|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3-531 |
1.63e-86 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 274.83 E-value: 1.63e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 3 NLPGWLFTVIALVLTLFVIGLIFARLYRRASAEQAFVRTG-LGGQKVVMSGGAIVMPIFHETIPVNMNTLKLEVSRAaaE 81
Cdd:COG2268 2 ETLGILIIIGVIVVVLLLLLIILARFYRKVPPNEALVITGrGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERT--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 82 SLITRDRMRVDVAVAFFLRVKPSAEGISTAAQTLGqcTLTPEDLRSLVEDKFVDALRATAARMSMQDLQDARENFVQGVQ 161
Cdd:COG2268 80 GLITKDGIRVDVDAVFYVKVNSDPEDIANAAERFL--GRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 162 NTVAEDLSKNGLELESVSLTSFNQtarehfnPDNAFDAEGLTLLTQETERRRRERNEVEQDVEVAIREKNRDALSRRLEI 241
Cdd:COG2268 158 EVAGTDLAKNGLELESVAITDLED-------ENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 242 EQQEAFMtleqqqrvktRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVrtrqveaerevaireieqQQA 321
Cdd:COG2268 231 EREIETA----------RIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREV------------------QRQ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 322 TEIASQARAIAVAAKSEEQSQAEARAskalaeavqaqqdveTTRQTAEADRTKQVAliaaaqeaetkaveltvRAQAEKE 401
Cdd:COG2268 283 LEIAEREREIELQEKEAEREEAELEA---------------DVRKPAEAEKQAAEA-----------------EAEAEAE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 402 AAelqaaaiielaeatRQKGLAEAEAQRALNDAINVLSDEQtslrFRLALLDALPAVIEKSTEPMKSIDGIKIIQVDGLN 481
Cdd:COG2268 331 AI--------------RAKGLAEAEGKRALAEAWNKLGDAA----ILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGG 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1881516507 482 GGVTRGKTattdisggnlaeqavtaalayRTQAPLIDSLLKEVGLSGEGL 531
Cdd:COG2268 393 NGAGSAVA---------------------EALAPLLESLLEETGLDLPGL 421
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
402-523 |
5.27e-32 |
|
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: 119.35 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 402 AAELQAAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLALLDALPAVIEKSTEPMKSIDGIKIIQVDGLN 481
Cdd:pfam15975 1 EAEAEADAIKLRAEAKRKKALAEAEGIRALNEAENALSDEQIALQVKLALLEALPEIIAESVKPLEKIDGIKILQVDGLG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1881516507 482 GGVTrGKTATTDISGGNLAEQAVTAALAYRTQAPLIDSLLKE 523
Cdd:pfam15975 81 GGAA-GGGGGGGGGGGSLAEQAVDSALGYRAQAPLIDSLLKE 121
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
55-203 |
3.09e-30 |
|
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: 115.29 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 55 IVMPIFHETIPVNMNTLKLEVSRAAAeslITRDRMRVDVAVAFFLRVKPSAEGISTAA-QTLGQctlTPEDLRSLVEDKF 133
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEV---LTKDGIPVDVTAVAQVKVGSDPEEIAAAAeRFLGK---STEEIRELVKETL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 134 VDALRATAARMSMQDLQDARENFVQGVQNTVAEDLSKNGLELESVSLTSFNQTArEHFNPDNAFDAEGLT 203
Cdd:cd03399 75 EGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDN-GYLESLGRKQAAEVK 143
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
222-455 |
4.50e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 222 DVEVAIREKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVR 301
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 302 TRQVEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAA 381
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1881516507 382 AQEAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLALLDAL 455
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
36-184 |
4.03e-13 |
|
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: 67.73 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 36 QAFVRTGLGG-QKVVMSGGAIVMPIFHETIPVNMNTLKLEVSRaaaESLITRDRMRVDVAVAFFLRVKPsaegisTAAQT 114
Cdd:pfam01145 7 EVGVVTRFGKlSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSV---QTVLTKDGVPVNVDVTVIYRVNP------DDPPK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 115 LGQCTLTPEDLRSLVEDKFVDALRATAARMSMQDLQDARENFVQGVQNTVAEDLSKNGLELESVSLTSFN 184
Cdd:pfam01145 78 LVQNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDID 147
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-430 |
1.58e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 228 REKNRDALSRRLEIEQQEAfMTLEQQQRVKTRTAEQSASIAAIEAErRREAESARILAERKIEEAEIERQQIVRTRQVEA 307
Cdd:COG1196 308 EERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEE-LEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 308 EREVAIREIEQQQATEIASQARAIAVAAksEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAET 387
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALL--ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1881516507 388 KAVELtvRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRA 430
Cdd:COG1196 464 LLAEL--LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
26-192 |
4.23e-11 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 61.52 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 26 ARLYRRASAEQAFVRTGLGGQKVVMSGGAIVMPIFHETIPVNMNTLKLEVSraaAESLITRDRMRVDVAVAFFLRVkpsA 105
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVP---PQETITKDNVKVSVDAVVYYRV---L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 106 EGISTAAQTLGqctLTPEDLRSLVEdkfvDALRATAARMSMQDLQ-DARENFVQGVQNTVAEDLSKNGLELESVSLT--S 182
Cdd:smart00244 75 DPLRAVYRVLD---ADYAVIEQLAQ----TTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKdiR 147
|
170
....*....|
gi 1881516507 183 FNQTAREHFN 192
Cdd:smart00244 148 LPEEIKEAME 157
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
250-427 |
3.04e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 250 LEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIvRTRQVEAEREVAIreiEQQQATEIASQAR 329
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAAL---KQKQAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 330 AIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQV-ALIAAAQEAETKAveltvRAQAEKEAAELQAA 408
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAeAAAKAAAEAKKKA-----EAEAKKKAAAEAKK 217
|
170
....*....|....*....
gi 1881516507 409 AIIELAEATRQKGLAEAEA 427
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-464 |
3.91e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 240 EIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERrreaesARILAERKIEEAEIERQQIVRTR------QVEAEREVAI 313
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAEL------EELEAELAELEAELEELRLELEEleleleEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 314 REIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELT 393
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1881516507 394 VRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLALLDALPAVIEKSTE 464
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-404 |
1.51e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 221 QDVEVAIREKNRDAlsRRLEIEQ--------QEAFMTLEQQQRVKTRTAEQSASI-AAIEAERRREAESAR-------IL 284
Cdd:PTZ00121 1150 DAKRVEIARKAEDA--RKAEEARkaedakkaEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARkaedakkAE 1227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 285 AERKIEEAEIERQQIVRTRQVEAEREVAIRE------IEQQQATEIASQARAIAVAAKSEEQSQA-EARASKALAEAVQA 357
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEearmahFARRQAAIKAEEARKADELKKAEEKKKAdEAKKAEEKKKADEA 1307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1881516507 358 QQDVETTRQTAEADRTkqvaliaaAQEAETKAVELTVRAQAEKEAAE 404
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKK--------AEEAKKKADAAKKKAEEAKKAAE 1346
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
238-439 |
2.09e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 238 RLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIE 317
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 318 QQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQ 397
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1881516507 398 AEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDAINVLS 439
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLD 267
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
207-434 |
2.48e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 207 QETERRRRERNEVEQDVEVAIREKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAE 286
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 287 RKIEEAEIE--RQQIVRTRQVEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETT 364
Cdd:COG1196 423 LEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 365 RQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDA 434
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
10-309 |
2.51e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 55.23 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 10 TVIALVLTLFVIGLIFARLYRRASAEQAfVRTGLGG-QKVVMSGGAIVMPIFHETIPVNMNTLKLEVsraAAESLITRDR 88
Cdd:COG0330 3 LILLLILLVLVLVLLFSSVYIVPQGERG-VVLRFGKyVRTLEPGLHFKIPFIDRVRKVDVREQVLDV---PPQEVLTKDN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 89 MRVDVAVAFFLRVKPSAEgistAAQTLgqctltpEDLRSLVEDKFVDALRATAARMSMQD-LQDARENFVQGVQNTVAED 167
Cdd:COG0330 79 NIVDVDAVVQYRITDPAK----FLYNV-------ENAEEALRQLAESALREVIGKMTLDEvLSTGRDEINAEIREELQEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 168 LSKNGLELESVSLTSfnqtarehFNPDnafdaegltlltqeterrrrerneveQDVEVAIREKnrdalsrrleieqqeaf 247
Cdd:COG0330 148 LDPYGIEVVDVEIKD--------IDPP--------------------------EEVQDAMEDR----------------- 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1881516507 248 MTLEQQQRvktrtaeqsASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAER 309
Cdd:COG0330 177 MKAERERE---------AAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEA 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
231-429 |
1.13e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 231 NRDALSRRLEIEQQE----AFMTLEQQQRVKTRtAEQSASIAAIEAERRREAESARILAERKIEEA-----------EIE 295
Cdd:PTZ00121 1056 HEGKAEAKAHVGQDEglkpSYKDFDFDAKEDNR-ADEATEEAFGKAEEAKKTETGKAEEARKAEEAkkkaedarkaeEAR 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 296 RQQIVR----TRQVEAEREVAI-REIEQQQATEI---ASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQT 367
Cdd:PTZ00121 1135 KAEDARkaeeARKAEDAKRVEIaRKAEDARKAEEarkAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1881516507 368 AEADRTKQVALIAAAQEAET--KAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQR 429
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEakKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
252-465 |
2.96e-07 |
|
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: 52.54 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 252 QQQRVKTRTAEQS----ASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATEIASQ 327
Cdd:TIGR02794 56 QQQKKPAAKKEQErqkkLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 328 ARAIAVAAKSEE-QSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAELQ 406
Cdd:TIGR02794 136 AEAEAERKAKEEaAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEA 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1881516507 407 AAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLALLDALPAVIEKSTEP 465
Cdd:TIGR02794 216 EAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQ 274
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
227-430 |
4.54e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 227 IREKNRDALSRRLEIEQQEAfmtleQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVE 306
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKA-----EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 307 AEREVAIREIEQQQATEIASQAR-AIAVAAKSEEQSQAEARASKAlAEAVQAQQDVETTRQTAEADRTKQvaliaAAQEA 385
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKkADEAKKKAEEAKKAEEAKKKA-EEAKKADEAKKKAEEAKKADEAKK-----KAEEA 1495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1881516507 386 ETKAVELTVRAQAEKEAAELQAAAIIELAEATRQkglAEaEAQRA 430
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK---AE-EAKKA 1536
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
257-429 |
6.37e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.33 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 257 KTRTAEQSASIAAIEAERRREAESARILAERKIEEA--EIERQQIVRTRQVEAEREVAIREIEQQQATEIASQARAiava 334
Cdd:PTZ00491 644 RTRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEArgRLERQKMHDKAKAEEQRTKLLELQAESAAVESSGQSRA---- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 335 akseeqsQAEARASKALAEavqAQQDVETTRQTAEADRtkqvalIAAAQEAETKAVELTVRAQAEKEAAELqaaaiiela 414
Cdd:PTZ00491 720 -------EALAEAEARLIE---AEAEVEQAELRAKALR------IEAEAELEKLRKRQELELEYEQAQNEL--------- 774
|
170
....*....|....*
gi 1881516507 415 EATRQKGLAEAEAQR 429
Cdd:PTZ00491 775 EIAKAKELADIEATK 789
|
|
| SPFH_prohibitin |
cd03401 |
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
39-278 |
1.61e-06 |
|
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: 48.66 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 39 VRTGLGGQKVVMSGGA-IVMPIFHETIPVNMNTLKLEVSRAAAesliTRDRMRVDVAVAFFLRVKPsaEGISTAAQTLGq 117
Cdd:cd03401 13 FRRGKGVKDEVLGEGLhFKIPWIQVVIIYDVRTQPREITLTVL----SKDGQTVNIDLSVLYRPDP--EKLPELYQNLG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 118 ctltPEDLRSLVEDKFVDALRATAARMSMQDLQDARENFVQGVQNTVAEDLSKNGLELESVSLTSFNqtarehfnpdnaF 197
Cdd:cd03401 86 ----PDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNID------------F 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 198 DAEgltlltqeterrrrerneveqdVEVAIREKnrdalsrrlEIEQQEAfmtleQQQRVKTRTAEQSASIAAIEAERRRE 277
Cdd:cd03401 150 PDE----------------------YEKAIEAK---------QVAEQEA-----ERAKFELEKAEQEAERKVIEAEGEAE 193
|
.
gi 1881516507 278 A 278
Cdd:cd03401 194 A 194
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
260-404 |
2.15e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 50.25 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 260 TAEQSASIAAIEAERRREAESARILAErkieEAeierqqivRTRQVEAEREVA-----IREIEQQQA---TEIASQARAI 331
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAAD----EA--------KTAAAAAAREAAplkasLRKLERAKAradAELKRADKAL 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1881516507 332 AVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAE 404
Cdd:PRK12472 249 AAAKTDEAKARAEERQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLALE 321
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
267-450 |
4.77e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 267 IAAIEAERRReaesarilAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEAr 346
Cdd:COG4913 612 LAALEAELAE--------LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDA- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 347 ASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAE 426
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....
gi 1881516507 427 AQRALNDAINVLSDEQTSLRFRLA 450
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAE 786
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
238-432 |
4.80e-06 |
|
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: 48.69 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 238 RLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIE 317
Cdd:TIGR02794 69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 318 QQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAvQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQ 397
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEA-EAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
170 180 190
....*....|....*....|....*....|....*
gi 1881516507 398 AEKEAAELQAAAIIELAEATRQKGLAEAEAQRALN 432
Cdd:TIGR02794 228 KADEAELGDIFGLASGSNAEKQGGARGAAAGSEVD 262
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
227-405 |
9.83e-06 |
|
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: 48.58 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 227 IREKNRDALSR-------RLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAER-----KIEEAEI 294
Cdd:pfam17380 377 MRELERLQMERqqknervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERaremeRVRLEEQ 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 295 ERQ-QIVRTRQVEAEREVAIREIE-QQQATEIASQARAIAVAAKSEEQSQA---EARASKALAEAVQAQQDV---ETTRQ 366
Cdd:pfam17380 457 ERQqQVERLRQQEEERKRKKLELEkEKRDRKRAEEQRRKILEKELEERKQAmieEERKRKLLEKEMEERQKAiyeEERRR 536
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1881516507 367 TAEADRTKQVALIA--AAQEAETKAVELTVRAQAEKEAAEL 405
Cdd:pfam17380 537 EAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREM 577
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
228-452 |
1.49e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 228 REKNRDALSRRLEIEqqeafmtleqqqRVKTRTAEQSASIAAIEAER---RREAESARILAERKIEEAEIERQQIVRTRQ 304
Cdd:TIGR02168 666 AKTNSSILERRREIE------------ELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 305 VEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQ-SQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQ 383
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1881516507 384 EAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALND----------AINVLSDEQTSLRFRLALL 452
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleelieelesELEALLNERASLEEALALL 892
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-520 |
1.55e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 221 QDVEVAIREKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAE------RRREAESA-----RILAERKI 289
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleelrlEVSELEEEieelqKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 290 EEAEIERQ---QIVRTRQVEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQ 366
Cdd:TIGR02168 296 EISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 367 TAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAE--LQAAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTS 444
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 445 LRFRLALLDALPAVIEKSTEPMKS-----------IDGIKIIQ--VDGLNGGVTRGKTATTDISG--GNLA--------- 500
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAaerelaqlqarLDSLERLQenLEGFSEGVKALLKNQSGLSGilGVLSelisvdegy 535
|
330 340
....*....|....*....|
gi 1881516507 501 EQAVTAALAYRTQAPLIDSL 520
Cdd:TIGR02168 536 EAAIEAALGGRLQAVVVENL 555
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-430 |
1.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 271 EAERRREAESARILAERKIEEAeierqqivrtRQVEAEREVAIREIEQQQATEIASQARAIAVA-AKSEEQSQAEARASK 349
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEA----------KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 350 ALAEAVQAQQDV---ETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAE 426
Cdd:PTZ00121 1635 VEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
....
gi 1881516507 427 AQRA 430
Cdd:PTZ00121 1715 KKKA 1718
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
229-454 |
4.46e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 229 EKNRDALSRRLEIEQQEAFMTLE----QQQRVKTRTAEQSASIAAIEAER-RREAESARILAERKIEEAEIERQQIVRTR 303
Cdd:TIGR02169 211 ERYQALLKEKREYEGYELLKEKEalerQKEAIERQLASLEEELEKLTEEIsELEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 304 QVEAErevaIREIEqqqaTEIASQARAIavAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQ 383
Cdd:TIGR02169 291 RVKEK----IGELE----AEIASLERSI--AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1881516507 384 EAETKAVELTVRAQAEKEAAelqaaaiielaEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLALLDA 454
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEF-----------AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
224-385 |
5.66e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 224 EVAIREKNRDALSRRLEiEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILA--ERKIEEAEIERQQIVR 301
Cdd:COG4913 628 EAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAalEEQLEELEAELEELEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 302 TRQvEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQdVETTRQTAEADRTKQVALIAA 381
Cdd:COG4913 707 ELD-ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV-ERELRENLEERIDALRARLNR 784
|
....
gi 1881516507 382 AQEA 385
Cdd:COG4913 785 AEEE 788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-434 |
6.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 229 EKNRDALSRRLEIEQQ--EAFMTLEQQQRVKTRTAEQsasiaAIEAERRREAESARILAE-RKIEE---AEiERQQIVRT 302
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEE-----AKKADEAKKAEEKKKADElKKAEElkkAE-EKKKAEEA 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 303 RQVEAEREVAIREIEQQQATEiasQARAIAVAAKSEEQSQAEA-RASKALAEAVQAQQ--DVETTRQTAEADRTKQVALI 379
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMKAeEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEK 1646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1881516507 380 AAAQEAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDA 434
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
232-406 |
7.19e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 232 RDALSRRLEIEQQEAFMTLEQQQRVkTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREV 311
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLV-AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 312 AIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAEtkavE 391
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP----E 758
|
170
....*....|....*
gi 1881516507 392 LTVRAQAEKEAAELQ 406
Cdd:COG1196 759 PPDLEELERELERLE 773
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-373 |
8.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 223 VEVAIREKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAeRRREAESARI-LAERKIEEAEIERQQIVR 301
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA-QIRGNGGDRLeQLEREIERLERELEERER 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1881516507 302 TRqveAEREVAIREIEQQQATEIAS-QARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRT 373
Cdd:COG4913 360 RR---ARLEALLAALGLPLPASAEEfAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-406 |
1.89e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 251 EQQQRVKTRTAEQSASIAAIEAERRR------EAESARILAERKIEEAEIERQQIVRTRQVEAER----EVAIREIEQQQ 320
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleelEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 321 ATEIASQARAIAVAAKSEEQSQAEARASKALaEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTV-RAQAE 399
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDL-EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLeKEYLE 832
|
....*..
gi 1881516507 400 KEAAELQ 406
Cdd:TIGR02169 833 KEIQELQ 839
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
264-405 |
2.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 264 SASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQAtEIASQARAIAVAAKSEEQSQA 343
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1881516507 344 EARASKALAEAVQAQQDVETTRQTAEADRTKQVAL---IAAAQEAETKAVEL-TVRAQAEKEAAEL 405
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAEEAKEILLeKVEEEARHEAAVL 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
248-404 |
2.85e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 248 MTLEQQQRVKTRTAEQSASIAAIEaERRREAEsaRILAERKIEEA--EIERQQIVRTRqveAEREVAIREIEQQQATEIA 325
Cdd:PRK02224 416 ELREERDELREREAELEATLRTAR-ERVEEAE--ALLEAGKCPECgqPVEGSPHVETI---EEDRERVEELEAELEDLEE 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1881516507 326 SQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAE 404
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
227-450 |
3.08e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 227 IREKNRDALSR-RLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRReAESARILAERKIEEAEIERQQIVRTRQV 305
Cdd:PRK02224 181 VLSDQRGSLDQlKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQ-ARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 306 EAEREVAIREIEQQQAT---EIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALiaAA 382
Cdd:PRK02224 260 IEDLRETIAETEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV--AA 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 383 QEAETKAVELTVRA-QAEKEAAELQaaaiieLAEATRQKGLAEAEAQRA-LNDAINVLSDEQTSLRFRLA 450
Cdd:PRK02224 338 QAHNEEAESLREDAdDLEERAEELR------EEAAELESELEEAREAVEdRREEIEELEEEIEELRERFG 401
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
233-349 |
3.99e-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: 42.67 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 233 DALSRRLEIEQQEAFMTL--EQQQRVKTRTAEQSASIAAIEAERrrEAESARILAERKIEEAEIERQQivrtRQVEAERE 310
Cdd:cd03406 162 EAIRRNYEAMEAEKTKLLiaEQHQKVVEKEAETERKRAVIEAEK--DAEVAKIQMQQKIMEKEAEKKI----SEIEDEMH 235
|
90 100 110
....*....|....*....|....*....|....*....
gi 1881516507 311 VAireieqqqateiasQARAIAVAAKSEEQSQAEARASK 349
Cdd:cd03406 236 LA--------------REKARADAEYYRALREAEANKLK 260
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-446 |
5.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 221 QDVEVAIREKNRDALSRRLEIEQQEAFMTLEQQQRvKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIV 300
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 301 RTRQVEAER---EVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEAdrtKQVA 377
Cdd:PTZ00121 1436 AKKKAEEAKkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---KKKA 1512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 378 LIAAAQEAETKAVELTvRAQAEKEAAELQAAAIIELAEATRQ-KGLAEAEAQRALNDAINVLSDEQTSLR 446
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
221-389 |
7.47e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 221 QDVEVAIREKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIV 300
Cdd:PRK09510 94 QKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 301 RTRQVEAEREVAIREIEQQQATEIASQARAIAVAaksEEQSQAEARAsKALAEAVQAQQDVETTRQtAEADRTKQVALIA 380
Cdd:PRK09510 174 EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKK-KAAAEAKAAAAKAAAEAK-AAAEKAAAAKAAE 248
|
....*....
gi 1881516507 381 AAQEAETKA 389
Cdd:PRK09510 249 KAAAAKAAA 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-451 |
8.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 251 EQQQRVKTRTAEQSASIAAIEAERR------REAESARILAERKIEEAEIERQQIVRT-RQVEAEREVAIREIEQQQAtE 323
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKallkqlAALERRIAALARRIRALEQELAALEAElAELEKEIAELRAELEAQKE-E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 324 IASQARA---------IAVAAKSEEQSQAEARAS--KALAEAVQAQ--------QDVETTRQTAEADRTKQVALIAAAQE 384
Cdd:COG4942 106 LAELLRAlyrlgrqppLALLLSPEDFLDAVRRLQylKYLAPARREQaeelradlAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1881516507 385 AETKAVEL-----TVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLAL 451
Cdd:COG4942 186 ERAALEALkaerqKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-406 |
8.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 229 EKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAE 308
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 309 REVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAetk 388
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA--- 1779
|
170
....*....|....*...
gi 1881516507 389 AVELTVRAQAEKEAAELQ 406
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVD 1797
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
261-434 |
9.05e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 261 AEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATEIASQARAIAVAakseEQ 340
Cdd:NF041483 174 AEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAA----ES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 341 SQAEARASKALAEAVQAQQDVETTRQTAEADRTKqvaLIAAAQEAETKAVElTVRAQAEKEAAELQAAAIIELAEATRQK 420
Cdd:NF041483 250 DQARRQAAELSRAAEQRMQEAEEALREARAEAEK---VVAEAKEAAAKQLA-SAESANEQRTRTAKEEIARLVGEATKEA 325
|
170
....*....|....
gi 1881516507 421 GLAEAEAQRALNDA 434
Cdd:NF041483 326 EALKAEAEQALADA 339
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
228-430 |
9.90e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 228 REKNRDALSRRLEIEQQEafmtLEQQQRVKTRTAEQSASIAAIEAeRRREAESARILAERKIEEAEIERQQIVRTRQVEA 307
Cdd:PRK07735 19 KEEARKRLVAKHGAEISK----LEEENREKEKALPKNDDMTIEEA-KRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 308 EREVAirEIEQQQATEIASQARAIAVAAKSEEQSQAEARAS-KALAEAVQ-AQQDVETTRQTAEADRTKQVALIAAAQEA 385
Cdd:PRK07735 94 KAKAA--AAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAaAAKAKAAAlAKQKREGTEEVTEEEEETDKEKAKAKAAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1881516507 386 ETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRA 430
Cdd:PRK07735 172 AAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAA 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
273-464 |
1.24e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 273 ERRREAEsarilaeRKIEEAE--IERQQIVRT---RQV---EAEREVAIR------EIEQQQATEIASQARAI--AVAAK 336
Cdd:COG1196 172 ERKEEAE-------RKLEATEenLERLEDILGeleRQLeplERQAEKAERyrelkeELKELEAELLLLKLRELeaELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 337 SEEQSQAEARASKALAEAVQAQQDVETTRQTAEADR----TKQVALIAAAQEAETKAVELTVRAQAEKEAAELQAAAIIE 412
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELEleleEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1881516507 413 LAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRFRLALLDALPAVIEKSTE 464
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
290-455 |
1.25e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 290 EEAEIERQQIVRTRQVEAEREVaIREIEQQQATEIASQARAIAVAAKSEEQSQAEA---RASKALAEAVQAQQDVETTRQ 366
Cdd:pfam07111 63 QQAELISRQLQELRRLEEEVRL-LRETSLQQKMRLEAQAMELDALAVAEKAGQAEAeglRAALAGAEMVRKNLEEGSQRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 367 TAEADRTKQVALIAAAQEAETKAVELTVRAQA-EKEAAELQaaaiielaeaTRQKGLAE--AEAQRALNDAINVLSDEQT 443
Cdd:pfam07111 142 LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGlEKSLNSLE----------TKRAGEAKqlAEAQKEAELLRKQLSKTQE 211
|
170
....*....|..
gi 1881516507 444 SLRFRLALLDAL 455
Cdd:pfam07111 212 ELEAQVTLVESL 223
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
238-309 |
1.26e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 41.78 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1881516507 238 RLEIEQQE----AFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAER 309
Cdd:PLN03086 11 KLEREQRErkqrAKLKLERERKAKEEAAKQREAIEAAQRSRRLDAIEAQIKADQQMQESLQAGRGIVFSRIFEAVS 86
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
234-340 |
1.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 234 ALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESArilAERKIEEAEIERQQIVRT-RQVEAEREVA 312
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE---AQQAIKEAKKEADEIIKElRQLQKGGYAS 603
|
90 100 110
....*....|....*....|....*....|.
gi 1881516507 313 IRE---IEQQQATEIASQARAIAVAAKSEEQ 340
Cdd:PRK00409 604 VKAhelIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
230-404 |
1.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 230 KNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAE--RKIEEAEIERQQIVRTRQVEA 307
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADEAKK 1490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 308 EREVAIREIEQ----QQATEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQ 383
Cdd:PTZ00121 1491 KAEEAKKKADEakkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
170 180
....*....|....*....|.
gi 1881516507 384 EAETKAVELTVRAQAEKEAAE 404
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEE 1591
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-446 |
1.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 244 QEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATE 323
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 324 IASQARAIAVAAKSEEQSQAEARAS--KALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEA--ETKAVELTVRAQAE 399
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEAA 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1881516507 400 KEAAELQAAAIIELAEATRQKGlaeaeAQRALNDAINVLSDEQTSLR 446
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEA-----ALRDLRRELRELEAEIASLE 432
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
234-395 |
1.69e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 234 ALSRRLEIEQQEafMTLEQQQRVKTRTAEQSASI-AAIEAERRREAESARILAERKIEE----AEIERQQIV-------R 301
Cdd:pfam15709 343 AEMRRLEVERKR--REQEEQRRLQQEQLERAEKMrEELELEQQRRFEEIRLRKQRLEEErqrqEEEERKQRLqlqaaqeR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 302 TRQVEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEARasKALAEAV---------QAQQDVETTRQTAEADR 372
Cdd:pfam15709 421 ARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ--KRLMEMAeeerleyqrQKQEAEEKARLEAEERR 498
|
170 180
....*....|....*....|...
gi 1881516507 373 TKQVALIAAAQEAETKAVELTVR 395
Cdd:pfam15709 499 QKEEEAARLALEEAMKQAQEQAR 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-426 |
2.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 229 EKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILAE---RKIEEAEieRQQIVRTRQV 305
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakKKAEEAK--KAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 306 EAEREVAIREIEQQQATEIAS---QARAIAVAAKSEEQSQAEARASKA---------LAEAVQAQQDVETTRQTAE---- 369
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAeedkkkadeLKKAAAAKKKADEAKKKAEekkk 1432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1881516507 370 ADRTKQVA--------LIAAAQEAEtKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAE 426
Cdd:PTZ00121 1433 ADEAKKKAeeakkadeAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAK 1496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-420 |
2.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 229 EKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASiaaiEAERRREAESARILAER-KIEEAEIERQQIVRTRQVEA 307
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEEnKIKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 308 EREvaiREIEQQQATEiasqaraiAVAAKSEEQSQAEARASKALAEAVQAQQdvetTRQTAEADRTKQVALIAAAQEAET 387
Cdd:PTZ00121 1680 AKK---AEEDEKKAAE--------ALKKEAEEAKKAEELKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKK 1744
|
170 180 190
....*....|....*....|....*....|...
gi 1881516507 388 KAVELTVRAQAEKEAAELQAAAIIELAEATRQK 420
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
224-450 |
4.18e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 224 EVAIREKNRDALSRRLEIEQQEAFMTLEQQQRVKTRTAEQSASIAAIEAERRREAESARILA---ERKIEEAEIERQQIV 300
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkelTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 301 RTRQ----VEAEREVAIREIEQQQatEIASQARAIAVAAKSEEQSQAEARASKALAEAVQAQQDVETTRQ---------T 367
Cdd:TIGR02168 772 EAEEelaeAEAEIEELEAQIEQLK--EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRledleeqieE 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 368 AEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAELQAAAIIELAEATRQKGLAEAEAQRALNDAINVLSDEQTSLRF 447
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
...
gi 1881516507 448 RLA 450
Cdd:TIGR02168 930 RLE 932
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
259-442 |
5.04e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 39.81 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 259 RTAEQSASIAAIEAERRR-----EAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATEIASQARAIAV 333
Cdd:NF041483 520 RQAEETLERTRAEAERLRaeaeeQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADAR 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 334 AAKSEEQSQAEARASKALAEAV--------QAQQDVETTRQTAEADrtkqvaliAAAQEAETKAVELTVRAQAEKEAAEL 405
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAAerirtlqaQAEQEAERLRTEAAAD--------ASAARAEGENVAVRLRSEAAAEAERL 671
|
170 180 190
....*....|....*....|....*....|....*..
gi 1881516507 406 QAAAIIELAeatRQKGLAEAEAQRALNDAINVLSDEQ 442
Cdd:NF041483 672 KSEAQESAD---RVRAEAAAAAERVGTEAAEALAAAQ 705
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
253-403 |
5.59e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 39.55 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 253 QQRVKTRTAEQSASIAAIEAERRREAESARILA-ERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATEIASQARAI 331
Cdd:PRK05035 459 QARLEREKAAREARHKKAAEARAAKDKDAVAAAlARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQ 538
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1881516507 332 AVAAKSEEQSQAEARASKALAEAvQAQQDVETTRQTAEADRTKQVAL-IA------AAQEAETKAVELTVRAQAEKEAA 403
Cdd:PRK05035 539 AAAAADPKKAAVAAAIARAKAKK-AAQQAANAEAEEEVDPKKAAVAAaIArakakkAAQQAASAEPEEQVAEVDPKKAA 616
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
344-434 |
6.29e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 38.82 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 344 EARASKALAeAVQAQQDVEttrQTAEADRTKQValIAAAQEAETKAVELTVRAqAEKEAaELQAAAIIELAEATRQKGLA 423
Cdd:cd03406 172 EAEKTKLLI-AEQHQKVVE---KEAETERKRAV--IEAEKDAEVAKIQMQQKI-MEKEA-EKKISEIEDEMHLAREKARA 243
|
90
....*....|.
gi 1881516507 424 EAEAQRALNDA 434
Cdd:cd03406 244 DAEYYRALREA 254
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
277-448 |
7.62e-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: 39.43 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 277 EAESARILAERKIEEAEIERQQivrtRQVEAEREVAIREIEQQQATEIASQARAIAVAAKS---EEQSQAEARASKALAE 353
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDIDD----AKADAEKRKDDALAKQNEAQQAESDANAAANDAQSrgeQDASAAENKANQAQAD 1768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 354 AVQAQQ--DVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAElqaaaiielaeatrqkGLAEAEaQRAL 431
Cdd:NF012221 1769 AKGAKQdeSDKPNRQGAAGSGLSGKAYSVEGVAEPGSHINPDSPAAADGRFSE----------------GLTEQE-QEAL 1831
|
170
....*....|....*..
gi 1881516507 432 NDAINVLSDEQTSLRFR 448
Cdd:NF012221 1832 EGATNAVNRLQINAGSR 1848
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
267-404 |
9.15e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 38.73 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881516507 267 IAAIEAERRREAESARILAERKIEEAEIERQQIVRTRQVEAEREVAIREIEQQQATEIASQARAIAVAAKSEEQSQAEAR 346
Cdd:PRK12678 52 IAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1881516507 347 ASKALAEAVQAQQDVETTRQTAEADRTKQVALIAAAQEAETKAVELTVRAQAEKEAAE 404
Cdd:PRK12678 132 ERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGE 189
|
|
| |
