|
Name |
Accession |
Description |
Interval |
E-value |
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
139-271 |
1.62e-49 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 161.28 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 139 AKVNSVERVHARHILV---------DTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAA 208
Cdd:COG0760 1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDpGSAANGGDLGWFSRGQLVPEFEEAA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841979023 209 FALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQKVQEKVAELRKSADV 271
Cdd:COG0760 81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
125-279 |
7.51e-33 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 123.67 E-value: 7.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 125 VNEEDVRKLYDQEAAK-VNSVERVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADE--M 200
Cdd:PRK00059 174 VTDKDAQKYYNENKSKfTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDpGSKDKGGDLGDVPYSDsgY 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 201 VPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQK----VQEKVAELRKSADVEMVDP 276
Cdd:PRK00059 254 DKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKqsevFKKKIEEWKKALKVKKYEK 333
|
...
gi 1841979023 277 DLQ 279
Cdd:PRK00059 334 NLL 336
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
131-235 |
1.12e-28 |
|
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.
Pssm-ID: 404499 [Multi-domain] Cd Length: 116 Bit Score: 106.30 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 131 RKLYDQEAAKVNsverVHARHILVD-------TEEQAR----DALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSAD 198
Cdd:pfam13616 4 SKLVDKKSAPDS----VKASHILISysqavsrTEEEAKakadSLLAALKNGADFAALAKTYSDDpASKNNGGDLGWFTKG 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1841979023 199 EMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERK 235
Cdd:pfam13616 80 QMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
139-271 |
1.62e-49 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 161.28 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 139 AKVNSVERVHARHILV---------DTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAA 208
Cdd:COG0760 1 DQFDSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDpGSAANGGDLGWFSRGQLVPEFEEAA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841979023 209 FALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQKVQEKVAELRKSADV 271
Cdd:COG0760 81 FALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
125-279 |
7.51e-33 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 123.67 E-value: 7.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 125 VNEEDVRKLYDQEAAK-VNSVERVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADE--M 200
Cdd:PRK00059 174 VTDKDAQKYYNENKSKfTEKPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDpGSKDKGGDLGDVPYSDsgY 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 201 VPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQK----VQEKVAELRKSADVEMVDP 276
Cdd:PRK00059 254 DKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKqsevFKKKIEEWKKALKVKKYEK 333
|
...
gi 1841979023 277 DLQ 279
Cdd:PRK00059 334 NLL 336
|
|
| prsA |
PRK03002 |
peptidylprolyl isomerase PrsA; |
118-279 |
3.82e-31 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 101162 [Multi-domain] Cd Length: 285 Bit Score: 118.11 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 118 HEKIQPTVNEEDVRKLYDQEaakvnsverVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFS 196
Cdd:PRK03002 117 NEAIKKSVTEKDVKDHYKPE---------IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDlLSKEKGGDLGYFN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 197 ADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvgGAEPFDKVKNGLRMIVLRQKVQEKV-------AELRKsA 269
Cdd:PRK03002 188 SGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTDKK--DLKPYDEVKDSIRKNLEEERTADPIfgkkllqSELKK-A 264
|
170
....*....|
gi 1841979023 270 DVEMVDPDLQ 279
Cdd:PRK03002 265 NIKINDSELE 274
|
|
| prsA |
PRK02998 |
peptidylprolyl isomerase; Reviewed |
117-279 |
5.41e-29 |
|
peptidylprolyl isomerase; Reviewed
Pssm-ID: 179522 [Multi-domain] Cd Length: 283 Bit Score: 112.37 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 117 FHEKIQPTVNEEDVRKLYDQEaakvnsverVHARHILVDTEEQARDALAKIEAGANFADLAKQISKD-GSAQYGGDLGFF 195
Cdd:PRK02998 114 FEKAIKATVTEKDVKDNYKPE---------MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDtGSKEQGGEISGF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 196 SADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvgGAEPFDKVKNGLRMIVLRQKVQEK--------VAELRK 267
Cdd:PRK02998 185 APGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK--ELKPFDEVKDSIRKDLEQQRLQDTtgkwkqqvVNDLLK 262
|
170
....*....|..
gi 1841979023 268 SADVEMVDPDLQ 279
Cdd:PRK02998 263 DADIKVNDKEFK 274
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
131-235 |
1.12e-28 |
|
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.
Pssm-ID: 404499 [Multi-domain] Cd Length: 116 Bit Score: 106.30 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 131 RKLYDQEAAKVNsverVHARHILVD-------TEEQAR----DALAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSAD 198
Cdd:pfam13616 4 SKLVDKKSAPDS----VKASHILISysqavsrTEEEAKakadSLLAALKNGADFAALAKTYSDDpASKNNGGDLGWFTKG 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1841979023 199 EMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERK 235
Cdd:pfam13616 80 QMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
|
|
| prsA |
PRK03095 |
peptidylprolyl isomerase PrsA; |
84-281 |
3.12e-28 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 179537 [Multi-domain] Cd Length: 287 Bit Score: 110.08 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 84 LMAQEAVKEaiaETNEYKKRLAFYQAKAlrdayfhekIQPTVNEEDVRKLYDQEaakvnsverVHARHILVDTEEQARDA 163
Cdd:PRK03095 91 LLKQQGIKE---ETLKTGVRAQLAQEKA---------IEKTITDKELKDNYKPE---------IKASHILVKDEATAKKV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 164 LAKIEAGANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvGGAEPF 242
Cdd:PRK03095 150 KEELGQGKSFEELAKQYSEDtGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIK-EPEKSF 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1841979023 243 DKVKNGLRMIVLRQKVQE-------KVAELRKsADVEMVDPDLQRL 281
Cdd:PRK03095 229 EQSKADIKKELVQKKAQDgefmndlMMKEIKK-ADVKVDDKDLKDL 273
|
|
| Rotamase |
pfam00639 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
151-233 |
1.33e-25 |
|
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.
Pssm-ID: 425792 [Multi-domain] Cd Length: 96 Bit Score: 97.76 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 151 HILV-----------DTEEQARDALAKIEAGAN-FADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAAFALQPGQVS 217
Cdd:pfam00639 1 HILIktpeaserdraEAKAKAEEILEQLKSGEDsFAELARKYSDDcPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80
|
90
....*....|....*.
gi 1841979023 218 QPVQTNYGWHIIKVEE 233
Cdd:pfam00639 81 GPVETRFGFHIIKLTD 96
|
|
| PTZ00356 |
PTZ00356 |
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional |
145-230 |
1.29e-22 |
|
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
Pssm-ID: 185573 [Multi-domain] Cd Length: 115 Bit Score: 90.47 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 145 ERVHARHILVD------------------TEEQARDALAK----IEAGAN-FADLAKQISKDGSAQYGGDLGFFSADEMV 201
Cdd:PTZ00356 4 DTVRAAHLLIKhtgsrnpvsrrtgkpvtrSKEEAIKELAKwreqIVSGEKtFEEIARQRSDCGSAAKGGDLGFFGRGQMQ 83
|
90 100
....*....|....*....|....*....
gi 1841979023 202 PEFSKAAFALQPGQVSQPVQTNYGWHIIK 230
Cdd:PTZ00356 84 KPFEDAAFALKVGEISDIVHTDSGVHIIL 112
|
|
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
143-279 |
1.56e-22 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 96.73 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 143 SVERVHARHIL-----VDTEEQARDALAKIEA-----GANFADLAKQISKD-GSAQYGGDLGFFSADEMVPEFSKAAFAL 211
Cdd:PRK10770 263 SVTEVHARHILlkpspIMTDEQARAKLEQIAAdiksgKTTFAAAAKEFSQDpGSANQGGDLGWATPDIFDPAFRDALMRL 342
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841979023 212 QPGQVSQPVQTNYGWHIIKVEE-RKVGGAEPFDKvKNGLRMIVLR---QKVQEKVAELRKSADVEMVDPDLQ 279
Cdd:PRK10770 343 NKGQISAPVHSSFGWHLIELLDtRQVDKTDAAQK-DRAYRMLFNRkfsEEAQTWMQEQRASAYVKILSNSNA 413
|
|
| Rotamase_2 |
pfam13145 |
PPIC-type PPIASE domain; |
125-247 |
5.17e-19 |
|
PPIC-type PPIASE domain;
Pssm-ID: 432992 [Multi-domain] Cd Length: 121 Bit Score: 80.95 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 125 VNEEDVRKLYDQEAAKVNSVERVHARHILVDTEE--QARDALAKIEAGANFADLAKQISKDGsaqygGDLGFFSADEMVP 202
Cdd:pfam13145 1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVaaDAALALLKAGALEDFAALAKGEGIKA-----ATLDIVESAELLP 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1841979023 203 -EFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKN 247
Cdd:pfam13145 76 eELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
|
|
| PRK15441 |
PRK15441 |
peptidyl-prolyl cis-trans isomerase C; Provisional |
149-235 |
6.05e-17 |
|
peptidyl-prolyl cis-trans isomerase C; Provisional
Pssm-ID: 185338 [Multi-domain] Cd Length: 93 Bit Score: 74.67 E-value: 6.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 149 ARHILVDTEEQARDALAKIEAGANFADLAKQISKDGSAQYGGDLGFFSADEMVPEFSKAAFALQPGQVSQPVQTNYGWHI 228
Cdd:PRK15441 7 ALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHI 86
|
....*..
gi 1841979023 229 IKVEERK 235
Cdd:PRK15441 87 IKVLYRN 93
|
|
| PRK10788 |
PRK10788 |
periplasmic folding chaperone; Provisional |
124-264 |
1.73e-15 |
|
periplasmic folding chaperone; Provisional
Pssm-ID: 182731 [Multi-domain] Cd Length: 623 Bit Score: 76.59 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 124 TVNEEDVRKLYDQEAAKVNSVERVHARHILVDTEEQARDALAKIEAGANFADLAKQISKDG-SAQYGGDLGFFSADEMVP 202
Cdd:PRK10788 248 TVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPD 327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841979023 203 EFSKAAFAlQPGQVSQPVQTNYGWHIIKVEERKVGGAEPFDKVKNGLRMIVLRQK-------VQEKVAE 264
Cdd:PRK10788 328 ELKNAGLK-EKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRDDIAAKVKQEKaldayyaLQQKVSD 395
|
|
| prsA |
PRK04405 |
peptidylprolyl isomerase; Provisional |
91-284 |
3.86e-12 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 235295 [Multi-domain] Cd Length: 298 Bit Score: 65.57 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 91 KEAIAETNEYKKRL-----AFYQAKALRDAYFHEKIQPT-VNEEDVRKLYD----QEAAKVNSVE-RVHARHILVDTEEQ 159
Cdd:PRK04405 78 KKVDKQYNSYKKQYgssfdSVLSQNGMTTSSFKQNLRTNlLSEAALKKLKKvtnsQLKKAWKSYQpKVTVQHILVSKKST 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 160 ARDALAKIEAGANFADLAKQISKDGSAQY-GGDLGFF-SADEMV-PEFSKAAFALQPGQVSQ-PVQTNYGWHIIKV---- 231
Cdd:PRK04405 158 AETVIKKLKDGKDFAKLAKKYSTDTATKNkGGKLSAFdSTDTTLdSTFKTAAFKLKNGEYTTtPVKTTYGYEVIKMikhp 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1841979023 232 ------EERKVGGAEPFDKVKNGLRMIvlrQKVQEKVAelrKSADVEMVDPDLQRLQSQ 284
Cdd:PRK04405 238 akgtfsDHKKALTKQIYAKWASDSSVM---QRVISKVL---KKANVSIKDKDLKDALSS 290
|
|
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
124-266 |
9.70e-08 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 52.82 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 124 TVNEEDVRKLYDQEAAKVNSVERVHARHILV------------DTEEQARDALAKIEAGANFADLAKQISKDGSAQYGGD 191
Cdd:PRK10770 133 TILPQEVDSLAKQIGNQNDASTELNLSHILIplpenptqdqvdEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841979023 192 LGFFSADEMVPEFSKAAFALQPGQVSQPVQTNYGWHIIKVEERKvGGAEPFDKVKNGLRMIVL-----------RQKVQE 260
Cdd:PRK10770 213 MGWGRIQELPGLFAQALSTAKKGDIVGPIRSGVGFHILKVNDLR-GESQNISVTEVHARHILLkpspimtdeqaRAKLEQ 291
|
....*.
gi 1841979023 261 KVAELR 266
Cdd:PRK10770 292 IAADIK 297
|
|
|