|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00037 |
PTZ00037 |
DnaJ_C chaperone protein; Provisional |
2-317 |
1.38e-90 |
|
DnaJ_C chaperone protein; Provisional
Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 276.32 E-value: 1.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 2 VKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEgEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKeggsGSPS 81
Cdd:PTZ00037 25 VDNEKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP-EKFKEISRAYEVLSDPEKRKIYDEYGEEGLE----GGEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 82 FSSPMDIFDMFFGGGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEKCPLCKGRGMQI 161
Cdd:PTZ00037 100 PADASDLFDLIFGGGRKPGGKKRGEDIVSHLKVTLEQIYNGAMRKLAINKDVICANCEGHGGPKDAFVDCKLCNGQGIRV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 162 HIQQIGPgMVQQIQTVCIECKGQGERINPKDRCESCSGAKVIREKKIIEVHVEKG------------------------- 216
Cdd:PTZ00037 180 QIRQMGS-MIHQTQSTCNSCNGQGKIIPESKKCKNCSGKGVKKTRKILEVNIDKGvpnqhkitfhgeadekpneipgnvv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 217 ----------------------------------------------------EVIKHGDLRCVRDEGMPIYKAPLEKGIL 244
Cdd:PTZ00037 259 filnekphdtfkreggdlfitkkislyealtgfvfyithldgrkllvntppgEVVKPGDIKVINNEGMPTYKSPFKKGNL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 245 IIQFLVIFPEKHWLSLEKLPQLEALLPPRQKVRITDDMDQVEL---KEFCPNEQNWRQHREAYEEDEDGPQAG----VQC 317
Cdd:PTZ00037 339 YVTFEVIFPVDRKFTNEEKEILKSLFPQNPEEKKDLEDTEIEVvtaQNVDPEEVKDRDQKQQYQEDEDDEHHQegerVAC 418
|
|
| DnaJ_bact |
TIGR02349 |
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
7-221 |
3.69e-69 |
|
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: 219.39 E-value: 3.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGG-------- 76
Cdd:TIGR02349 2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEaeEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGggggggfn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 77 -SGSPSFSSPMDIFDMFFGGGGRMAR-----ERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGS-VE 149
Cdd:TIGR02349 82 gFDIGFFGDFGDIFGDFFGGGGGSGRrrrsgPRRGEDLRYDLELTFEEAVFGVEKEIEIPRKESCETCHGTGAKPGTdPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184352 150 KCPLCKGRGMQIHIQQIGPGMVQQIQTvCIECKGQGERInpKDRCESCSGAKVIREKKIIEVH----VEKGEVIKH 221
Cdd:TIGR02349 162 TCPTCGGTGQVRRQQGTPFGFFQQQQT-CPTCGGEGKII--KEPCSTCKGKGRVKERKTITVKipagVDTGQRLRV 234
|
|
| PRK10767 |
PRK10767 |
chaperone protein DnaJ; Provisional |
7-216 |
4.91e-60 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 196.13 E-value: 4.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG---EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFS 83
Cdd:PRK10767 6 YYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKeaeEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGGGFGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 84 SPM------DIFDMFFGG--GGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG-SVEKCPLC 154
Cdd:PRK10767 86 GGGfgdifgDIFGDIFGGgrGGGRQRARRGADLRYNMEITLEEAVRGVTKEIRIPTLVTCDTCHGSGAKPGtSPKTCPTC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184352 155 KGRGmQIHIQQiGPGMVQQiqtVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK10767 166 HGAG-QVRMQQ-GFFTVQQ---TCPTCHGRGKII--KDPCKKCHGQGRVEKEKTLSVKIPAG 220
|
|
| PRK14298 |
PRK14298 |
chaperone protein DnaJ; Provisional |
1-216 |
2.83e-59 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 194.30 E-value: 2.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 1 MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKN--PDEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAI-----K 73
Cdd:PRK14298 1 MATTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNkePDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIdnqysA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 74 EGGSGSPSFSSPMDIFDMFFGGGGRMARE--RRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEK- 150
Cdd:PRK14298 81 EDIFRGADFGGFGDIFEMFFGGGGRRGRMgpRRGSDLRYDLYITLEEAAFGVRKDIDVPRAERCSTCSGTGAKPGTSPKr 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184352 151 CPLCKGRGmQIHIQQIGPGMVQQIQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14298 161 CPTCGGTG-QVTTTRSTPLGQFVTTTTCSTCHGRGQVI--ESPCPVCSGTGKVRKTRKITVNVPAG 223
|
|
| PRK14289 |
PRK14289 |
molecular chaperone DnaJ; |
1-216 |
7.33e-57 |
|
molecular chaperone DnaJ;
Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 188.50 E-value: 7.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 1 MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNP---DEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGS 77
Cdd:PRK14289 1 MAEKRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgdkEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGGAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 78 GSPSFSSPM---DIFDMF----------------FGGGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKC 138
Cdd:PRK14289 81 GGGFSGEGMsmeDIFSMFgdifgghgggfggfggFGGGGSQQRVFRGSDLRVKVKLNLKEISTGVEKKFKVKKYVPCSHC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1913184352 139 EGVGGK-KGSVEKCPLCKGRGMQIHIQQIGPGMVQQiQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14289 161 HGTGAEgNNGSETCPTCKGSGSVTRVQNTILGTMQT-QSTCPTCNGEGKII--KKKCKKCGGEGIVYGEEVITVKIPAG 236
|
|
| PRK14278 |
PRK14278 |
chaperone protein DnaJ; Provisional |
5-216 |
6.30e-54 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 180.63 E-value: 6.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 5 TQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGG---EQAIKEGGSGS 79
Cdd:PRK14278 3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEaqEKFKEISVAYEVLSDPEKRRIVDLGGdplESAGGGGGGFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 80 PSFSSPMDIFDMFFGGG----GRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEK-CPLC 154
Cdd:PRK14278 83 GGFGGLGDVFEAFFGGGaasrGPRGRVRPGSDSLLRMRLDLEECATGVTKQVTVDTAVLCDRCHGKGTAGDSKPVtCDTC 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 155 KGRGmqiHIQQIGPGMVQQIQTV--CIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14278 163 GGRG---EVQTVQRSFLGQVMTSrpCPTCRGVGEVI--PDPCHECAGDGRVRARREITVKIPAG 221
|
|
| PRK14280 |
PRK14280 |
molecular chaperone DnaJ; |
7-216 |
6.79e-51 |
|
molecular chaperone DnaJ;
Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 172.60 E-value: 6.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFSS 84
Cdd:PRK14280 6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGadEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGFGGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 85 PM-------DIFDMFFGGGGRMARE---RRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG-SVEKCPL 153
Cdd:PRK14280 86 DFgggfgfeDIFSSFFGGGGRRRDPnapRQGADLQYTMTLTFEEAVFGKEKEIEIPKEETCDTCHGSGAKPGtSKETCSH 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 154 CKGRGmQIHIQQIGP-GMVQQiQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14280 166 CGGSG-QVSVEQNTPfGRVVN-RQTCPHCNGTGQEI--KEKCPTCHGKGKVRKRKKINVKIPAG 225
|
|
| PRK14276 |
PRK14276 |
chaperone protein DnaJ; Provisional |
4-216 |
1.08e-50 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 172.19 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 4 ETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQ----------GGEQA 71
Cdd:PRK14276 3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKEVQEAYETLSDPQKRAAYDQygaaganggfGGGAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 72 IKEGGSGSPSFSSPMDIFDMFFGGGGRMAR---ERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG-S 147
Cdd:PRK14276 83 GFGGFDGSGGFGGFEDIFSSFFGGGGARRNpnaPRQGDDLQYRVNLDFEEAIFGKEKEVSYNREATCHTCNGSGAKPGtS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 148 VEKCPLCKGRGMqIHIQQIGP-GMVQQiQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14276 163 PVTCGKCHGSGV-ITVDTQTPlGMMRR-QVTCDVCHGTGKEI--KEPCQTCHGTGHEKQAHTVSVKIPAG 228
|
|
| PRK14283 |
PRK14283 |
chaperone protein DnaJ; Provisional |
1-231 |
1.20e-50 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 171.93 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 1 MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGE--------- 69
Cdd:PRK14283 1 MAEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGaeEKFKEISEAYAVLSDDEKRQRYDQFGHagmdgfsqe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 70 ---QAIKEGGSGSPSFSSPMDIFDMFFGGGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG 146
Cdd:PRK14283 81 difNNINFEDIFQGFGFGIGNIFDMFGFGGGSRHGPQRGADIYTEVEITLEEAASGVEKDIKVRHTKKCPVCNGSRAEPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 147 S-VEKCPLCKGRGMQIHIQQIGPGMVQQIQTvCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKGevIKHGDLR 225
Cdd:PRK14283 161 SeVKTCPTCGGTGQVKQVRNTILGQMMNVTT-CPDCQGEGKIV--EKPCSNCHGKGVVRETKTISVKIPAG--VETGSRL 235
|
....*.
gi 1913184352 226 CVRDEG 231
Cdd:PRK14283 236 RVSGEG 241
|
|
| PRK14297 |
PRK14297 |
molecular chaperone DnaJ; |
7-216 |
1.06e-49 |
|
molecular chaperone DnaJ;
Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 169.58 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG---EKFKLISQAYEVLSDPKKRDVYDQ---------GGEQAIKE 74
Cdd:PRK14297 6 YYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKeaeEKFKEINEAYQVLSDPQKKAQYDQfgtadfngaGGFGSGGF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 75 GGSGSPSFSSPMDIFDMFFGGGGRMARERR-----GKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVE 149
Cdd:PRK14297 86 GGFDFSDMGGFGDIFDSFFGGGFGSSSRRRngpqrGADIEYTINLTFEEAVFGVEKEISVTRNENCETCNGTGAKPGTSP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 150 K-CPLCKGRGmQIHIQQIGPGMVQQIQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14297 166 KtCDKCGGTG-QIRVQRNTPLGSFVSTTTCDKCGGSGKVI--EDPCNKCHGKGKVRKNRKIKVNVPAG 230
|
|
| PRK14294 |
PRK14294 |
chaperone protein DnaJ; Provisional |
7-216 |
1.65e-48 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 166.09 E-value: 1.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNP---DEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFS 83
Cdd:PRK14294 6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPgdkEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTGFSGFSGF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 84 SPM-----DIFDMFFG-GGGRMARE----RRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGS-VEKCP 152
Cdd:PRK14294 86 DDIfssfgDIFEDFFGfGGGRRGRSrtavRAGADLRYDLTLPFLEAAFGTEKEIRIQKLETCEECHGSGCEPGTsPTTCP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 153 LCKGRGMQIHIQqigpGMVqQIQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14294 166 QCGGSGQVTQSQ----GFF-SIRTTCPRCRGMGKVI--VSPCKTCHGQGRVRVSKTVQVKIPAG 222
|
|
| PRK14291 |
PRK14291 |
chaperone protein DnaJ; Provisional |
7-216 |
8.18e-47 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 162.25 E-value: 8.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFSS 84
Cdd:PRK14291 5 YYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEaeEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQGQEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 85 PMDIFDM--------------FFGGGGRMA--RERR--------GKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEG 140
Cdd:PRK14291 85 FSDFGGGniediledvfdifgFGDIFGRRRatRERRktyqrpvkGEDIYQTVEISLEEAYTGTTVSLEVPRYVPCEACGG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1913184352 141 VGGKKGSVEK-CPLCKGRGmqiHIQQigPGMVQQIQTVCIECKGQGERINPkdrCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14291 165 TGYDPGSGEKvCPTCGGSG---EIYQ--RGGFFRISQTCPTCGGEGVLREP---CSKCNGRGLVIKKETIKVRIPPG 233
|
|
| PRK14281 |
PRK14281 |
chaperone protein DnaJ; Provisional |
7-231 |
8.76e-47 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 162.28 E-value: 8.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG---EKFKLISQAYEVLSDPKKRDVYDQ------GGEQAIKEGGS 77
Cdd:PRK14281 5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKeaeEHFKEVNEAYEVLSNDDKRRRYDQfghagvGSSAASGGGPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 78 GSPSFSSPMDIF----DMF-----------------FGGGGRMARER---RGKNVVHQLSVTLEDLYNGVTKKLALQKNV 133
Cdd:PRK14281 85 YGGGGGDFNDIFsafnDMFgggarrgggspfgfedvFGGGGRRRRASagiPGTDLKIRLKLTLEEIAKGVEKTLKIKKQV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 134 ICEKCEGVGGKKGSVEKCPLCKGRGmqiHIQQIGPGMVQQIQ--TVCIECKGQGERInpKDRCESCSGAKVIREKKIIEV 211
Cdd:PRK14281 165 PCKECNGTGSKTGATETCPTCHGSG---EVRQASKTMFGQFVniTACPTCGGEGRVV--KDRCPACYGEGIKQGEVTVKV 239
|
250 260
....*....|....*....|
gi 1913184352 212 HVEKGevIKHGDLRCVRDEG 231
Cdd:PRK14281 240 TVPAG--VQDGNYLTLRGQG 257
|
|
| PRK14277 |
PRK14277 |
chaperone protein DnaJ; Provisional |
1-233 |
2.31e-46 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 161.12 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 1 MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGE---KFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGS 77
Cdd:PRK14277 1 MAAKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEaeqKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 78 GSPSFSSP------------------MDIFDMFFGGGGRMARE--RRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEK 137
Cdd:PRK14277 81 GQGGFGQGgfggggfdfdfggfgdifEDIFGDFFGTGRRRAETgpQKGADIRYDLELTFEEAAFGTEKEIEVERFEKCDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 138 CEGVGGKKGS-VEKCPLCKGRGmQIHIQQIGP-GMVQQIQTvCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEK 215
Cdd:PRK14277 161 CKGSGAKPGSkPVTCPVCHGTG-QVRTRQNTPfGRIVNIRT-CDRCHGEGKII--TDPCNKCGGTGRIRRRRKIKVNIPA 236
|
250
....*....|....*...
gi 1913184352 216 GevIKHGDLRCVRDEGMP 233
Cdd:PRK14277 237 G--IDDGQMITLRGEGEP 252
|
|
| PRK14290 |
PRK14290 |
chaperone protein DnaJ; Provisional |
1-216 |
6.53e-43 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 151.24 E-value: 6.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 1 MVKEtqYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG----EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGG 76
Cdd:PRK14290 1 MAKD--YYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKaeaeEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 77 SGS-----PSFSSPMDIFDMFFGG----------GGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGV 141
Cdd:PRK14290 79 SNFnwdnfTHFSDINDIFNQIFGGnfgsdffsgfGNQQSTRNIDLDIYTNLDISLEDAYYGTEKRIKYRRNAMCPDCSGT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184352 142 GGKKGSVEKCPLCKGRGMQIHIQqiGPGMVQQIQ-TVCIECKGQGeRInPKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14290 159 GAKNGKLITCPTCHGTGQQRIVR--GQGFFRMVTvTTCRTCGGRG-RI-PEEKCPRCNGTGTVVVNEDISVKIPKG 230
|
|
| PRK14286 |
PRK14286 |
chaperone protein DnaJ; Provisional |
2-231 |
2.63e-42 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 150.14 E-value: 2.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 2 VKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKN---PDEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSG 78
Cdd:PRK14286 1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNkgnKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 79 SPSFSSP---------MDIFDMFFG-------GGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVG 142
Cdd:PRK14286 81 FGQGAYTdfsdifgdfGDIFGDFFGggrgggsGGGRRSGPQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCVDCNGSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 143 GKKGSVEK-CPLCKGRGmQIHIQQigpGMVqQIQTVCIECKGQGERI-NPkdrCESCSGAKVIREKKIIEVHVEKGevIK 220
Cdd:PRK14286 161 ASKGSSPTtCPDCGGSG-QIRRTQ---GFF-SVATTCPTCRGKGTVIsNP---CKTCGGQGLQEKRRTINIKIPPG--VE 230
|
250
....*....|.
gi 1913184352 221 HGDLRCVRDEG 231
Cdd:PRK14286 231 TGSRLKVSGEG 241
|
|
| PRK14301 |
PRK14301 |
chaperone protein DnaJ; Provisional |
7-233 |
4.27e-42 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 149.51 E-value: 4.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGE---KFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFS 83
Cdd:PRK14301 6 YYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEaeqKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGNGGFGGFSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 84 SP------MDIFDMFFG----GGGRMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG-SVEKCP 152
Cdd:PRK14301 86 AEdifshfSDIFGDLFGfsggGSRRGPRPQAGSDLRYNLTVSFRQAAKGDEVTLRIPKNVTCDDCGGSGAAPGtSPETCR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 153 LCKGRGmQIHIQQigpGMVqQIQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKGevIKHGDLRCVRDEGM 232
Cdd:PRK14301 166 HCGGSG-QVRQSQ---GFF-QIAVPCPVCRGEGRVI--THPCPKCKGSGIVQQTRELKVRIPAG--VDTGSRLRLRGEGE 236
|
.
gi 1913184352 233 P 233
Cdd:PRK14301 237 P 237
|
|
| PRK14284 |
PRK14284 |
chaperone protein DnaJ; Provisional |
5-216 |
3.59e-41 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 147.30 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 5 TQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGE---KFKLISQAYEVLSDPKKRDVYDQGGEQA-IKEGGSGSP 80
Cdd:PRK14284 1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEaekRFKEVSEAYEVLSDAQKRESYDRYGKDGpFAGAGGFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 81 SFSSPMD-------------------IFDMFFGG---------GGRMARERRGKNVvhQLSVTLEDLYNGVTKKLALQKN 132
Cdd:PRK14284 81 AGMGNMEdalrtfmgafggefggggsFFEGLFGGlgeafgmrgGPAGARQGASKKV--HITLSFEEAAKGVEKELLVSGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 133 VICEKCEGVGG-KKGSVEKCPLCKGRGmQIhIQQIGpgmVQQIQTVCIECKGQGERINpkDRCESCSGAKVIREKKIIEV 211
Cdd:PRK14284 159 KSCDACSGSGAnSSQGIKVCDRCKGSG-QV-VQSRG---FFSMASTCPECGGEGRVIT--DPCSVCRGQGRIKDKRSVHV 231
|
....*
gi 1913184352 212 HVEKG 216
Cdd:PRK14284 232 HIPAG 236
|
|
| PRK14295 |
PRK14295 |
molecular chaperone DnaJ; |
4-216 |
1.20e-40 |
|
molecular chaperone DnaJ;
Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 146.15 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 4 ETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKN---PDEGEKFKLISQAYEVLSDPKKRDVYD--------------- 65
Cdd:PRK14295 8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANkgdAKAEERFKEISEAYDVLSDEKKRKEYDearslfgnggfrpgp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 66 --------------------QGGEQAikeggsgsPSFSSPMDIFDMFFGGGGRMARERRGKNVVHQLSVTLEDLYNGVTK 125
Cdd:PRK14295 88 gggggggfnfdlgdlfgggaQGGGGA--------GGGGGLGDVFGGLFNRGGRRTQPRRGADVESEVTLSFTEAIDGATV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 126 KLALQKNVICEKCEGVGGKKGSVEK-CPLCKGRGmqiHIQQIGPGMvqQIQTVCIECKGQGerINPKDRCESCSGAKVIR 204
Cdd:PRK14295 160 PLRLTSQAPCPACSGTGAKNGTTPRvCPTCSGTG---QVSRNSGGF--SLSEPCPDCKGRG--LIADDPCLVCKGSGRAK 232
|
250
....*....|..
gi 1913184352 205 EKKIIEVHVEKG 216
Cdd:PRK14295 233 SSRTMQVRIPAG 244
|
|
| PRK14293 |
PRK14293 |
molecular chaperone DnaJ; |
7-216 |
1.25e-40 |
|
molecular chaperone DnaJ;
Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 145.52 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGEQAIkeGGSGSPSFSS 84
Cdd:PRK14293 5 YYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGaeDRFKEINRAYEVLSDPETRARYDQFGEAGV--SGAAGFPDMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 85 PM----DIFDMFF------GGGGRMARER---RGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGS-VEK 150
Cdd:PRK14293 83 DMggfaDIFETFFsgfggaGGQGGRRRRRgpqRGDDLRYDLKLDFREAIFGGEKEIRIPHLETCETCRGSGAKPGTgPTT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1913184352 151 CPLCKGRGmQIHIQQIGP-GMVQQIqTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14293 163 CSTCGGAG-QVRRATRTPfGSFTQV-SECPTCNGTGQVI--EDPCDACGGQGVKQVTKKLKINIPAG 225
|
|
| PRK14287 |
PRK14287 |
chaperone protein DnaJ; Provisional |
7-222 |
5.80e-39 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 141.30 E-value: 5.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPD--KNPDEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKE--GGSGSPSF 82
Cdd:PRK14287 6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDvnKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQgfGGGGAGDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 83 SSPMDIFDMFFGGGGRMAR---ERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSV-EKCPLCKGRG 158
Cdd:PRK14287 86 GGFSDIFDMFFGGGGGRRNpnaPRQGADLQYTMTLEFKEAVFGKETEIEIPREETCGTCHGSGAKPGTKpETCSHCGGSG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 159 mQIHIQQIGPGMVQQIQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKGevIKHG 222
Cdd:PRK14287 166 -QLNVEQNTPFGRVVNRRVCHHCEGTGKII--KQKCATCGGKGKVRKRKKINVKVPAG--IDHG 224
|
|
| PRK14285 |
PRK14285 |
chaperone protein DnaJ; Provisional |
7-216 |
1.05e-37 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 137.82 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEGEK---FKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFS 83
Cdd:PRK14285 5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAesiFKEATEAYEVLIDDNKRAQYDRFGHTAFEGGGGFEGFSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 84 SPM----------DIFDMFFGGGGRMARER---RGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG-SVE 149
Cdd:PRK14285 85 GFSgfsdifedfgDIFDSFFTGNRGQDKNRkheKGQDLTYQIEISLEDAYLGYKNNINITRNMLCESCLGKKSEKGtSPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 150 KCPLCKGRGMQIHiqqiGPGMVqQIQTVCIECKGQGERI-NPkdrCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14285 165 ICNMCNGSGRVMQ----GGGFF-RVTTTCPKCYGNGKIIsNP---CKSCKGKGSLKKKETIELKIPAG 224
|
|
| PRK14292 |
PRK14292 |
chaperone protein DnaJ; Provisional |
7-216 |
1.82e-37 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 136.94 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGEQ---AIKEGGSGSPS 81
Cdd:PRK14292 4 YYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGaaEKFAQINEAYAVLSDAEKRAHYDRFGTApgaGMPGGDPFGGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 82 FSSPMDIFDMFFGGGGRMA-----RERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGS--VEKCPLC 154
Cdd:PRK14292 84 GFDPMDIFEQLFGGAGFGGgrgrrGPARGDDLETEARITLEQARAGEEVEVEVDRLTECEHCHGSRTEPGGkpPKTCPTC 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184352 155 KGRGmQIHIQQIGPGMVQQIQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14292 164 RGAG-AVRAQARTIFGVVETQQPCPTCRGEGQII--TDPCTVCRGRGRTLKAETVKVKLPRG 222
|
|
| PRK14279 |
PRK14279 |
molecular chaperone DnaJ; |
4-216 |
3.37e-37 |
|
molecular chaperone DnaJ;
Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 136.79 E-value: 3.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 4 ETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDE---GEKFKLISQAYEVLSDPKKRDVYDQ-------GGEQAIK 73
Cdd:PRK14279 8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDpaaEERFKAVSEAHDVLSDPAKRKEYDEtrrlfagGGFGGRR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 74 EGGSG------SPSFSSPMDIFDMFFGGGG---------------------RMARERRGKNVVHQLSVTLEDLYNGVTKK 126
Cdd:PRK14279 88 FDGGGgfggfgTGGDGAEFNLNDLFDAAGRgggggigdlfgglfnrgggsaRPSRPRRGNDLETETTLDFVEAAKGVTMP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 127 LALQKNVICEKCEGVGGKKG-SVEKCPLCKGRGMqIHIQQIGPGMVQQiqtvCIECKGQGERINpkDRCESCSGAKVIRE 205
Cdd:PRK14279 168 LRLTSPAPCTTCHGSGARPGtSPKVCPTCNGSGV-ISRNQGAFGFSEP----CTDCRGTGSIIE--DPCEECKGTGVTTR 240
|
250
....*....|.
gi 1913184352 206 KKIIEVHVEKG 216
Cdd:PRK14279 241 TRTINVRIPPG 251
|
|
| PRK14296 |
PRK14296 |
chaperone protein DnaJ; Provisional |
2-216 |
4.11e-36 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 133.53 E-value: 4.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 2 VKETQYYDILGVKPSASPEEIKKAYRKLALKYHPD--KNPDEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIK------ 73
Cdd:PRK14296 1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDlnKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDgssgfs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 74 ------EGGSGSPSFSSPMDIFDMF--FGGGGRMARER--RGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGG 143
Cdd:PRK14296 81 snfgdfEDLFSNMGSSGFSSFTNIFsdFFGSNKSDYQRstKGQSVSLDIYLTFKELLFGVDKIIELDLLTNCSKCFGSGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 144 KKGS-VEKCPLCKGRGMQIHIQQIGPGMVQQiQTVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14296 161 ESNSdIHICNNCHGTGEVLVQKNMGFFQFQQ-SAKCNVCNGAGKII--KNKCKNCKGKGKYLERKKIEVNIPKG 231
|
|
| DnaJ |
COG0484 |
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
7-74 |
1.88e-35 |
|
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: 125.20 E-value: 1.88e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG---EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKE 74
Cdd:COG0484 2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPeaeEKFKEINEAYEVLSDPEKRAAYDRFGHAAELL 72
|
|
| PRK14282 |
PRK14282 |
chaperone protein DnaJ; Provisional |
7-220 |
3.69e-35 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 131.07 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG----EKFKLISQAYEVLSDPKKRDVYDQG---GEQAIKEGGSGS 79
Cdd:PRK14282 6 YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRkeaeQKFKEIQEAYEVLSDPQKRAMYDRFgyvGEQPPYQETESG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 80 PSFSSPM----------DIFDMFFGGGG----RMARERRGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKK 145
Cdd:PRK14282 86 GGFFEDIfkdfenifnrDIFDIFFGERRtqeeQREYARRGEDIRYEIEVTLSDLINGAEIPVEYDRYETCPHCGGTGVEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 146 GS-VEKCPLCKGRGMqIHIQQIGPGMVQQIQTVCIECKGQGeRInPKDRCESCSGAKVIREKKIIEVH----VEKGEVIK 220
Cdd:PRK14282 166 GSgYVTCPKCHGTGR-IREERRSFFGVFVSERTCERCGGTG-KI-PGEYCHECGGSGRIRRRVRTTVKipagVEDGTVLR 242
|
|
| PRK14300 |
PRK14300 |
chaperone protein DnaJ; Provisional |
7-221 |
3.64e-34 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 128.21 E-value: 3.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNP--DEGEKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSPSFSS 84
Cdd:PRK14300 5 YYQILGVSKTASQADLKKAYLKLAKQYHPDTTDakDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQSRGGGGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 85 P------MDIFDMFFG---GGGRMARER----RGKNVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKG-SVEK 150
Cdd:PRK14300 85 GgfhpdiNDIFGDFFSdfmGGSRRSRPTsskvRGSDLKYNLTINLEEAFHGIEKNISFSSEVKCDTCHGSGSEKGeTVTT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1913184352 151 CPLCKGRGMQiHIQQiGPGMVQQiqtVCIECKGQGERInpKDRCESCSGAKVIREKKIIEVH----VEKGEVIKH 221
Cdd:PRK14300 165 CDACSGVGAT-RMQQ-GFFTIEQ---ACHKCQGNGQII--KNPCKKCHGMGRYHKQRNLSVNipagVENGTRIRH 232
|
|
| DnaJ |
pfam00226 |
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
7-65 |
7.07e-34 |
|
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: 118.73 E-value: 7.07e-34
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDE---GEKFKLISQAYEVLSDPKKRDVYD 65
Cdd:pfam00226 2 YYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVLSDPEKRAIYD 63
|
|
| DnaJ_C |
pfam01556 |
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
108-250 |
2.82e-29 |
|
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region.
Pssm-ID: 460251 [Multi-domain] Cd Length: 213 Bit Score: 111.19 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 108 VVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEKCPLCKGRGMQIHIQqigpgmvQQIQTVCIECKGQGER 187
Cdd:pfam01556 1 LEYELELTLEEAYFGCTKKIKITRNVICDTCGGSGAKPGTSPKTCPCCGGGGQVRRQ-------FGFFSTCTCCPCCGGG 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 188 INPKDRCESCSGAKVIREKKIIEVHVEKGevIKHGD-LRcVRDEGMPIYKaPLEKGILIIQFLV 250
Cdd:pfam01556 74 GKIIDKCCKCCGGGGVVEKKTLEVKIPAG--VDDGQrIR-LRGEGDAGEN-GGPPGDLYVVIRV 133
|
|
| PRK14288 |
PRK14288 |
molecular chaperone DnaJ; |
4-216 |
1.01e-28 |
|
molecular chaperone DnaJ;
Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 113.63 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 4 ETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG---EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGSGSP 80
Cdd:PRK14288 2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeaeEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 81 SFSSPMD----IFDMFFGGGGRMARERRGK---NVVHQLSVTLEDLYNGVTKKLALQKNVICEKCEGVGGKKGSVEKCPL 153
Cdd:PRK14288 82 DFSDFFEdlgsFFEDAFGFGARGSKRQKSSiapDYLQTIELSFKEAVFGCKKTIKVQYQSVCESCDGTGAKDKALETCKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1913184352 154 CKGRGmQIHIQQigpGMVQQIQTvCIECKGQGERInpKDRCESCSGAKVIREKKIIEVHVEKG 216
Cdd:PRK14288 162 CNGQG-QVFMRQ---GFMSFAQT-CGACQGKGKII--KTPCQACKGKTYILKDEEIDAIIPEG 217
|
|
| DnaJ |
smart00271 |
DnaJ molecular chaperone homology domain; |
5-60 |
1.41e-26 |
|
DnaJ molecular chaperone homology domain;
Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 99.23 E-value: 1.41e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 5 TQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDE----GEKFKLISQAYEVLSDPKK 60
Cdd:smart00271 1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeeaEEKFKEINEAYEVLSDPEK 60
|
|
| DnaJ |
cd06257 |
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
7-57 |
2.24e-26 |
|
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: 98.77 E-value: 2.24e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDE---GEKFKLISQAYEVLSD 57
Cdd:cd06257 2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpeaEEKFKEINEAYEVLSD 55
|
|
| SEC63 |
COG5407 |
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
7-61 |
3.97e-25 |
|
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 95.45 E-value: 3.97e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG---EKFKLISQAYEVLSDPKKR 61
Cdd:COG5407 2 PYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPkaeERFKEINEAYELLSDAEKR 59
|
|
| CbpA |
COG2214 |
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
1-71 |
1.46e-24 |
|
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 95.17 E-value: 1.46e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1913184352 1 MVKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG----EKFKLISQAYEVLSDPKKRDVYDQGGEQA 71
Cdd:COG2214 1 MPDLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalaeELFQRLNEAYEVLSDPERRAEYDRELGQS 75
|
|
| PRK14299 |
PRK14299 |
chaperone protein DnaJ; Provisional |
7-129 |
5.26e-23 |
|
chaperone protein DnaJ; Provisional
Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 96.55 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDKNPDEG--EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKEGGS------- 77
Cdd:PRK14299 6 YYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGaeEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQgpppgpp 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 78 -----GSPSFSSPMDIFDMFFGGGGRMA-----------RERRGKNVVHQLSVTLEDLYNGVTKKLAL 129
Cdd:PRK14299 86 gggdfSGFNVGDFSDFFQQLFGGRGGFGgfgdlfgsvgrRARKGRDLEAELPLTLEEAYRGGEKVVEV 153
|
|
| PRK10266 |
PRK10266 |
curved DNA-binding protein; |
7-118 |
7.19e-23 |
|
curved DNA-binding protein;
Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 96.43 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPD--KNPDEGEKFKLISQAYEVLSDPKKRDVYDQ--------GGEQAIKEGG 76
Cdd:PRK10266 6 YYAIMGVKPTDDLKTIKTAYRRLARKYHPDvsKEPDAEARFKEVAEAWEVLSDEQRRAEYDQlwqhrndpQFNRQFQHGD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1913184352 77 SGSPSFSSPMDIFDMFFGGGGRMARER---RGKNVVHQLSVTLED 118
Cdd:PRK10266 86 GQSFNAEDFDDIFSSIFGQHARQSRQRpaaRGHDIEIEVAVFLEE 130
|
|
| DnaJ_CXXCXGXG |
pfam00684 |
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ... |
135-201 |
5.68e-20 |
|
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.
Pssm-ID: 459904 [Multi-domain] Cd Length: 65 Bit Score: 81.84 E-value: 5.68e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 135 CEKCEGVGGKKG-SVEKCPLCKGRGMQIHIQQIGPGMVQQiQTVCIECKGQGERInpKDRCESCSGAK 201
Cdd:pfam00684 1 CPTCNGSGAKPGtKPTTCPTCGGTGQVRRVQQTGPGFFQM-QSTCPTCGGTGKII--KDPCKKCKGKG 65
|
|
| DnaJ_zf |
cd10719 |
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ... |
135-201 |
2.32e-18 |
|
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ 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 chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.
Pssm-ID: 199908 [Multi-domain] Cd Length: 65 Bit Score: 77.68 E-value: 2.32e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 135 CEKCEGVGGKKGS-VEKCPLCKGRGMQIHIQQIGpGMVQQIQTVCIECKGQGERInpKDRCESCSGAK 201
Cdd:cd10719 1 CPTCNGSGAKPGTkPKTCPTCGGSGQVRQVQGTG-FGFFQTQTTCPTCGGTGKII--KDPCPKCKGKG 65
|
|
| DjlA |
COG1076 |
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
7-63 |
2.23e-14 |
|
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 67.13 E-value: 2.23e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184352 7 YYDILGVKPSASPEEIKKAYRKLALKYHPDK----NPDE-----GEKFKLISQAYEVLSDPKKRDV 63
Cdd:COG1076 6 AFELLGLPPDADDAELKRAYRKLQREHHPDRlaagLPEEeqrlaLQKAAAINEAYETLKDPRGIDL 71
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
2-74 |
1.53e-11 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 65.19 E-value: 1.53e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1913184352 2 VKETQYYDILGVKPSASPEEIKKAYRKLALKYHPDK-NPDEG-EKFKLISQAYEVLSDPKKRDVYDQGGEQAIKE 74
Cdd:PTZ00341 570 IPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKrSGNEGfHKFKKINEAYQILGDIDKKKMYNKFGYDGIKG 644
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
3-65 |
6.12e-10 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 59.66 E-value: 6.12e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1913184352 3 KETQYYDILGV---KPSASPEEIKKAYRKLALKYHPDKNPDEGEK-----FKLISQAYEVLSDPKKRDVYD 65
Cdd:COG5269 41 KKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKgcdefFKLIQKAREVLGDRKLRLQYD 111
|
|
| djlA |
PRK09430 |
co-chaperone DjlA; |
8-55 |
2.37e-08 |
|
co-chaperone DjlA;
Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 54.05 E-value: 2.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1913184352 8 YDILGVKPSASPEEIKKAYRKLALKYHPDK-----NPDE-----GEKFKLISQAYEVL 55
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakgLPPEmmemaKEKAQEIQAAYELI 260
|
|
| DnaJ_C |
cd10747 |
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
106-255 |
2.69e-07 |
|
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70.
Pssm-ID: 199909 [Multi-domain] Cd Length: 158 Bit Score: 49.35 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 106 KNVVHQLSVTLEDLYNGVTKKLALQKNVICEKcegvggkkgsvekcplcKGRGMQIHIQqigPGmVQQIQTVCIEckGQG 185
Cdd:cd10747 1 ADLRYDLELTLEEAYFGKEKEIKIPRKVTRVR-----------------EKKTLTVKIP---AG-VDDGQRLRLR--GEG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913184352 186 E---------------RINPKDRCEScSGAKVIREKKI----------IEVHVEKGEV-------IKHGDLRCVRDEGMP 233
Cdd:cd10747 58 DagpnggppgdlyvviRVKPHPVFRR-DGNDLYCEVPIslteallggeIEVPTLGGKVklkippgTQPGTVLRLKGKGMP 136
|
170 180
....*....|....*....|..
gi 1913184352 234 IYKaPLEKGILIIQFLVIFPEK 255
Cdd:cd10747 137 RLR-GGGRGDLYVEVKVEFPKK 157
|
|
| PHA03102 |
PHA03102 |
Small T antigen; Reviewed |
9-70 |
5.72e-05 |
|
Small T antigen; Reviewed
Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 42.74 E-value: 5.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913184352 9 DILGVKPSA--SPEEIKKAYRKLALKYHPDKNPDEgEKFKLISQAYEVLSDPKKRDVYDQGGEQ 70
Cdd:PHA03102 9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKGGDE-EKMKELNTLYKKFRESVKSLRDLDGEED 71
|
|
| PHA02624 |
PHA02624 |
large T antigen; Provisional |
9-61 |
1.84e-04 |
|
large T antigen; Provisional
Pssm-ID: 222912 [Multi-domain] Cd Length: 647 Bit Score: 43.05 E-value: 1.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1913184352 9 DILGVKPSA--SPEEIKKAYRKLALKYHPDKNPDEgEKFKLISQAYEVLSDPKKR 61
Cdd:PHA02624 15 DLLGLPMAAwgNLPLMRKAYLRKCKEYHPDKGGDE-EKMKRLNSLYKKLQEGVKS 68
|
|
| PTZ00100 |
PTZ00100 |
DnaJ chaperone protein; Provisional |
5-36 |
6.60e-04 |
|
DnaJ chaperone protein; Provisional
Pssm-ID: 240265 Cd Length: 116 Bit Score: 38.68 E-value: 6.60e-04
10 20 30
....*....|....*....|....*....|..
gi 1913184352 5 TQYYDILGVKPSASPEEIKKAYRKLALKYHPD 36
Cdd:PTZ00100 65 SEAYKILNISPTASKERIREAHKQLMLRNHPD 96
|
|
| hscB |
PRK01356 |
co-chaperone HscB; Provisional |
7-64 |
1.32e-03 |
|
co-chaperone HscB; Provisional
Pssm-ID: 167217 [Multi-domain] Cd Length: 166 Bit Score: 38.70 E-value: 1.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1913184352 7 YYDILGVKP--SASPEEIKKAYRKLALKYHPD--KNPDEGEKFKLIS----QAYEVLSDPKKRDVY 64
Cdd:PRK01356 4 YFQLLGLPQeyNIDLKILEKQYFAMQVKYHPDkaKTLQEKEQNLIIAselnNAYSTLKDALKRAEY 69
|
|
|