|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
5-424 |
2.75e-95 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 292.93 E-value: 2.75e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 5 FVTCGPNEALVVSGCcYMKPLLVPGGRAFVWPVGQQVQRISLNTMTLQVE-SPCVYTSQGVPISVTGIAQVKVQGqNEDM 83
Cdd:COG2268 28 YRKVPPNEALVITGR-GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPED 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 84 LLTACEQFLGKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEgd 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDEN-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 164 skGYLRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTD-----IAKAQRDFELKKAAYDVEVQTKK 238
Cdd:COG2268 184 --NYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETAR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 239 AEAEMAYELQAAKTKQRIkeeQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEA 318
Cdd:COG2268 262 AEAEAAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 319 EAESIRirgeaeafaiaakakaeaeqmaMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKKITMVSSGTGDIGAA 398
Cdd:COG2268 339 EAEGKR----------------------ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAG 396
|
410 420
....*....|....*....|....*.
gi 24653894 399 KLtgeVLSIVNKVPELVKNITGVDIA 424
Cdd:COG2268 397 SA---VAEALAPLLESLLEETGLDLP 419
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
33-182 |
1.45e-66 |
|
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: 208.90 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 33 FVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEdMLLTACEQFLGKSEAEINHIALVTLEGHQR 112
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPE-EIAAAAERFLGKSTEEIRELVKETLEGHLR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 113 AIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEgdskGYLRSLGMARTAEVKRD 182
Cdd:cd03399 80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDN----GYLESLGRKQAAEVKKD 145
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
6-194 |
2.06e-18 |
|
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: 82.37 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 6 VTCGPNEALVVSGCCYMKPLLVPGGRaFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEDMLL 85
Cdd:pfam01145 1 IIVPPGEVGVVTRFGKLSRVLEPGLH-FIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 86 TACeqflgKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRdeegDSK 165
Cdd:pfam01145 80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDID----PPP 150
|
170 180
....*....|....*....|....*....
gi 24653894 166 GYLRSLGMARTAEVKRDARIgeAEARAEA 194
Cdd:pfam01145 151 EIAEAIEAKQTAEQEAEAEI--ARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
87-273 |
9.28e-17 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 77.32 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 87 ACEQFLGKSEAEINHIALVTLEghqRAIMGSMTVEEIYKDRKKfskqVFEVASSDLANMGITVVSYTIKDLRDEEGdskg 166
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVV---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 167 YLRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEeqrmaarflndTDIAKAQRDFELKKAAYDVEVQTKKAEAeMAYE 246
Cdd:smart00244 70 YYRVLDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIK 137
|
170 180
....*....|....*....|....*..
gi 24653894 247 LQAAKTKQRikeeQMQVKVIERTQEIA 273
Cdd:smart00244 138 VEDVEIKDI----RLPEEIKEAMEAQQ 160
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-362 |
3.18e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 173 MARTAEVKRDARigEAEARAEAHIK----EAIAEEQRMAARFLNDTDIAKAQRDfELKKA--AYDVEVQTKKAEAEMAYE 246
Cdd:PTZ00121 1462 AKKKAEEAKKAD--EAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAeeAKKADEAKKAEEAKKADE 1538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 247 LQAAKTKQRiKEEQMQVKVIERTQEIAVQEQEimRRERELEATIRRPAE----AEKFRMEKLAEANKQRVVMEAE----A 318
Cdd:PTZ00121 1539 AKKAEEKKK-ADELKKAEELKKAEEKKKAEEA--KKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEeakkA 1615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24653894 319 EAESIR---IRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVE 362
Cdd:PTZ00121 1616 EEAKIKaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
5-424 |
2.75e-95 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 292.93 E-value: 2.75e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 5 FVTCGPNEALVVSGCcYMKPLLVPGGRAFVWPVGQQVQRISLNTMTLQVE-SPCVYTSQGVPISVTGIAQVKVQGqNEDM 83
Cdd:COG2268 28 YRKVPPNEALVITGR-GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPED 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 84 LLTACEQFLGKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEgd 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDEN-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 164 skGYLRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTD-----IAKAQRDFELKKAAYDVEVQTKK 238
Cdd:COG2268 184 --NYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETAR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 239 AEAEMAYELQAAKTKQRIkeeQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEA 318
Cdd:COG2268 262 AEAEAAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 319 EAESIRirgeaeafaiaakakaeaeqmaMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKKITMVSSGTGDIGAA 398
Cdd:COG2268 339 EAEGKR----------------------ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAG 396
|
410 420
....*....|....*....|....*.
gi 24653894 399 KLtgeVLSIVNKVPELVKNITGVDIA 424
Cdd:COG2268 397 SA---VAEALAPLLESLLEETGLDLP 419
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
33-182 |
1.45e-66 |
|
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: 208.90 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 33 FVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEdMLLTACEQFLGKSEAEINHIALVTLEGHQR 112
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPE-EIAAAAERFLGKSTEEIRELVKETLEGHLR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 113 AIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEgdskGYLRSLGMARTAEVKRD 182
Cdd:cd03399 80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDN----GYLESLGRKQAAEVKKD 145
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
6-194 |
2.06e-18 |
|
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: 82.37 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 6 VTCGPNEALVVSGCCYMKPLLVPGGRaFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEDMLL 85
Cdd:pfam01145 1 IIVPPGEVGVVTRFGKLSRVLEPGLH-FIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 86 TACeqflgKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRdeegDSK 165
Cdd:pfam01145 80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDID----PPP 150
|
170 180
....*....|....*....|....*....
gi 24653894 166 GYLRSLGMARTAEVKRDARIgeAEARAEA 194
Cdd:pfam01145 151 EIAEAIEAKQTAEQEAEAEI--ARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
87-273 |
9.28e-17 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 77.32 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 87 ACEQFLGKSEAEINHIALVTLEghqRAIMGSMTVEEIYKDRKKfskqVFEVASSDLANMGITVVSYTIKDLRDEEGdskg 166
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVV---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 167 YLRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEeqrmaarflndTDIAKAQRDFELKKAAYDVEVQTKKAEAeMAYE 246
Cdd:smart00244 70 YYRVLDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIK 137
|
170 180
....*....|....*....|....*..
gi 24653894 247 LQAAKTKQRikeeQMQVKVIERTQEIA 273
Cdd:smart00244 138 VEDVEIKDI----RLPEEIKEAMEAQQ 160
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
30-241 |
6.72e-12 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 65.63 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 30 GRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVqgqnedmllTACEQFLGKSEAEINHIALVTlEG 109
Cdd:COG0330 45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRI---------TDPAKFLYNVENAEEALRQLA-ES 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 110 HQRAIMGSMTVEEIY-KDRKKFSKQVFEVASSDLANMGITVVSYTIKDLR-DEEgdskgYLRSLGMARTAEVKRDARIGE 187
Cdd:COG0330 115 ALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDpPEE-----VQDAMEDRMKAEREREAAILE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24653894 188 AEARAEAHIKEAIAEEQRMAARflndtdiAKAQRDFELKKAAYDVEVQTKKAEA 241
Cdd:COG0330 190 AEGYREAAIIRAEGEAQRAIIE-------AEAYREAQILRAEGEAEAFRIVAEA 236
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
49-159 |
6.00e-10 |
|
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259797 [Multi-domain] Cd Length: 110 Bit Score: 56.22 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 49 MTLQVESPCVYTSQGVPISVTGIAQVKVQGQNedmLLTACEQFLGKSEAEiNHIaLVTLEGHQRAIMGSMTVEEIYKDRK 128
Cdd:cd02106 3 QFDDVRVEPVGTADGVPVAVDLVVQFRITDYN---ALPAFYLVDFVKDIK-ADI-RRKIADVLRAAIGRMTLDQIISGRD 77
|
90 100 110
....*....|....*....|....*....|.
gi 24653894 129 KFSKQVFEVASSDLANMGITVVSYTIKDLRD 159
Cdd:cd02106 78 EIAKAVKEDLEEDLENFGVVISDVDITSIEP 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-321 |
5.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 174 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYELQAAKTK 253
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653894 254 QRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAE 321
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-359 |
6.20e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 174 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDtDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYELQAAKTK 253
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 254 QRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAESIRIRGEAEAFA 333
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180
....*....|....*....|....*.
gi 24653894 334 IAAKAKAEAEQMAMKAEAYREYREAA 359
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEEL 426
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
280-327 |
9.86e-05 |
|
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: 43.63 E-value: 9.86e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24653894 280 MRRERELEATIRRpAEAEKFRMEKLAEANKQRVVMEAEAEAESIRIRG 327
Cdd:cd03405 162 MRAERERIAAEYR-AEGEEEAEKIRAEADRERTVILAEAYREAEEIRG 208
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-377 |
1.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 175 RTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYE---LQAAK 251
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEelaEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 252 TKQRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKfrmEKLAEANKQRVVMEAEAEAESIRIRGEAEA 331
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---EEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24653894 332 FAIAAKAKAEAEQMAMKAEAYREYREAAMVEMLLDTLPKVAAEVAA 377
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-362 |
3.18e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 173 MARTAEVKRDARigEAEARAEAHIK----EAIAEEQRMAARFLNDTDIAKAQRDfELKKA--AYDVEVQTKKAEAEMAYE 246
Cdd:PTZ00121 1462 AKKKAEEAKKAD--EAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAeeAKKADEAKKAEEAKKADE 1538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 247 LQAAKTKQRiKEEQMQVKVIERTQEIAVQEQEimRRERELEATIRRPAE----AEKFRMEKLAEANKQRVVMEAE----A 318
Cdd:PTZ00121 1539 AKKAEEKKK-ADELKKAEELKKAEEKKKAEEA--KKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEeakkA 1615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24653894 319 EAESIR---IRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVE 362
Cdd:PTZ00121 1616 EEAKIKaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
|
| SPFH_alloslipin |
cd13437 |
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
27-212 |
7.72e-04 |
|
Alloslipin, 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 some eukaryotes and viruses. 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. This diverse subgroup of the SLPs remains largely uncharacterized.
Pssm-ID: 259815 [Multi-domain] Cd Length: 222 Bit Score: 40.68 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 27 VPGGRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGI----------AQVKVQgqNEDMLLTaceqflgkse 96
Cdd:cd13437 27 VDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVvyyriidpykAIYRID--NVKQALI---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 97 aeinHIALVTLeghqRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRdeegDSKGYLRSLGMART 176
Cdd:cd13437 95 ----ERTQTTL----RSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIV----LSKDLQQSLSSAAK 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 24653894 177 AEvkrdaRIGEAE---ARAEAhikEAiAEEQRMAARFLN 212
Cdd:cd13437 163 AK-----RIGESKiisAKADV---ES-AKLMREAADILD 192
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
234-311 |
9.12e-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: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 234 VQTKKAEAEMAYELQAAktkqrikEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRP---AEAEKFRMEKLAEANKQ 310
Cdd:cd03406 187 VVEKEAETERKRAVIEA-------EKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREkarADAEYYRALREAEANKL 259
|
.
gi 24653894 311 R 311
Cdd:cd03406 260 K 260
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
174-376 |
1.01e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 174 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARflndTDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYELQAAKTK 253
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 254 QRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANK--------QRVVMEAEAEAESIRI 325
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeeeealLELLAELLEEAALLEA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24653894 326 RGEAEAFAIAAKAKAEAEQMAMKAEaYREYREAAMVEMLLDTLPKVAAEVA 376
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEAD-YEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
174-325 |
1.14e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 174 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKaaydVEVQTKKAEAEMAYELQAAKTK 253
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK----LEKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653894 254 QRikeeqmqvKVIERTQEIAVQEQEIMRRERELEATIrrpAEAEKfRMEKLA-----EAnKQRVV--MEAEAEAESIRI 325
Cdd:PRK12704 109 EE--------ELEKKEKELEQKQQELEKKEEELEELI---EEQLQ-ELERISgltaeEA-KEILLekVEEEARHEAAVL 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
175-384 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 175 RTAEVKRDARigEAEARAEAHIKEA-----IAEEQRMAArflndtDIAKAqrdfELKKAAYDVEVQTKKAEAEmayELQA 249
Cdd:PTZ00121 1309 KKAEEAKKAD--EAKKKAEEAKKKAdaakkKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 250 AKTKQRIKEEQMQVKVIERTQEIAVQEQEIMRRERELeatiRRPAEAEKFRMEKLAEANKQRVVMEAEAEAESIRIRGEA 329
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL----KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24653894 330 EAFAIAAKAKAEAEQMAMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKK 384
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
|
| SPFH_stomatin |
cd03403 |
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
30-213 |
1.55e-03 |
|
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.
Pssm-ID: 259801 [Multi-domain] Cd Length: 202 Bit Score: 39.46 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 30 GRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQgqNEDMLLTACEQFlgksEAEINHIALVTLeg 109
Cdd:cd03403 8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQ--NATIAVTNVENA----DRSTRLLAQTTL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 110 hqRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRdeegdskgylrslgmaRTAEVKRdARIGEAE 189
Cdd:cd03403 80 --RNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVR----------------LPVQLQR-AMAAEAE 140
|
170 180
....*....|....*....|....
gi 24653894 190 ARAEAHIKEAIAEEQRMAARFLND 213
Cdd:cd03403 141 AAREARAKVIAAEGEQNASRALKE 164
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-324 |
2.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 178 EVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAaYDVEVQTKKAEAEMAYElQAAKTKQRIK 257
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL-YEEEKKMKAEEAKKAEE-AKIKAEELKK 1627
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653894 258 EEQMQVKV--IERTQEIAVQEQEIMRRERELE----ATIRRPAEAEKFRMEKL--AEANKQRVVMEAEAEAESIR 324
Cdd:PTZ00121 1628 AEEEKKKVeqLKKKEAEEKKKAEELKKAEEENkikaAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAK 1702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
158-375 |
6.54e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 158 RDEEGDSKGYLRSLGMARTAEVKRDARI-----GEAEARAEAHIKEaiaEEQRMAARFLNDTDIAKAQRDFELKKAAYDV 232
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKA---EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 233 EVQTKKAEAEMAYELQAAKTKQRIKEEQMQVKVIERTQEIAVQEQEIMRRERElEA----TIRRPAEAEKFRMEKLAEAN 308
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAkkaeELKKKEAEEKKKAEELKKAE 1725
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653894 309 KQRVVMEAEAEAESirirgeaeafaiaakakaeaEQMAMKAEAYR-EYREAAMVEMLLDTLPKVAAEV 375
Cdd:PTZ00121 1726 EENKIKAEEAKKEA--------------------EEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-384 |
7.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 169 RSLGMARTAEVKR---DARIGEAEARAEA--HIKEAI--AEEQRMAARFLNDTDIAKAQR----DFELKKAAYDVEVQTK 237
Cdd:PTZ00121 1200 RKAEAARKAEEERkaeEARKAEDAKKAEAvkKAEEAKkdAEEAKKAEEERNNEEIRKFEEarmaHFARRQAAIKAEEARK 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 238 KAEAEMAYELQAAKtKQRIKEEQMQVKVIERTQEIAVQEQEIMRREREleatIRRPAEAEKfrmEKLAEANKQRVVMEAE 317
Cdd:PTZ00121 1280 ADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE----AKKKADAAK---KKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653894 318 AEAESIRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAmvemllDTLPKVAAEVAAPLSQAKK 384
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA------DEAKKKAEEDKKKADELKK 1412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
175-358 |
8.68e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 175 RTAEVKRDAR--IGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDfELKKAAydvEVQTKKAEAEMAYELQAAKt 252
Cdd:PTZ00121 1451 KKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAA---EAKKKADEAKKAEEAKKAD- 1525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 253 KQRIKEEQMQVKVIERTQEiaVQEQEIMRRERELeatiRRPAEAEKFRMEKLAEANKQRVVMEAE--AEAESIRIrgeae 330
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEE--KKKADELKKAEEL----KKAEEKKKAEEAKKAEEDKNMALRKAEeaKKAEEARI----- 1594
|
170 180
....*....|....*....|....*...
gi 24653894 331 afaiAAKAKAEAEQMAMKAEAYREYREA 358
Cdd:PTZ00121 1595 ----EEVMKLYEEEKKMKAEEAKKAEEA 1618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
177-362 |
8.98e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 177 AEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDfELKKAAYDV----EVQTKKAEAEMAYELQaAKT 252
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKkkadEAKKKAEEAKKADEAK-KKA 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653894 253 KQRIKEEQMQVKVIE-RTQEIAVQEQEIMRREREL---------EATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAES 322
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAkkkaeeakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24653894 323 IRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVE 362
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
|
| |
