|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
321-392 |
2.55e-21 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 94.83 E-value: 2.55e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221219056 321 SKRkDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEVQkeeekkFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK10767 2 AKR-DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGdKEAEEK------FKEIKEAYEVLSDPQKRAAYD 67
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
325-413 |
3.42e-21 |
|
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.
Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 94.20 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDS-GQDLDEEGM- 402
Cdd:TIGR02349 1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAE------EKFKEINEAYEVLSDPEKRAQYDQfGHAGFNGGGg 74
|
90
....*....|..
gi 221219056 403 -NMGDFDPNNIF 413
Cdd:TIGR02349 75 gGGGGFNGFDIG 86
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
113-342 |
9.54e-21 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 90.84 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 113 LEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDhekaci 192
Cdd:COG0457 1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 193 acrNAKALKAKkedGNKAFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYI 272
Cdd:COG0457 75 ---DAEALNNL---GLALQALGRYEEALEDYDKALELDPDD----AEALYNLGLALLELGRYDEAIEAYERALELDPDDA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 273 KAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIK 342
Cdd:COG0457 145 DALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAIL 214
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
325-392 |
1.36e-20 |
|
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.
Pssm-ID: 395170 [Multi-domain] Cd Length: 63 Bit Score: 84.83 E-value: 1.36e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEVQkeeekkFKEVGEAFTILSDPKKKTRYD 392
Cdd:pfam00226 1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGdPEAEEK------FKEINEAYEVLSDPEKRAIYD 63
|
|
| terminal_TopJ |
NF037946 |
terminal organelle assembly protein TopJ; |
321-413 |
3.39e-20 |
|
terminal organelle assembly protein TopJ;
Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 92.19 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 321 SKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDS-GQDlDE 399
Cdd:NF037946 2 EEKRDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAA------EIFAEINEAYEVLSNPEKRANYDKyGHD-GV 74
|
90
....*....|....
gi 221219056 400 EGMNMGDFDPNNIF 413
Cdd:NF037946 75 DGEGGFGFDAFDVF 88
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
323-406 |
1.61e-19 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 89.89 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDS-------- 393
Cdd:PRK14289 4 KRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGdKEAE------EKFKEAAEAYDVLSDPDKRSRYDQfghagvgg 77
|
90
....*....|....*.
gi 221219056 394 ---GQDLDEEGMNMGD 406
Cdd:PRK14289 78 aagGGGFSGEGMSMED 93
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
325-392 |
7.61e-19 |
|
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440252 [Multi-domain] Cd Length: 139 Bit Score: 82.44 E-value: 7.61e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEVQkeeekkFKEVGEAFTILSDPKKKTRYD 392
Cdd:COG0484 1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEK------FKEINEAYEVLSDPEKRAAYD 63
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
323-407 |
1.22e-18 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 87.16 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeekKFKEVGEAFTILSDPKKKTRYDSGQD--LDEE 400
Cdd:PRK14277 4 KKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQ-----KFKEINEAYEILSDPQKRAQYDQFGHaaFDPG 78
|
....*..
gi 221219056 401 GMNMGDF 407
Cdd:PRK14277 79 GFGQGGF 85
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
3-227 |
1.56e-18 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 84.67 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefkn 82
Cdd:COG0457 5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 83 anavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGL 162
Cdd:COG0457 79 ------LNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221219056 163 CLYYEDCIEKAVQFFVQAL-RMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEAL 227
Cdd:COG0457 153 ALEKLGRYEEALELLEKLEaAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAA 218
|
|
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
324-392 |
2.07e-17 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 83.29 E-value: 2.07e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14297 4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGnKEAE------EKFKEINEAYQVLSDPQKKAQYD 67
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
324-413 |
2.27e-17 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 83.06 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeeKKFKEVGEAFTILSDPKKKTRYDSGQDLD----E 399
Cdd:PRK14290 3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAE----EKFKEISEAYEVLSDPQKRRQYDQTGTVDfgagG 78
|
90
....*....|....*...
gi 221219056 400 EGMNMGDF----DPNNIF 413
Cdd:PRK14290 79 SNFNWDNFthfsDINDIF 96
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
321-392 |
2.35e-17 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 83.36 E-value: 2.35e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221219056 321 SKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14298 2 ATTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAE------EKFKEISEAYAVLSDAEKRAQYD 67
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
324-438 |
3.21e-17 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 82.97 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDSGQDLdeegM 402
Cdd:PRK14295 9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGdAKAE------ERFKEISEAYDVLSDEKKRKEYDEARSL----F 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 221219056 403 NMGDFDPNnifkaffggpggfsFEASGPGNFFFQFG 438
Cdd:PRK14295 79 GNGGFRPG--------------PGGGGGGGFNFDLG 100
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
325-413 |
3.56e-17 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 82.63 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeekkFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNM 404
Cdd:PRK14292 3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEK------FAQINEAYAVLSDAEKRAHYDRFGTAPGAGMPG 76
|
90
....*....|....*
gi 221219056 405 GD------FDPNNIF 413
Cdd:PRK14292 77 GDpfggmgFDPMDIF 91
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
324-393 |
9.06e-17 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 80.37 E-value: 9.06e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDS 393
Cdd:PRK14299 4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAE------EKFKEINEAYTVLSDPEKRRIYDT 67
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
39-330 |
1.04e-16 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 79.77 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 39 FVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefknanavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPA 118
Cdd:COG2956 7 AALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEA------------HLALGNLYRRRGEYDRAIRIHQKLLERDPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 119 CHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIacrnak 198
Cdd:COG2956 75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYC------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 199 alkakkEDGNKAFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRR 278
Cdd:COG2956 149 ------ELAELYLEQGDYDEAIEALEKALKLDPDC----ARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRL 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 221219056 279 AQCYMDTEQYEEAVRDYEKVYqtEKTKEHKQLLKNAQLELKKSKRKDYYKIL 330
Cdd:COG2956 219 AELYEKLGDPEEALELLRKAL--ELDPSDDLLLALADLLERKEGLEAALALL 268
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
324-387 |
1.42e-16 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 73.42 E-value: 1.42e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeeKKFKEVGEAFTILSDPKK 387
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAE----EKFKEINEAYEVLSDPEK 60
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
324-392 |
2.79e-16 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 80.16 E-value: 2.79e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14279 9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGdPAAE------ERFKAVSEAHDVLSDPAKRKEYD 72
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
321-407 |
5.11e-16 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 79.38 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 321 SKRkDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD------SG 394
Cdd:PRK14280 2 AKR-DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGAD------EKFKEISEAYEVLSDDQKRAQYDqfghagPN 74
|
90
....*....|...
gi 221219056 395 QDLDEEGMNMGDF 407
Cdd:PRK14280 75 QGFGGGGFGGGDF 87
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
12-297 |
5.59e-16 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 77.85 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 12 RAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEfknanavmeyek 91
Cdd:COG2956 14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 92 IAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIE 171
Cdd:COG2956 82 LAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 172 KAVQFFVQALRMAPDHEKACIACrnakalkakkedGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLycnrGTVNSKL 251
Cdd:COG2956 162 EAIEALEKALKLDPDCARALLLL------------AELYLEQGDYEEAIAALERALEQDPDYLPALPRL----AELYEKL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 221219056 252 RKLDDAIEDCTNAVKLDDTyIKAYLRRAQCYMDTEQYEEAVRDYEK 297
Cdd:COG2956 226 GDPEEALELLRKALELDPS-DDLLLALADLLERKEGLEAALALLER 270
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
323-412 |
5.70e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 79.04 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD-------SGQ 395
Cdd:PRK14291 2 KKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAE------EKFKEINEAYQVLSDPEKRKLYDqfghaafSGS 75
|
90
....*....|....*...
gi 221219056 396 DLDEEGMN-MGDFDPNNI 412
Cdd:PRK14291 76 GQQQQGQEgFSDFGGGNI 93
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
324-392 |
5.94e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 78.98 E-value: 5.94e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14276 4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAE------EKYKEVQEAYETLSDPQKRAAYD 66
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
321-392 |
6.59e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 78.65 E-value: 6.59e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221219056 321 SKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEVQkeeekkFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14294 1 MVKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGdKEAEEL------FKEAAEAYEVLSDPKKRGIYD 67
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
323-408 |
7.00e-16 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 78.90 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeekkFKEVGEAFTILSDPKKKTRYDSGQDLDEE-- 400
Cdd:PRK14287 3 KRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDK------FKEVKEAYDTLSDPQKKAHYDQFGHTDPNqg 76
|
90
....*....|
gi 221219056 401 --GMNMGDFD 408
Cdd:PRK14287 77 fgGGGAGDFG 86
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
323-392 |
1.16e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 78.25 E-value: 1.16e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14301 3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDnPEAE------QKFKEAAEAYEVLRDAEKRARYD 67
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
195-300 |
1.41e-15 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 75.72 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 195 RNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKA 274
Cdd:COG4785 68 ALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDL----AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
|
90 100
....*....|....*....|....*.
gi 221219056 275 YLRRAQCYMDTEQYEEAVRDYEKVYQ 300
Cdd:COG4785 144 YLNRGIALYYLGRYELAIADLEKALE 169
|
|
| termin_org_DnaJ |
TIGR03835 |
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ... |
323-415 |
1.95e-15 |
|
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274808 [Multi-domain] Cd Length: 871 Bit Score: 78.70 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDS-GQD-LDEE 400
Cdd:TIGR03835 1 KRDYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRNKAPDAA------SIFAEINEANDVLSNPKKRANYDKyGHDgVDRE 74
|
90
....*....|....*
gi 221219056 401 GMNmgDFDPnNIFKA 415
Cdd:TIGR03835 75 DDF--DFQA-DVFNS 86
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
323-392 |
1.96e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 77.56 E-value: 1.96e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14283 4 KRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAE------EKFKEISEAYAVLSDDEKRQRYD 67
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
130-306 |
2.18e-15 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 78.50 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 130 LAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACrnakalkakkedGNK 209
Cdd:COG3914 88 LQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNL------------GEA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 210 AFKEGNYKLAYELYTEALGIDPNniktNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYE 289
Cdd:COG3914 156 LRRLGRLEEAIAALRRALELDPD----NAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWE 231
|
170
....*....|....*..
gi 221219056 290 EAVRDYEKVYQTEKTKE 306
Cdd:COG3914 232 VYDRFEELLAALARGPS 248
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
323-392 |
4.11e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 76.37 E-value: 4.11e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14282 3 KKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAE----QKFKEIQEAYEVLSDPQKRAMYD 68
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
325-384 |
4.84e-15 |
|
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.
Pssm-ID: 99751 [Multi-domain] Cd Length: 55 Bit Score: 69.11 E-value: 4.84e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeekKFKEVGEAFTILSD 384
Cdd:cd06257 1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEE-----KFKEINEAYEVLSD 55
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
325-392 |
5.89e-15 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 76.03 E-value: 5.89e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14284 2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGdAEAE------KRFKEVSEAYEVLSDAQKRESYD 64
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
67-330 |
2.57e-14 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 72.35 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 67 LELDHKNAQAqqefknanavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDI 146
Cdd:COG0457 1 LELDPDDAEA------------YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 147 LRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDhekaciacrNAKALKAKkedGNKAFKEGNYKLAYELYTEA 226
Cdd:COG0457 69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPD---------DAEALYNL---GLALLELGRYDEAIEAYERA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 227 LGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKE 306
Cdd:COG0457 137 LELDPDD----ADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLA 212
|
250 260
....*....|....*....|....
gi 221219056 307 HKQLLKNAQLELKKSKRKDYYKIL 330
Cdd:COG0457 213 ILTLAALAELLLLALALLLALRLA 236
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
323-415 |
3.17e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 74.07 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGAS-AEvqkeeeKKFKEVGEAFTILSDPKKKTRYD--------- 392
Cdd:PRK14281 2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKeAE------EHFKEVNEAYEVLSNDDKRRRYDqfghagvgs 75
|
90 100
....*....|....*....|...
gi 221219056 393 SGQDLDEEGMNMGDFDPNNIFKA 415
Cdd:PRK14281 76 SAASGGGPGYGGGGGDFNDIFSA 98
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
325-407 |
3.74e-14 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 73.49 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD-------SG--- 394
Cdd:PRK14293 4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAE------DRFKEINRAYEVLSDPETRARYDqfgeagvSGaag 77
|
90
....*....|....
gi 221219056 395 -QDLDeegmNMGDF 407
Cdd:PRK14293 78 fPDMG----DMGGF 87
|
|
| SEC63 |
COG5407 |
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
325-390 |
4.30e-14 |
|
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 66.56 E-value: 4.30e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSG-ASAEvqkeeeKKFKEVGEAFTILSDPKKKTR 390
Cdd:COG5407 1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGdPKAE------ERFKEINEAYELLSDAEKRAR 61
|
|
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
324-413 |
4.68e-14 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 73.70 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRhsGASAEvqkeeekKFKEVGEAFTILSDPKKKTRYDsgqDLDEEGM- 402
Cdd:PTZ00037 28 EKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDK--GGDPE-------KFKEISRAYEVLSDPEKRKIYD---EYGEEGLe 95
|
90
....*....|..
gi 221219056 403 -NMGDFDPNNIF 413
Cdd:PTZ00037 96 gGEQPADASDLF 107
|
|
| PLN03088 |
PLN03088 |
SGT1, suppressor of G2 allele of SKP1; Provisional |
197-297 |
6.91e-14 |
|
SGT1, suppressor of G2 allele of SKP1; Provisional
Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 72.51 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 197 AKALKAKkedGNKAFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYL 276
Cdd:PLN03088 2 AKDLEDK---AKEAFVDDDFALAVDLYTQAIDLDPNN----AELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYL 74
|
90 100
....*....|....*....|.
gi 221219056 277 RRAQCYMDTEQYEEAVRDYEK 297
Cdd:PLN03088 75 RKGTACMKLEEYQTAKAALEK 95
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
321-392 |
7.24e-14 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 67.05 E-value: 7.24e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221219056 321 SKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHsgasAEVQKEEEKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:COG2214 2 PDLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRG----GELKALAEELFQRLNEAYEVLSDPERRAEYD 69
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
324-401 |
8.86e-14 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 72.39 E-value: 8.86e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEG 401
Cdd:PRK14278 3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQ------EKFKEISVAYEVLSDPEKRRIVDLGGDPLESA 74
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
11-191 |
9.36e-14 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 73.10 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 11 NRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREgkcHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYE 90
Cdd:COG3914 52 AEAAAAALLALAAGEAAAAAAALLLLAALLELAALL---LQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 91 KIAETdfekrdfrkvvfCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCI 170
Cdd:COG3914 129 EEALA------------ALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRL 196
|
170 180
....*....|....*....|.
gi 221219056 171 EKAVQFFVQALRMAPDHEKAC 191
Cdd:COG3914 197 EEAIAAYRRALELDPDNADAH 217
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
153-300 |
1.74e-13 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 72.33 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 153 NADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKED-----GNKAFKEGNYKLAYELYTEAL 227
Cdd:COG3914 60 LALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEalfnlGNLLLALGRLEEALAALRRAL 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221219056 228 GIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQ 300
Cdd:COG3914 140 ALNPDF----AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALE 208
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
324-405 |
6.79e-13 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 69.63 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGasaevQKEEEKKFKEVGEAFTILSDPKKKTRYDSgqdLDEEGMN 403
Cdd:PRK14286 4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKG-----NKESEEKFKEATEAYEILRDPKKRQAYDQ---FGKAGVN 75
|
..
gi 221219056 404 MG 405
Cdd:PRK14286 76 AG 77
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
33-227 |
8.04e-13 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 68.11 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 33 VRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefknanavmeYEKIAETDFEKRDFRKVVFCMDRA 112
Cdd:COG0457 1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEA------------LYNLGLAYLRLGRYEEALADYEQA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 113 LEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACI 192
Cdd:COG0457 69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALY 148
|
170 180 190
....*....|....*....|....*....|....*
gi 221219056 193 ACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEAL 227
Cdd:COG0457 149 NLGIALEKLGRYEEALELLEKLEAAALAALLAAAL 183
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
323-392 |
2.24e-12 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 68.09 E-value: 2.24e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 323 RKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGasaevQKEEEKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14285 2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKG-----NKEAESIFKEATEAYEVLIDDNKRAQYD 66
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
179-300 |
6.81e-12 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 67.33 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 179 QALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNniktNAKLYCNRGTVNSKLRKLDDAI 258
Cdd:COG3914 57 AALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPD----NAEALFNLGNLLLALGRLEEAL 132
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 221219056 259 EDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQ 300
Cdd:COG3914 133 AALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALE 174
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
325-386 |
2.64e-11 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 59.04 E-value: 2.64e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221219056 325 DYYKILGVDKNASEDEIKKAYRKRALMHHPDRH-SGASAEVQKEEEKKFKEVGEAFTILSDPK 386
Cdd:COG1076 5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRLaAGLPEEEQRLALQKAAAINEAYETLKDPR 67
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
322-392 |
4.60e-11 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 64.20 E-value: 4.60e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221219056 322 KRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK14296 2 KKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAH------DKMVEINEAADVLLDKDKRKQYD 66
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
12-182 |
4.76e-11 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 64.63 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 12 RAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQefknanavmeyeK 91
Cdd:COG3914 84 AALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYL------------N 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 92 IAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYvRGLCLYYEDCIE 171
Cdd:COG3914 152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHS-NLLFALRQACDW 230
|
170
....*....|.
gi 221219056 172 KAVQFFVQALR 182
Cdd:COG3914 231 EVYDRFEELLA 241
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
3-188 |
7.42e-11 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 62.44 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQ---- 78
Cdd:COG2956 39 PETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRllae 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 79 ------EFKNANAVME------------YEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQ 140
Cdd:COG2956 119 iyeqegDWEKAIEVLErllklgpenahaYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 221219056 141 SVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHE 188
Cdd:COG2956 199 AALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDD 246
|
|
| 3a0801s09 |
TIGR00990 |
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
195-295 |
1.11e-10 |
|
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 63.46 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 195 RNAKALKAKkEDGNKAFKEGNYKLAYELYTEALGIDPNNIktnakLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKA 274
Cdd:TIGR00990 123 RKKYAAKLK-EKGNKAYRNKDFNKAIKLYSKAIECKPDPV-----YYSNRAACHNALGDWEKVVEDTTAALELDPDYSKA 196
|
90 100
....*....|....*....|.
gi 221219056 275 YLRRAQCYMDTEQYEEAVRDY 295
Cdd:TIGR00990 197 LNRRANAYDGLGKYADALLDL 217
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
154-300 |
2.18e-10 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 58.66 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 154 ADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDhekaciacrNAKALKAKkedGNKAFKEGNYKLAYELYTEALGIDPNN 233
Cdd:COG4783 4 AEALYALAQALLLAGDYDEAEALLEKALELDPD---------NPEAFALL---GEILLQLGDLDEAIVLLHEALELDPDE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221219056 234 iktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQ 300
Cdd:COG4783 72 ----PEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALE 134
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
324-413 |
1.20e-09 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 59.64 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEvqkeeeKKFKEVGEAFTILSDPKKKTRYDS-GQDLDEE-- 400
Cdd:PRK14300 3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAE------KKFKEINAAYDVLKDEQKRAAYDRfGHDAFQNqq 76
|
90
....*....|....*....
gi 221219056 401 ----GMNMGDFDP--NNIF 413
Cdd:PRK14300 77 srggGGNHGGFHPdiNDIF 95
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
324-392 |
3.15e-09 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 57.91 E-value: 3.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQkeeekkFKEVGEAFTILSDPKKKTRYD 392
Cdd:PRK10266 4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEAR------FKEVAEAWEVLSDEQRRAEYD 66
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
83-233 |
3.48e-09 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 55.20 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 83 ANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGL 162
Cdd:COG4783 1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221219056 163 CLYYEDCIEKAVQFFVQALRMAPDHEKAciACRNAKALKAKkedgnkafkeGNYKLAYELYTEALGIDPNN 233
Cdd:COG4783 81 ALLKAGDYDEALALLEKALKLDPEHPEA--YLRLARAYRAL----------GRPDEAIAALEKALELDPDD 139
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
3-153 |
3.60e-09 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 58.85 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEfkn 82
Cdd:COG3914 109 PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN--- 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221219056 83 anavmeyekIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTN 153
Cdd:COG3914 186 ---------LGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELLAALARGP 247
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
326-407 |
1.12e-08 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 56.62 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 326 YYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGasaevQKEEEKKFKEVGEAFTILSDPKKKTRYD--SGQDLDEEGMN 403
Cdd:PRK14288 5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAG-----DKEAEEKFKLINEAYGVLSDEKKRALYDryGKKGLNQAGAS 79
|
....
gi 221219056 404 MGDF 407
Cdd:PRK14288 80 QSDF 83
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
210-300 |
1.73e-08 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 51.71 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 210 AFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEdCTNAVKLDDTYIKAYLRRAQCYMDTEQYE 289
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELDPDN----ADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD 76
|
90
....*....|.
gi 221219056 290 EAVRDYEKVYQ 300
Cdd:COG3063 77 EALAYLERALE 87
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
58-190 |
1.93e-08 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 52.70 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 58 AACRSFQRALELDHKNAQAqqefknanavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYP 137
Cdd:COG4235 1 EAIARLRQALAANPNDAEG------------WLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 221219056 138 EAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKA 190
Cdd:COG4235 69 EAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPA 121
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
207-355 |
2.17e-08 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 55.12 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 207 GNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLycnrGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTE 286
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELDPETVEAHLAL----GNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 287 QYEEAVRDYEKVYQT---------------EKTKEHKQLLKNA-QLELKKSKRKDYYKILGV--DKNASEDEIKKAYRKr 348
Cdd:COG2956 91 LLDRAEELLEKLLELdpddaealrllaeiyEQEGDWEKAIEVLeRLLKLGPENAHAYCELAElyLEQGDYDEAIEALEK- 169
|
....*..
gi 221219056 349 ALMHHPD 355
Cdd:COG2956 170 ALKLDPD 176
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
197-298 |
2.79e-08 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 52.50 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 197 AKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYL 276
Cdd:COG4783 1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDN----PEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARL 76
|
90 100
....*....|....*....|..
gi 221219056 277 RRAQCYMDTEQYEEAVRDYEKV 298
Cdd:COG4783 77 NLGLALLKAGDYDEALALLEKA 98
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
207-298 |
5.71e-08 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 51.16 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 207 GNKAFKEGNYKLAYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTE 286
Cdd:COG4235 24 GRAYLRLGRYDEALAAYEKALRLDPDN----ADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQG 99
|
90
....*....|..
gi 221219056 287 QYEEAVRDYEKV 298
Cdd:COG4235 100 DYAEAIAAWQKL 111
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
3-302 |
5.98e-08 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 55.09 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqEFKN 82
Cdd:TIGR02917 156 PRSLYAKLGLAQLALAENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAV--LLAL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 83 ANAVMEYEKIAETDFEkrdfrkvvfcMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGL 162
Cdd:TIGR02917 234 ATILIEAGEFEEAEKH----------ADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 163 CLYYEDCIEKAVQFFVQALRMAPDHekaciacRNAKALKAKKEdgnkaFKEGNYKLAYELYTEALGIDPNniktNAKLYC 242
Cdd:TIGR02917 304 SEYQLGNLEQAYQYLNQILKYAPNS-------HQARRLLASIQ-----LRLGRVDEAIATLSPALGLDPD----DPAALS 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 243 NRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTE 302
Cdd:TIGR02917 368 LLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLD 427
|
|
| djlA |
PRK09430 |
co-chaperone DjlA; |
324-355 |
1.26e-07 |
|
co-chaperone DjlA;
Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 52.51 E-value: 1.26e-07
10 20 30
....*....|....*....|....*....|....
gi 221219056 324 KDYYKILGVDKNASEDEIKKAYRKraLM--HHPD 355
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRK--LMseHHPD 231
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
153-303 |
1.31e-07 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 51.11 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 153 NADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPN 232
Cdd:COG5010 7 FDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPN 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221219056 233 NiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEK 303
Cdd:COG5010 87 N----PELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
104-233 |
2.32e-07 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 49.62 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 104 KVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRM 183
Cdd:COG4235 1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 221219056 184 APDHekaciacrnakaLKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNN 233
Cdd:COG4235 81 DPDN------------PEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
1-76 |
7.27e-07 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 49.91 E-value: 7.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221219056 1 MCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQA 76
Cdd:COG4785 102 LDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPNDPER 177
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
6-153 |
1.27e-06 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 47.49 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 6 ASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefknana 85
Cdd:COG4783 4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEA--------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 86 vmeYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTN 153
Cdd:COG4783 75 ---RLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
47-323 |
1.55e-06 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 50.47 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 47 GKCHLSLGNAMAACRSFQRALELDHKNAQA----------QQEFKNANAVME-------------YEKIAETDFEKRDFR 103
Cdd:TIGR02917 63 GKIYLALGDYAAAEKELRKALSLGYPKNQVlpllarayllQGKFQQVLDELPgktllddegaaelLALRGLAYLGLGQLE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 104 KVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRM 183
Cdd:TIGR02917 143 LAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIAL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 184 APDHEKACIAcrnakalkakkeDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKlycnRGTVNSKLRKLDDAIEDCTN 263
Cdd:TIGR02917 223 RPNNIAVLLA------------LATILIEAGEFEEAEKHADALLKKAPNSPLAHYL----KALVDFQKKNYEDARETLQD 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221219056 264 AVKLDDTYIKA-YLRRAQCYM--DTEQYEEAVRDYEKvyQTEKTKEHKQLLKNAQLELKKSKR 323
Cdd:TIGR02917 287 ALKSAPEYLPAlLLAGASEYQlgNLEQAYQYLNQILK--YAPNSHQARRLLASIQLRLGRVDE 347
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
3-150 |
3.26e-06 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 48.57 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefkn 82
Cdd:COG2956 141 PENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPA------ 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 83 anavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPAcHRFKILKAECLAMLGRYPEAQSVASDILRMD 150
Cdd:COG2956 215 ------LPRLAELYEKLGDPEEALELLRKALELDPS-DDLLLALADLLERKEGLEAALALLERQLRRH 275
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
2-76 |
7.55e-06 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 46.83 E-value: 7.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221219056 2 CPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQA 76
Cdd:COG4785 69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
3-352 |
1.26e-05 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.77 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNamaacrsFQRALEldhknAQAQQEFKN 82
Cdd:TIGR02917 394 PENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQ-------FDKALA-----AAKKLEKKQ 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 83 ANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPAcHRFKILKaecLAML----GRYPEAQSVASDILRMDSTNADALy 158
Cdd:TIGR02917 462 PDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPD-FFPAAAN---LARIdiqeGNPDDAIQRFEKVLTIDPKNLRAI- 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 159 vRGLCLYYEDC--IEKAVQFFVQALRmapdhekaciacRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALgidpNNIKT 236
Cdd:TIGR02917 537 -LALAGLYLRTgnEEEAVAWLEKAAE------------LNPQEIEPALALAQYYLGKGQLKKALAILNEAA----DAAPD 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 237 NAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKnAQL 316
Cdd:TIGR02917 600 SPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGL-AQL 678
|
330 340 350
....*....|....*....|....*....|....*.
gi 221219056 317 ELKKSKRKDYYKILgvdknaseDEIKKAYRKRALMH 352
Cdd:TIGR02917 679 LLAAKRTESAKKIA--------KSLQKQHPKAALGF 706
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
317-393 |
1.30e-05 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 46.95 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 317 ELKKSKRKDYYKILGVDK---NASEDEIKKAYRKRALMHHPDRhsgASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDS 393
Cdd:COG5269 36 DFKNWKKVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDK---TAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDS 112
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
3-118 |
1.33e-05 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 44.61 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefkn 82
Cdd:COG4235 14 PNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEA------ 87
|
90 100 110
....*....|....*....|....*....|....*.
gi 221219056 83 anavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPA 118
Cdd:COG4235 88 ------LYLLGLAAFQQGDYAEAIAAWQKLLALLPA 117
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
3-99 |
1.55e-05 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 44.41 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKN 82
Cdd:COG4783 35 PDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLAR 114
|
90
....*....|....*..
gi 221219056 83 ANAVMEYEKIAETDFEK 99
Cdd:COG4783 115 AYRALGRPDEAIAALEK 131
|
|
| PRK11447 |
PRK11447 |
cellulose synthase subunit BcsC; Provisional |
134-234 |
3.52e-05 |
|
cellulose synthase subunit BcsC; Provisional
Pssm-ID: 183140 [Multi-domain] Cd Length: 1157 Bit Score: 46.23 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 134 GRYPEAQSVASDILRMDSTNADAlyVRGLC-LYYEDCIEKAVQFfVQALrmaPDHEKACIA-CRNAKALKAKKEDGNKAF 211
Cdd:PRK11447 399 KDYAAAERYYQQALRMDPGNTNA--VRGLAnLYRQQSPEKALAF-IASL---SASQRRSIDdIERSLQNDRLAQQAEALE 472
|
90 100
....*....|....*....|...
gi 221219056 212 KEGNYKLAYELYTEALGIDPNNI 234
Cdd:PRK11447 473 NQGKWAQAAELQRQRLALDPGSV 495
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
3-70 |
4.16e-05 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 42.08 E-value: 4.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALgDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELD 70
Cdd:COG3063 23 PDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELD 89
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
248-392 |
4.20e-05 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 45.93 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 248 NSKLRKLDDAIEDCTnavkLDDTYIKAYLRRAQcymdtEQYEEAVRDYEKVYQTEKTkehkqllknaqLELKKSKrkdYY 327
Cdd:PTZ00341 520 NEEQQTADEHVEEPT----IAEEHVEEEISTAE-----EHIEEPASDVQQDSEAAPT-----------IEIPDTL---FY 576
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221219056 328 KILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAevqkeeEKKFKEVGEAFTILSDPKKKTRYD 392
Cdd:PTZ00341 577 DILGVGVNADMKEISERYFKLAENYYPPKRSGNEG------FHKFKKINEAYQILGDIDKKKMYN 635
|
|
| PLN03088 |
PLN03088 |
SGT1, suppressor of G2 allele of SKP1; Provisional |
3-94 |
4.34e-05 |
|
SGT1, suppressor of G2 allele of SKP1; Provisional
Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 45.55 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAAcrsfQRALELDHKNAQAQQEFKN 82
Cdd:PLN03088 33 PNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTA----KAALEKGASLAPGDSRFTK 108
|
90
....*....|..
gi 221219056 83 ANAVMEyEKIAE 94
Cdd:PLN03088 109 LIKECD-EKIAE 119
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
3-73 |
7.53e-05 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 42.49 E-value: 7.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKN 73
Cdd:COG4783 69 PDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
219-298 |
9.02e-05 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 41.92 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 219 AYELYTEALGIDPNNiktnAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKV 298
Cdd:COG4235 2 AIARLRQALAANPND----AEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERA 77
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
16-121 |
9.54e-05 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 41.31 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 16 LMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAAcRSFQRALELDHKNAQAqqefknanavmeYEKIAET 95
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEA------------LLNLAEL 68
|
90 100
....*....|....*....|....*.
gi 221219056 96 DFEKRDFRKVVFCMDRALEFAPACHR 121
Cdd:COG3063 69 LLELGDYDEALAYLERALELDPSALR 94
|
|
| BamD |
COG4105 |
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ... |
56-320 |
1.06e-04 |
|
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443281 [Multi-domain] Cd Length: 254 Bit Score: 43.72 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 56 AMAACRSFQRALeldhKNAQAQQEFKNANAVME---YEKiAETDFEKrdfrkvvfcMDRALEFAPACHRFKILKAECLAM 132
Cdd:COG4105 16 LLAGCSSFKKAL----KSWDAEELYEEAKEALEkgdYEK-AIKLFEE---------LEPRYPGSPYAEQAQLMLAYAYYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 133 LGRYPEAQSVASDILRM--DSTNAD-ALYVRGLCLYYED--------CIEKAVQFFVQALRMAPDHEKAciacrnakalk 201
Cdd:COG4105 82 QGDYEEAIAAADRFIKLypNSPNADyAYYLRGLSYYEQSpdsdrdqtSTRKAIEAFQELINRYPDSEYA----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 202 akkEDGNKAFKEGNYKLA-YELYtealgidpnniktNAKLYCNRGTVNSKLRKLDDAIEDC--TNAVKlddtyiKAYLRR 278
Cdd:COG4105 151 ---EDAKKRIDELRDKLArKELE-------------VARYYLKRGAYVAAINRFQNVLEDYpdTPAVE------EALYLL 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221219056 279 AQCYMDTEQYEEAvRDYEKVYQ-----TEKTKEHKQLLKNAQLELKK 320
Cdd:COG4105 209 VEAYYALGRYDEA-QDAAAVLGknypdSPYLKDAEKLLKKIGKELKK 254
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
110-231 |
1.46e-04 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 42.25 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 110 DRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEK 189
Cdd:COG5010 44 AAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPN 123
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 221219056 190 ACIACRNAKAlkakkedgnkafKEGNYKLAYELYTEALGIDP 231
Cdd:COG5010 124 AYSNLAALLL------------SLGQDDEAKAALQRALGTSP 153
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
6-99 |
2.94e-04 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 41.10 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 6 ASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANA 85
Cdd:COG5010 54 FAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLL 133
|
90
....*....|....
gi 221219056 86 VMEYEKIAETDFEK 99
Cdd:COG5010 134 SLGQDDEAKAALQR 147
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
129-232 |
4.77e-04 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 39.00 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 129 CLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFvQALRMAPDhekaciacrNAKALKAKkedGN 208
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALE-KALKLDPN---------NAEALLNL---AE 67
|
90 100
....*....|....*....|....
gi 221219056 209 KAFKEGNYKLAYELYTEALGIDPN 232
Cdd:COG3063 68 LLLELGDYDEALAYLERALELDPS 91
|
|
| CpoB |
COG1729 |
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ... |
209-301 |
5.70e-04 |
|
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 39.20 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 209 KAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYcNRGTVNSKLRKLDDAIEDCTNAVKL---DDTYIKAYLRRAQCYMDT 285
Cdd:COG1729 2 ALLKAGDYDEAIAAFKAFLKRYPNSPLAPDALY-WLGEAYYALGDYDEAAEAFEKLLKRypdSPKAPDALLKLGLSYLEL 80
|
90
....*....|....*.
gi 221219056 286 EQYEEAVRDYEKVYQT 301
Cdd:COG1729 81 GDYDKARATLEELIKK 96
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
3-70 |
6.22e-04 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 40.33 E-value: 6.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELD 70
Cdd:COG5010 85 PNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTS 152
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
74-185 |
9.09e-04 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 39.94 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 74 AQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTN 153
Cdd:COG5010 42 LAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDN 121
|
90 100 110
....*....|....*....|....*....|..
gi 221219056 154 ADALYVRGLCLYYEDCIEKAVQFFVQALRMAP 185
Cdd:COG5010 122 PNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
|
|
| TPR_1 |
pfam00515 |
Tetratricopeptide repeat; |
238-271 |
1.74e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 35.86 E-value: 1.74e-03
10 20 30
....*....|....*....|....*....|....
gi 221219056 238 AKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTY 271
Cdd:pfam00515 1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
|
|
| PRK12370 |
PRK12370 |
HilA/EilA family virulence transcriptional regulator; |
48-176 |
2.10e-03 |
|
HilA/EilA family virulence transcriptional regulator;
Pssm-ID: 237080 [Multi-domain] Cd Length: 553 Bit Score: 40.22 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 48 KCHLSLG--------NAM-AACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKrdfrkvvfcmdrALEFAPA 118
Cdd:PRK12370 303 ECYLSMAqmgifdkqNAMiKAKEHAIKATELDHNNPQALGLLGLINTIHSEYIVGSLLFKQ------------ANLLSPI 370
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 119 CHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQF 176
Cdd:PRK12370 371 SADIKYYYGWNLFMAGQLEEALQTINECLKLDPTRAAAGITKLWITYYHTGIDDAIRL 428
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
43-322 |
2.22e-03 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 40.45 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 43 HLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEfknanavmeyekIAETDFEKRDFRKVVFCMDRALEFAPACHRF 122
Cdd:TIGR02917 25 LIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFL------------LGKIYLALGDYAAAEKELRKALSLGYPKNQV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 123 KILKAECLAMLGRYPEAQSVASDILRMDSTNADALY-VRGLCLYYEDCIEKAVQFFVQALRMAPdhekaciacrnaKALK 201
Cdd:TIGR02917 93 LPLLARAYLLQGKFQQVLDELPGKTLLDDEGAAELLaLRGLAYLGLGQLELAQKSYEQALAIDP------------RSLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 202 AKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKtnAKLYcnRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQC 281
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVLTADPGNVD--ALLL--KGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 221219056 282 YMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKnAQLELKKSK 322
Cdd:TIGR02917 237 LIEAGEFEEAEKHADALLKKAPNSPLAHYLK-ALVDFQKKN 276
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
3-147 |
2.51e-03 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 39.22 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNamaacrsFQRALELDHKNAQAQQEFKN 82
Cdd:COG0457 107 PDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGR-------YEEALELLEKLEAAALAALL 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221219056 83 ANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDIL 147
Cdd:COG0457 180 AAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYR 244
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
3-150 |
3.35e-03 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 38.02 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAqqefkn 82
Cdd:COG5010 17 LTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPEL------ 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221219056 83 anavmeYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMD 150
Cdd:COG5010 91 ------YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTS 152
|
|
| NlpI |
COG4785 |
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis]; |
50-250 |
4.39e-03 |
|
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 38.36 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 50 HLSLGNAMAACRSFQRALE--LDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFApachrfkiLKA 127
Cdd:COG4785 9 LLALALAAAAASKAAILLAalLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLYY--------ERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 128 ECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKAciacRNAKALkakkedg 207
Cdd:COG4785 81 VAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA----YLNRGI------- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 221219056 208 nkAFKE-GNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSK 250
Cdd:COG4785 150 --ALYYlGRYELAIADLEKALELDPNDPERALWLYLAERKLDPE 191
|
|
| 3a0801s09 |
TIGR00990 |
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
3-205 |
5.40e-03 |
|
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 39.20 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 3 PKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALeldhknaqaqQEFKN 82
Cdd:TIGR00990 396 SEDPDIYYHRAQLHFIKGEFAQAGKDYQKSIDLDPDFIFSHIQLGVTQYKEGSIASSMATFRRCK----------KNFPE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221219056 83 ANAVMEYekIAETDFEKRDFRKVVFCMDRALEFA----PACHRFKILKAECLAML---GRYPEAQSVASDILRMDSTNAD 155
Cdd:TIGR00990 466 APDVYNY--YGELLLDQNKFDEAIEKFDTAIELEketkPMYMNVLPLINKALALFqwkQDFIEAENLCEKALIIDPECDI 543
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221219056 156 ALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKE 205
Cdd:TIGR00990 544 AVATMAQLLLQQGDVDEALKLFERAAELARTEGELVQAISYAEATRTQIQ 593
|
|
| TPR |
smart00028 |
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ... |
238-271 |
5.85e-03 |
|
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.
Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 34.34 E-value: 5.85e-03
10 20 30
....*....|....*....|....*....|....
gi 221219056 238 AKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTY 271
Cdd:smart00028 1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
|
|
| |
