|
Name |
Accession |
Description |
Interval |
E-value |
| Myb_DNA-bind_7 |
pfam15963 |
Myb DNA-binding like; |
251-337 |
1.08e-29 |
|
Myb DNA-binding like;
Pssm-ID: 464956 [Multi-domain] Cd Length: 85 Bit Score: 112.63 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 251 SFRKRGfgKSSFWSEKETDLFYEVLQCTGQDFGLMSHYLPKRTRPELKAKYNREEKINWARVLNAISHPVRLDGNLEVRI 330
Cdd:pfam15963 1 SFRKRK--KTKRWSKEETELFYKALSMFGTDFSLIAQLFPGRTRRQIKLKFKREERKNPELVDKALKNRKPFDLEEFKRL 78
|
....*..
gi 17505318 331 SKLMTEM 337
Cdd:pfam15963 79 LEKEKEE 85
|
|
| BDP1 |
COG5118 |
Transcription initiation factor TFIIIB, Bdp1 subunit [Transcription]; |
43-375 |
1.47e-12 |
|
Transcription initiation factor TFIIIB, Bdp1 subunit [Transcription];
Pssm-ID: 227448 [Multi-domain] Cd Length: 507 Bit Score: 70.90 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 43 ILENVetMTNQVSLTVASESMKSLHVDTSKNHHVHftdDVIDNEQNRIQETPDIVMISPTSQQNAQFASPNPPARLtprS 122
Cdd:COG5118 172 SPPTA--MTDSLDRNFSSETSTSREADENENYVIS---KVKDIPKKVRDGESAKYFIDEENFTMAELCKPNFPIQI---S 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 123 RNVSmcedEAILQPKQPRDKKRFSG--REELDTKTWKMSDLTRWNPKNEMTRFKRERRsstsssVITKSEIGDLDAPPAP 200
Cdd:COG5118 244 ENFE----KSKMAKKAKLEKRRHVKflEGSNTHEMDQLLKHFLDNSNFRQDRRSRKKK------ASASRDISDQNAEEIL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 201 RInapqvkigADGRLVIDETSLVV--HSAQINHESVWETVEEGRMGAKITSMSFRKRGfgKSSFWSEKETDLFYEVLQCT 278
Cdd:COG5118 314 MI--------KNGHIVVDEANMYVdrHKNASIEVEEMEVVEENPFARIVTSSTFGKKK--GALRWSKKEIEKFYKALSIW 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 279 GQDFGLMSHYLPKRTRPELKAKYNREEKINWARVLNA--ISHPVRLDGNLEVRISKLMTEMEEEAQEKKAKGEYEKAEEK 356
Cdd:COG5118 384 GTDFSLISSLFPNRERKQIKAKFIKEEKVNPERINEAlnEKKPFDQVEYNKLRSYLLEKLIELQNEHKHHMKEIEEAKNT 463
|
330
....*....|....*....
gi 17505318 357 RIREQNRLQKATERNQAKE 375
Cdd:COG5118 464 AKEEDQTAQRLNDANLNKK 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-504 |
1.78e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 339 EEAQEKKAKGEYEKAEEKRIREQNRlQKATERNQAKELVKQAKELERDARNA---AKLNMKADKEARAQEKSETRQLEKT 415
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAkkkAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 416 ALKE--ARLMATEAKRIAMEARaiikesRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRRTAHFNKNDKPAA 493
Cdd:PTZ00121 1363 EEKAeaAEKKKEEAKKKADAAK------KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
170
....*....|.
gi 17505318 494 PKSTEEATTSE 504
Cdd:PTZ00121 1437 KKKAEEAKKAD 1447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
326-483 |
9.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 326 LEVRISKLMTEMEEE-AQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNAAKLNMKADKEARAQ 404
Cdd:COG1196 272 LRLELEELELELEEAqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 405 EKSETRQLEKTAlkEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQ-ESQREDRRTA 483
Cdd:COG1196 352 ELEEAEAELAEA--EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERlEEELEELEEA 429
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
339-450 |
2.58e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.15 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 339 EEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQA----KELERDARNAAKLNMKADKEARAQEKSET----- 409
Cdd:TIGR02794 66 EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAeqaaKQAEEKQKQAEEAKAKQAAEAKAKAEAEAerkak 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17505318 410 ----RQLEKTALKEArlmATEAKRIAMEARAIIKESRKLEKSKKA 450
Cdd:TIGR02794 146 eeaaKQAEEEAKAKA---AAEAKKKAEEAKKKAEAEAKAKAEAEA 187
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
332-430 |
5.61e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 332 KLMTEMEEEAQEKKAKGEYEKAEEKRIREQNRLQ----KATERNQAKELVKQAKELERDARNAAKLNMKAdKEARAQEks 407
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELeqklEDQERSYEEHLRQLKEKMEEERENLLKEQERA-LESKLKE-- 267
|
90 100
....*....|....*....|...
gi 17505318 408 ETRQLEKTALKEARLMATEAKRI 430
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSL 290
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
316-500 |
8.56e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 316 ISHPVRLDGNLEVRISKLM-----TEMEEEAQEKKAKGEYEKAEEKRIREQNRLQK-----ATERNQAKELVKQAKELER 385
Cdd:pfam02463 132 PEAYNFLVQGGKIEIIAMMkperrLEIEEEAAGSRLKRKKKEALKKLIEETENLAEliidlEELKLQELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 386 DARNAAKL-----NMKADKEARAQEKSETRQLEKTALKEARLMATEAKRIAmEARAIIKESRKLEKSKKADSVQ---SDS 457
Cdd:pfam02463 212 YYQLKEKLeleeeYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-EEEKLAQVLKENKEEEKEKKLQeeeLKL 290
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17505318 458 HNLEREAERIIRRLLQESQREDRRTAHFNKNDKPAAPKSTEEA 500
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Myb_DNA-bind_7 |
pfam15963 |
Myb DNA-binding like; |
251-337 |
1.08e-29 |
|
Myb DNA-binding like;
Pssm-ID: 464956 [Multi-domain] Cd Length: 85 Bit Score: 112.63 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 251 SFRKRGfgKSSFWSEKETDLFYEVLQCTGQDFGLMSHYLPKRTRPELKAKYNREEKINWARVLNAISHPVRLDGNLEVRI 330
Cdd:pfam15963 1 SFRKRK--KTKRWSKEETELFYKALSMFGTDFSLIAQLFPGRTRRQIKLKFKREERKNPELVDKALKNRKPFDLEEFKRL 78
|
....*..
gi 17505318 331 SKLMTEM 337
Cdd:pfam15963 79 LEKEKEE 85
|
|
| BDP1 |
COG5118 |
Transcription initiation factor TFIIIB, Bdp1 subunit [Transcription]; |
43-375 |
1.47e-12 |
|
Transcription initiation factor TFIIIB, Bdp1 subunit [Transcription];
Pssm-ID: 227448 [Multi-domain] Cd Length: 507 Bit Score: 70.90 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 43 ILENVetMTNQVSLTVASESMKSLHVDTSKNHHVHftdDVIDNEQNRIQETPDIVMISPTSQQNAQFASPNPPARLtprS 122
Cdd:COG5118 172 SPPTA--MTDSLDRNFSSETSTSREADENENYVIS---KVKDIPKKVRDGESAKYFIDEENFTMAELCKPNFPIQI---S 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 123 RNVSmcedEAILQPKQPRDKKRFSG--REELDTKTWKMSDLTRWNPKNEMTRFKRERRsstsssVITKSEIGDLDAPPAP 200
Cdd:COG5118 244 ENFE----KSKMAKKAKLEKRRHVKflEGSNTHEMDQLLKHFLDNSNFRQDRRSRKKK------ASASRDISDQNAEEIL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 201 RInapqvkigADGRLVIDETSLVV--HSAQINHESVWETVEEGRMGAKITSMSFRKRGfgKSSFWSEKETDLFYEVLQCT 278
Cdd:COG5118 314 MI--------KNGHIVVDEANMYVdrHKNASIEVEEMEVVEENPFARIVTSSTFGKKK--GALRWSKKEIEKFYKALSIW 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 279 GQDFGLMSHYLPKRTRPELKAKYNREEKINWARVLNA--ISHPVRLDGNLEVRISKLMTEMEEEAQEKKAKGEYEKAEEK 356
Cdd:COG5118 384 GTDFSLISSLFPNRERKQIKAKFIKEEKVNPERINEAlnEKKPFDQVEYNKLRSYLLEKLIELQNEHKHHMKEIEEAKNT 463
|
330
....*....|....*....
gi 17505318 357 RIREQNRLQKATERNQAKE 375
Cdd:COG5118 464 AKEEDQTAQRLNDANLNKK 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
339-504 |
1.78e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 339 EEAQEKKAKGEYEKAEEKRIREQNRlQKATERNQAKELVKQAKELERDARNA---AKLNMKADKEARAQEKSETRQLEKT 415
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAkkkAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 416 ALKE--ARLMATEAKRIAMEARaiikesRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRRTAHFNKNDKPAA 493
Cdd:PTZ00121 1363 EEKAeaAEKKKEEAKKKADAAK------KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
170
....*....|.
gi 17505318 494 PKSTEEATTSE 504
Cdd:PTZ00121 1437 KKKAEEAKKAD 1447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
326-483 |
9.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 326 LEVRISKLMTEMEEE-AQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNAAKLNMKADKEARAQ 404
Cdd:COG1196 272 LRLELEELELELEEAqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 405 EKSETRQLEKTAlkEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQ-ESQREDRRTA 483
Cdd:COG1196 352 ELEEAEAELAEA--EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERlEEELEELEEA 429
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
327-499 |
1.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 327 EVRISKLMTEMEEEA-----QEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKEL----ERDARNAAKLNMKA 397
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 398 DKEARAQEKSETRQLEKTALKEARLMATEAKRIAMEARAIIKES-RKLEKSKKADSVQS-DSHNLEREAERIIRRL--LQ 473
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkKKAEELKKAEEENKiKAEEAKKEAEEDKKKAeeAK 1750
|
170 180
....*....|....*....|....*.
gi 17505318 474 ESQREDRRTAHFNKNDKPAAPKSTEE 499
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-598 |
2.06e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 336 EMEEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNA-AKLNMKADKEARAQEKSETRQLEK 414
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 415 TalkEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRRTAHFNKNDKPAAP 494
Cdd:PTZ00121 1374 E---EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 495 KSTEEATTSEvSAPTKSPAPVVVTIDASEGELGDTSTDAADSSSASSSDDDALRKdaARREKQRMKEARRNLKPRKTVAD 574
Cdd:PTZ00121 1451 KKAEEAKKAE-EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEA 1527
|
250 260
....*....|....*....|....
gi 17505318 575 KKPVYVDTTDPKYAQQKVSRAVEM 598
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADEL 1551
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
326-481 |
2.13e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 326 LEVRISKLMTEMEE-EAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELvKQAKELERDARNAAKLNMKADKEARAQ 404
Cdd:COG1196 328 LEEELEELEEELEElEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELE 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17505318 405 EKSETRQLEKTALKEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRR 481
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
335-597 |
6.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 335 TEMEEEAQEKKAKGE--------YEKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNAAKLNMKADKEARAQEK 406
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEeakkadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 407 SETRQLEKTAlkEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRRTAHFN 486
Cdd:PTZ00121 1378 KKADAAKKKA--EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 487 KNDKPAAPKSTEEATTSEvSAPTKSPAPVVVTIDASEGELGDTSTDAADSSSASSSDDDALRKdaaRREKQRMKEARRNL 566
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK---AEEAKKADEAKKAE 1531
|
250 260 270
....*....|....*....|....*....|.
gi 17505318 567 KPRKTVADKKPVYVDTTDPKYAQQKVSRAVE 597
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-505 |
6.85e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 305 EKINWARVlNAISHPVRLDGNLEVRISKLMTEMEEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKELE 384
Cdd:PTZ00121 1053 DGNHEGKA-EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 385 --RDARNAAKLNmKADKEARAQEKSETRQLEKTALKEARLMATEAKRIAMEARAIikESRKLEKSKKADSVQSDSHNLER 462
Cdd:PTZ00121 1132 eaRKAEDARKAE-EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE--EVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17505318 463 EAERII---RRLLQESQREDRRTAHFNKNDKPAAPKSTEEATTSEV 505
Cdd:PTZ00121 1209 EEERKAeeaRKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
325-454 |
6.98e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 325 NLEVRISKLmtemeeEAQEKKAKGEYEKAEEKRiREQNRLQKATERnQAKELVKQAKELERDARNAAKLNMKADKEARAQ 404
Cdd:PRK00409 517 KLNELIASL------EELERELEQKAEEAEALL-KEAEKLKEELEE-KKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADE 588
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 17505318 405 EKSETRQLEKTALKEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQ 454
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
327-480 |
8.54e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 327 EVRISKLMTEMEEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKElerdARNAAKLNMKADKEAR-AQE 405
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE----AKKAEELKKKEAEEKKkAEE 1720
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17505318 406 KSETRQLEKTALKEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAerIIRRLLQESQREDR 480
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA--VIEEELDEEDEKRR 1793
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
339-450 |
2.58e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.15 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 339 EEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQA----KELERDARNAAKLNMKADKEARAQEKSET----- 409
Cdd:TIGR02794 66 EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAeqaaKQAEEKQKQAEEAKAKQAAEAKAKAEAEAerkak 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17505318 410 ----RQLEKTALKEArlmATEAKRIAMEARAIIKESRKLEKSKKA 450
Cdd:TIGR02794 146 eeaaKQAEEEAKAKA---AAEAKKKAEEAKKKAEAEAKAKAEAEA 187
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
325-483 |
2.74e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 325 NLEVRISKLMTEMEE-EAQEKKAKGEYEKAEEKRirEQNRLQKATERNQAKELVKQAKELERD-ARNAAKLNMKADKEAR 402
Cdd:COG1196 236 ELEAELEELEAELEElEAELEELEAELAELEAEL--EELRLELEELELELEEAQAEEYELLAElARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 403 AQEKSETRQLEKTALkEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRRT 482
Cdd:COG1196 314 LEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
.
gi 17505318 483 A 483
Cdd:COG1196 393 R 393
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
339-465 |
2.83e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 339 EEAQEKKAKGEYEKAEEKRIREQNRLQK-ATERNQAKELVKQAKELERDARNAAKLNMKADKEARAQEKSETRQLEKTAL 417
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17505318 418 KEARLMATEAKRIA---MEARAIIKESRKLEKSKKADSVQSDSHNLEREAE 465
Cdd:PRK09510 158 AAAKKAAAEAKKKAeaeAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAK 208
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
338-454 |
5.03e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 338 EEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNAAKLNMKADKEARAQEKSETRQLEKTAL 417
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
90 100 110
....*....|....*....|....*....|....*..
gi 17505318 418 KEARLMATEAKRIAMEARAiiKESRKLEKSKKADSVQ 454
Cdd:PRK09510 214 EAKKKAAAEAKAAAAKAAA--EAKAAAEKAAAAKAAE 248
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
332-430 |
5.61e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 332 KLMTEMEEEAQEKKAKGEYEKAEEKRIREQNRLQ----KATERNQAKELVKQAKELERDARNAAKLNMKAdKEARAQEks 407
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELeqklEDQERSYEEHLRQLKEKMEEERENLLKEQERA-LESKLKE-- 267
|
90 100
....*....|....*....|...
gi 17505318 408 ETRQLEKTALKEARLMATEAKRI 430
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSL 290
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
351-482 |
2.27e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 44.75 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 351 EKAEEKRIREQNRLQKATErnqakELVKQAKELERDARNAAKLNMKADKEARAQEKsETRQLEKtalKEARLMAtEAKRi 430
Cdd:COG1193 503 ERARELLGEESIDVEKLIE-----ELERERRELEEEREEAERLREELEKLREELEE-KLEELEE---EKEEILE-KARE- 571
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17505318 431 amEARAIIKESRklekskkadsvqsdshnleREAERIIRRlLQESQREDRRT 482
Cdd:COG1193 572 --EAEEILREAR-------------------KEAEELIRE-LREAQAEEEEL 601
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
336-465 |
5.04e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 336 EMEEEAQEKKAKGEYEKAEEKRIREQNRLQKAtERNQAKELVKQAKELERD------------ARNAAKLNMKADKEARA 403
Cdd:COG2268 209 ERETEIAIAQANREAEEAELEQEREIETARIA-EAEAELAKKKAEERREAEtaraeaeaayeiAEANAEREVQRQLEIAE 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17505318 404 QEKSETRQLEKTALKEARLMATEAKRIAMEARAIIKESRKLEKSKKADsvqsdshnLEREAE 465
Cdd:COG2268 288 REREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAK--------GLAEAE 341
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
316-500 |
8.56e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 316 ISHPVRLDGNLEVRISKLM-----TEMEEEAQEKKAKGEYEKAEEKRIREQNRLQK-----ATERNQAKELVKQAKELER 385
Cdd:pfam02463 132 PEAYNFLVQGGKIEIIAMMkperrLEIEEEAAGSRLKRKKKEALKKLIEETENLAEliidlEELKLQELKLKEQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 386 DARNAAKL-----NMKADKEARAQEKSETRQLEKTALKEARLMATEAKRIAmEARAIIKESRKLEKSKKADSVQ---SDS 457
Cdd:pfam02463 212 YYQLKEKLeleeeYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-EEEKLAQVLKENKEEEKEKKLQeeeLKL 290
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17505318 458 HNLEREAERIIRRLLQESQREDRRTAHFNKNDKPAAPKSTEEA 500
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
337-586 |
1.75e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 337 MEEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNAAKLNMKADK---EARAQEKSETRQLE 413
Cdd:PTZ00108 1131 LEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASvvgNSKRVDSDEKRKLD 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 414 KTALKEARlMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQESQREDRRTAHFNKNDKPAA 493
Cdd:PTZ00108 1211 DKPDNKKS-NSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPS 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 494 PKST-EEATTSEVSAPTKSPAPVVVTIDASEGELGDTSTDAADSSSASSSDDdalrKDAARREKQRMKEARRNLKPRKTV 572
Cdd:PTZ00108 1290 KRPDgESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRV----KQASASQSSRLLRRPRKKKSDSSS 1365
|
250
....*....|....
gi 17505318 573 ADKKPVYVDTTDPK 586
Cdd:PTZ00108 1366 EDDDDSEVDDSEDE 1379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
327-499 |
2.23e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 327 EVRISKLMTEMEEEAQEKKAKG-------EYEKAEEKRIREQNRLQKATERNQAKELVK------QAKELERDARNAAKL 393
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNmalrkaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeakiKAEELKKAEEEKKKV 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 394 NMKADKEARAQEKSEtrQLEKtALKEARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQ 473
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAE--ELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
170 180
....*....|....*....|....*....
gi 17505318 474 ESQR---EDRRTAHFNKNDKPAAPKSTEE 499
Cdd:PTZ00121 1713 EEKKkaeELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
344-471 |
2.46e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 344 KKAKGEYEKAEEKrireqnrLQKATERNQAKElvkqaKELERDARNAAKLNMKADK--EARAQEKSETRQLEKTALKEAR 421
Cdd:PRK00409 505 EEAKKLIGEDKEK-------LNELIASLEELE-----RELEQKAEEAEALLKEAEKlkEELEEKKEKLQEEEDKLLEEAE 572
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17505318 422 LMATEAKRIAM-EARAIIKESRKLEKSKKADSVqsdshnlEREAERIIRRL 471
Cdd:PRK00409 573 KEAQQAIKEAKkEADEIIKELRQLQKGGYASVK-------AHELIEARKRL 616
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
323-483 |
2.86e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 323 DGNLEvRISKLMTEMEE-----EAQEKKAKgEY-EKAEEKRIREQNRLQKATERNQAKELVKQAKELERDARNAAKLNMK 396
Cdd:COG1196 185 EENLE-RLEDILGELERqleplERQAEKAE-RYrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 397 ADKEARAQEKSETRQLEKTALKE--ARLMATEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERIIRRLLQE 474
Cdd:COG1196 263 AELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
....*....
gi 17505318 475 SQREDRRTA 483
Cdd:COG1196 343 EEELEEAEE 351
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
336-576 |
3.53e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 336 EMEEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAK----ELVKQAKELERDARNAAKLNMKADKEARAQEKSETRQ 411
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEirkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 412 LEKTalkearlmatEAKRIAMEARAIIKESRKLEKS-KKADSVQSDSHNLEREAERIIRR--LLQESQREDRRTAHFNKN 488
Cdd:PTZ00121 1295 AKKA----------EEKKKADEAKKKAEEAKKADEAkKKAEEAKKKADAAKKKAEEAKKAaeAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 489 DKPAAPKSTEEATTSEVSAPTKSPAPVVVTIDASEGELGDTSTDAADSSSASSSDDDALRKDA-----ARREKQRMKEAR 563
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeekkkADEAKKKAEEAK 1444
|
250
....*....|...
gi 17505318 564 RNLKPRKTVADKK 576
Cdd:PTZ00121 1445 KADEAKKKAEEAK 1457
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
336-464 |
6.01e-03 |
|
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: 39.83 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 336 EMEEEAQEKKAKGEYEKA-----EEKRIREQNRLQKATERNQAKE---LVKQAKELERDARNAAKLNMKADKEARAQEKS 407
Cdd:TIGR02794 93 ELEQRAAAEKAAKQAEQAakqaeEKQKQAEEAKAKQAAEAKAKAEaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 408 ETRQLEKTALKEArlmatEAKRIAMEARA---IIKESRKLEKSKKADSVQSDSHNLEREA 464
Cdd:TIGR02794 173 KKAEAEAKAKAEA-----EAKAKAEEAKAkaeAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
338-464 |
7.24e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.40 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 338 EEEAQEKKAKGEYEKAEE--KRIREQNRLQKATERNQAKELVKQAKElERDARNAAKLNMKADKEARAQEKSETRQ---- 411
Cdd:PRK09510 119 QAEEAAKQAALKQKQAEEaaAKAAAAAKAKAEAEAKRAAAAAKKAAA-EAKKKAEAEAAKKAAAEAKKKAEAEAAAkaaa 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 17505318 412 -LEKTALKEARLMA-TEAKRIAMEARAIIKESRKLEKSKKADSVQSDSHNLEREA 464
Cdd:PRK09510 198 eAKKKAEAEAKKKAaAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
335-525 |
9.35e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 39.64 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 335 TEMEEEAQEKKAKGEYEKAEEKRIREQNRLQKATERNQAKElvKQAKELERDARNAAKLNMKADKEARAQ--EKSETRQL 412
Cdd:PRK10811 582 GGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRD--TRDNRTRREGRENREENRRNRRQAQQQtaETRESQQA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505318 413 EKTALKEARLMATEAKRiAMEARAIIKESRKLEKSKKADSVQSDSHNLEREAERII-------RRLLQESQR---EDRRT 482
Cdd:PRK10811 660 EVTEKARTQDEQQQAPR-RERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQqvqprrkQRQLNQKVRieqSVAEE 738
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17505318 483 AHFNKNDKPAAPKSTEEATTSEVSAPTKSPAPVVVTIDASEGE 525
Cdd:PRK10811 739 AVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDE 781
|
|
|