd:COG0330 195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFY-RSLEALEEVLS-------PNSKVIVLP 266
|
....*.
gi 1622929039 304 SGSGTM 309
Cdd:COG0330 267 PDGNGF 272
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
30-155 |
8.34e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 52.92 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 30 RAIMAHMTVEEIY-KDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDA 108
Cdd:COG0330 117 REVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREA 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622929039 109 GIREAKAKQEKVsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQA 155
Cdd:COG0330 197 AIIRAEGEAQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
83-284 |
1.30e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 83 HSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQ 162
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 163 VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLE-RLAEAEKSQLIMQAEAEAESVRMRG 241
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622929039 242 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQ 284
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
81-289 |
1.36e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 81 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLS----EIEMAKAQRDYELKKAAYDIEVNTRRAQAD 156
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 157 LAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvrkpAEAERYKLERLAEAEKSQLIMQAEAEAES 236
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-----AEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622929039 237 VRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 289
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
87-290 |
1.97e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKT 166
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 167 KQQIEEQRVQVQVVE-RAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAESVRMRGEAEA 245
Cdd:COG1196 336 EEELEELEEELEEAEeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622929039 246 FAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEIS 290
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
231-316 |
2.79e-05 |
|
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: 43.08 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 231 EAEAESVRMRGEAEafAIGARARAEAEQMAKKAEAFQLY---QEAAQLDM-LLEKLPQVAEEISGPLTSANKITLVSSGS 306
Cdd:pfam15975 1 EAEAEADAIKLRAE--AKRKKALAEAEGIRALNEAENALsdeQIALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVDG 78
|
90
....*....|
gi 1622929039 307 GTMGAAKVTG 316
Cdd:pfam15975 79 LGGGAAGGGG 88
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
97-269 |
3.14e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 97 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 176
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 177 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLI--MQAEAEAESVRMRGEAEaf 246
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLekVEEEARHEAAVLIKEIE-- 179
|
170 180
....*....|....*....|....*
gi 1622929039 247 aigARARAEAEQMAKK--AEAFQLY 269
Cdd:PRK12704 180 ---EEAKEEADKKAKEilAQAIQRC 201
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-281 |
6.18e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqylseiEMAKAqrdyELKKAAYDIEVNTRRAQADlayQLQVAKT 166
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 167 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELE--ARVRKPAEAERYKLERLAEAEksQLIMQAEAEAESVRMRGEAE 244
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAE 1454
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622929039 245 AFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEK 281
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-288 |
1.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 85 LGKARTAQVQKDARIGEaEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVA 164
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 165 KTK----QQIEEQRVQVQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLAEAEKSQLIMQAEAEAESV 237
Cdd:PTZ00121 1606 KMKaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622929039 238 RMRGEAEAFAIGARARAEAEQMAKKAE-----AFQLYQEAAQLDMLLEKLPQVAEE 288
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAeekkkAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-278 |
1.44e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEAEAKRDagirEAKAKQEKVSAQYLSEIEMAK----AQRDYELKKAAYDIEVNTRRAQADLAYQLQ 162
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 163 VAKTKQQIEEQRVQVQVVERAQQVAVQEQEiARREKELearvRKPAEAERYKLERLAEAEKSQLIMQAEAEAESVRMRGE 242
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622929039 243 AEAFAIGARARAE----AEQMAKKAEAFQLYQEAAQLDML 278
Cdd:PTZ00121 1488 AKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
87-261 |
2.38e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqylseiEMAKAQRDYELKKAAydIEVNTRRAQAdlayqlqvAKT 166
Cdd:PRK05035 531 RARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQA------ANAEAEEEVDPKKAA--VAAAIARAKA--------KKA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 167 KQQIEEQRVQVQVVERAQQVAVQEQEIARRE--KELEARVRKPAEAERYKLERL------AEAEKSQLIMQAEAEAESVR 238
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKakKAEQQANAEPEEPVDPRKAAVaaaiarAKARKAAQQQANAEPEEAED 674
|
170 180
....*....|....*....|...
gi 1622929039 239 MRGEAEAFAIgarARAEAEQMAK 261
Cdd:PRK05035 675 PKKAAVAAAI---ARAKAKKAAQ 694
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
162-268 |
2.79e-04 |
|
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: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.28 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 162 QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvRKPAEaeryklerLAEAEKSQLIMqaEAEAESVRMRG 241
Cdd:cd03406 163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEA--EKDAE--------VAKIQMQQKIM--EKEAEKKISEI 230
|
90 100
....*....|....*....|....*....
gi 1622929039 242 EAEAFAIGARARAEAE--QMAKKAEAFQL 268
Cdd:cd03406 231 EDEMHLAREKARADAEyyRALREAEANKL 259
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
89-289 |
3.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 89 RTAQVQKDARIGEAEAKRDAGIR---EAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAK 165
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRkaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 166 TKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA----EAEKSQLIMQAEAE----A 234
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeAKKAEEDEKKAAEALKkeaeEAKKAEELKKKEAEekkkA 1718
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622929039 235 ESVRmRGEAEAFAIGARARAEAEQMAKKAEAFQLYQ-EAAQLDMLLEKLPQVAEEI 289
Cdd:PTZ00121 1719 EELK-KAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeEKKKIAHLKKEEEKKAEEI 1773
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
165-226 |
5.72e-04 |
|
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: 259804 [Multi-domain] Cd Length: 293 Bit Score: 41.13 E-value: 5.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622929039 165 KTKQQIEEQRV-QVQVVERAQQVAvqEQEIARREKELE-----ARVRKPAEAERYKLERLAEAEKSQL 226
Cdd:cd03406 196 RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemhlAREKARADAEYYRALREAEANKLKL 261
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
72-298 |
5.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 72 LKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIR--EAKAKQEKVSAQYLSEIEMAKAQRDyelkkaAYDIEVN 149
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAED------AKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 150 TRRAQADLAYQLQVAKTKQQIEEQRVQVQVvERAQQVAVQEQ----EIARREKElearVRKPAEAERYKLERLAEAEKSQ 225
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEV-RKAEELRKAEDarkaEAARKAEE----ERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 226 LIMQAEAE----AESVRMRGEAEAF-------------AIGARARAEAEQMAK-----KAEAFQLYQEAAQLDMLLEK-- 281
Cdd:PTZ00121 1233 EEAKKDAEeakkAEEERNNEEIRKFeearmahfarrqaAIKAEEARKADELKKaeekkKADEAKKAEEKKKADEAKKKae 1312
|
250 260
....*....|....*....|....
gi 1622929039 282 -------LPQVAEEISGPLTSANK 298
Cdd:PTZ00121 1313 eakkadeAKKKAEEAKKKADAAKK 1336
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
23-79 |
8.23e-04 |
|
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: 38.50 E-value: 8.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622929039 23 ETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQ 79
Cdd:cd02106 54 RKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
160-264 |
1.12e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 40.97 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 160 QLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEiaRREKELEARVRKP-AEAERYKLERLA---EAEKSQliMQAEAEAE 235
Cdd:NF012221 1670 GKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGE--QNQANAEQDIDDAkADAEKRKDDALAkqnEAQQAE--SDANAAAN 1745
|
90 100
....*....|....*....|....*....
gi 1622929039 236 SVRMRGEAEAFAIGARArAEAEQMAKKAE 264
Cdd:NF012221 1746 DAQSRGEQDASAAENKA-NQAQADAKGAK 1773
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
115-327 |
1.14e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 115 AKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIE--------VNTRRAQADLAY-QLQVAKTKQQIEEqrvqvqvVERAQQ 185
Cdd:PRK10929 125 AQQEQDRAREISDSLSQLPQQQTEARRQLNEIErrlqtlgtPNTPLAQAQLTAlQAESAALKALVDE-------LELAQL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 186 VAVQEQEIARREKELearvrkpAEAERYKLERLAEAEKSQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEA 265
Cdd:PRK10929 198 SANNRQELARLRSEL-------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622929039 266 FQ-LYQEAAQLDMLLEKLPQVAEEIsgpLTSANKITLVSSGSGTMGAAKVTGEVL-DILTRLPE 327
Cdd:PRK10929 271 SQaLNQQAQRMDLIASQQRQAASQT---LQVRQALNTLREQSQWLGVSNALGEALrAQVARLPE 331
|
|
| SPFH_prohibitin |
cd03401 |
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
30-108 |
1.38e-03 |
|
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.
Pssm-ID: 259799 [Multi-domain] Cd Length: 195 Bit Score: 39.42 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 30 RAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS----------LGKAR----TAQVQK 95
Cdd:cd03401 102 KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAieakqvaeqeAERAKfeleKAEQEA 181
|
90
....*....|...
gi 1622929039 96 DARIGEAEAKRDA 108
Cdd:cd03401 182 ERKVIEAEGEAEA 194
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-274 |
2.73e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEA-----EAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDI----EVNTRRAQADL 157
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAarkaeEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVkkaeEAKKDAEEAKK 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 158 AYQLQVAKTKQQIEEQRVqvqvVERAQQVAVQEQEIARREKELearvrKPAEaERYKLERLAEAEKSQLIMQAEAEAESV 237
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARM----AHFARRQAAIKAEEARKADEL-----KKAE-EKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622929039 238 RMRGEAEAFAigARARAEAEQMAKKAEAFQLYQEAAQ 274
Cdd:PTZ00121 1315 KKADEAKKKA--EEAKKKADAAKKKAEEAKKAAEAAK 1349
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
187-270 |
2.93e-03 |
|
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: 38.62 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 187 AVQEQEIARREKElEARVRkpAEAERYKLERLAEAEKSQLIMQAEAEAESVRMRGEAEAfaigARARAEAEQMAKKAEAF 266
Cdd:cd03405 157 SVYERMRAERERI-AAEYR--AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDA----EAARIYAEAYGKDPEFY 229
|
....
gi 1622929039 267 QLYQ 270
Cdd:cd03405 230 SFYR 233
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
164-274 |
3.32e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 164 AKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAEryKLERLAEAEKSQLIMQAEAEAESVRMRGEA 243
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAE--EAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110
....*....|....*....|....*....|.
gi 1622929039 244 EAFAIGARARAEAEQMAKKAEAFQLYQEAAQ 274
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-288 |
4.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQylsEIEMAKAQRDYELKKAAYDIEVNTRRAQADlayQLQVAKT 166
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE---AKKKADEAKKAEEAKKADEAKKAEEAKKAD---EAKKAEE 1544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 167 KQQIEEQRvQVQVVERAQQVAVQEQeiARREKELEARVRKPAE----AERYKLERLAEAEKSQLIMQAEAEAESVRMRGE 242
Cdd:PTZ00121 1545 KKKADELK-KAEELKKAEEKKKAEE--AKKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622929039 243 AEAFAIGARARAEAEQMAKKAE-----AFQLYQEAAQLDMLLEKLPQVAEE 288
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAeekkkAEELKKAEEENKIKAAEEAKKAEE 1672
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
89-279 |
4.85e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 38.63 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 89 RTAQVQKDARIGEAEAKRDAGIREAKAKQEK-VSAQYLSEIEMAKAQRDYELKKA---AYDIEVNTRRAQADLAYQLQVA 164
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 165 KTKQQIEEQRVQV---QVVERAQ---QVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAESvr 238
Cdd:PRK09510 146 KAKAEAEAKRAAAaakKAAAEAKkkaEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA-- 223
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622929039 239 mRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLL 279
Cdd:PRK09510 224 -KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-220 |
5.77e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 112 EAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAYDIEVNTRRAQADLAYQLQVAK----------TKQQIEEQRVQVQVVE 181
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERE 640
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622929039 182 RAQQvaVQEQEIARREKELEARVRK---PAEAERYKLERLAE 220
Cdd:PRK04863 641 RELT--VERDELAARKQALDEEIERlsqPGGSEDPRLNALAE 680
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
87-274 |
5.97e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 38.65 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 164
Cdd:NF041483 432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 165 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAE 235
Cdd:NF041483 497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622929039 236 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 274
Cdd:NF041483 577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-264 |
6.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 87 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydiEVNTRRAQADLAYQLQVAKT 166
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929039 167 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARV---RKPAEAERYKLERLA-EAEKSQLIMQAeAEAESVRMRGE 242
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAAdEAEAAEEKAEA-AEKKKEEAKKK 1379
|
170 180
....*....|....*....|..
gi 1622929039 243 AEAFAIGARARAEAEQMAKKAE 264
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAE 1401
|
|
| |
