|
Name |
Accession |
Description |
Interval |
E-value |
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
128-257 |
1.40e-43 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 144.33 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 128 AGDKEYHARHILV---------ATEAEAKDIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWASPASYVKPFSDAMVAL 196
Cdd:COG0760 4 DSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKeYSQDpGSAANGGDLGWFSRGQLVPEFEEAAFAL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224780290 197 KPGQITQtPVQTQFGYHVIKLEETRPTKLPALEEVKGQVAESLQQKKLAAYRDELLKKAKI 257
Cdd:COG0760 84 KPGEISG-PVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
25-243 |
4.61e-31 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 117.50 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 25 VATVNGKAIPSSRVDQ--VVKQVVAQGKQ------ADSPQLREAIKK-------DLIGREVLIQEADKQG-YGTRPEVKS 88
Cdd:PRK00059 38 VATVNGEKITRGDLDKdpKMQQVLEQLKQqygdnyEKNEQVKEQIKQqkeqildSLITEKVLLQKAKELKlIPSEEELNK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 89 QIDNA---------------------------------RQSIIINALLADYVKKNPVKDAEIKAEYDKFKAQ--AGDKEY 133
Cdd:PRK00059 118 EVDKKineikkqfnndeeqfeealkatgfteetfkeylKNQIIIEKVINEVVKDVKVTDKDAQKYYNENKSKftEKPNTM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 134 HARHILVATEAEAKDIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWA--SPASYVKPFSDAMVALKPGQITQtPVQTQ 209
Cdd:PRK00059 198 HLAHILVKTEDEAKKVKKRLDKGEDFAKVAKeVSQDpGSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISA-PVKTQ 276
|
250 260 270
....*....|....*....|....*....|....
gi 1224780290 210 FGYHVIKLEETRPTKLPALEEVKGQVAESLQQKK 243
Cdd:PRK00059 277 FGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEK 310
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
134-221 |
3.16e-20 |
|
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: 83.19 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 134 HARHILVA-------TEAEAK----DIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWASPASYVKPFSDAMVALKPGQ 200
Cdd:pfam13616 17 KASHILISysqavsrTEEEAKakadSLLAALKNGADFAALAKtYSDDpASKNNGGDLGWFTKGQMVKEFEDAVFSLKVGE 96
|
90 100
....*....|....*....|.
gi 1224780290 201 ITQtPVQTQFGYHVIKLEETR 221
Cdd:pfam13616 97 ISG-VVKTQFGFHIIKVTDKK 116
|
|
| prsA |
PRK04405 |
peptidylprolyl isomerase; Provisional |
8-217 |
2.95e-16 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 235295 [Multi-domain] Cd Length: 298 Bit Score: 76.36 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 8 LILALVAVVAIPAFA-----QNVATVNGKAIPSSRVDQVVKQVVAQGKQADSPQLREAIKKDLiGREVLIQEADKQGYGT 82
Cdd:PRK04405 9 ALAAASAGLALSLAGcssnqATVATYSGGKITQSQYYKEMKQSSAGKTVLANMIIYRALEKQY-GKKVSTKKVDKQYNSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 83 RPEVKSQIDNA-----------RQSIIINALLADYVKKN-PVKDAEIKAEYdkfkaqagdKEYHAR----HILVATEAEA 146
Cdd:PRK04405 88 KKQYGSSFDSVlsqngmttssfKQNLRTNLLSEAALKKLkKVTNSQLKKAW---------KSYQPKvtvqHILVSKKSTA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224780290 147 KDIIAKLKGGAKFEELAK-VSKDGSAAN-GGDLDW--ASPASYVKPFSDAMVALKPGQITQTPVQTQFGYHVIKL 217
Cdd:PRK04405 159 ETVIKKLKDGKDFAKLAKkYSTDTATKNkGGKLSAfdSTDTTLDSTFKTAAFKLKNGEYTTTPVKTTYGYEVIKM 233
|
|
| SurA_N_3 |
pfam13624 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
6-90 |
1.60e-07 |
|
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
Pssm-ID: 433358 [Multi-domain] Cd Length: 162 Bit Score: 49.88 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 6 ARLILALVAVVAI--------PAFAQNVATVNGKAIPSSRVDQVVKQVVAQ----------GKQADSPQLREAIKKDLIG 67
Cdd:pfam13624 14 AKIILGLIILSFVfwgvgsyfSGGGGAVAKVNGEKISRAEFQRAYRRQLDQlrqqfgpnldAELLDELGLRQQVLDQLID 93
|
90 100
....*....|....*....|....
gi 1224780290 68 REVLIQEADKQGYG-TRPEVKSQI 90
Cdd:pfam13624 94 RALLLQEAKKLGLAvSDEEVRQAI 117
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
128-257 |
1.40e-43 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 144.33 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 128 AGDKEYHARHILV---------ATEAEAKDIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWASPASYVKPFSDAMVAL 196
Cdd:COG0760 4 DSPEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKeYSQDpGSAANGGDLGWFSRGQLVPEFEEAAFAL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224780290 197 KPGQITQtPVQTQFGYHVIKLEETRPTKLPALEEVKGQVAESLQQKKLAAYRDELLKKAKI 257
Cdd:COG0760 84 KPGEISG-PVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAKI 143
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
25-243 |
4.61e-31 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 117.50 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 25 VATVNGKAIPSSRVDQ--VVKQVVAQGKQ------ADSPQLREAIKK-------DLIGREVLIQEADKQG-YGTRPEVKS 88
Cdd:PRK00059 38 VATVNGEKITRGDLDKdpKMQQVLEQLKQqygdnyEKNEQVKEQIKQqkeqildSLITEKVLLQKAKELKlIPSEEELNK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 89 QIDNA---------------------------------RQSIIINALLADYVKKNPVKDAEIKAEYDKFKAQ--AGDKEY 133
Cdd:PRK00059 118 EVDKKineikkqfnndeeqfeealkatgfteetfkeylKNQIIIEKVINEVVKDVKVTDKDAQKYYNENKSKftEKPNTM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 134 HARHILVATEAEAKDIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWA--SPASYVKPFSDAMVALKPGQITQtPVQTQ 209
Cdd:PRK00059 198 HLAHILVKTEDEAKKVKKRLDKGEDFAKVAKeVSQDpGSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISA-PVKTQ 276
|
250 260 270
....*....|....*....|....*....|....
gi 1224780290 210 FGYHVIKLEETRPTKLPALEEVKGQVAESLQQKK 243
Cdd:PRK00059 277 FGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEK 310
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
134-221 |
3.16e-20 |
|
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: 83.19 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 134 HARHILVA-------TEAEAK----DIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWASPASYVKPFSDAMVALKPGQ 200
Cdd:pfam13616 17 KASHILISysqavsrTEEEAKakadSLLAALKNGADFAALAKtYSDDpASKNNGGDLGWFTKGQMVKEFEDAVFSLKVGE 96
|
90 100
....*....|....*....|.
gi 1224780290 201 ITQtPVQTQFGYHVIKLEETR 221
Cdd:pfam13616 97 ISG-VVKTQFGFHIIKVTDKK 116
|
|
| prsA |
PRK03095 |
peptidylprolyl isomerase PrsA; |
3-254 |
1.29e-18 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 179537 [Multi-domain] Cd Length: 287 Bit Score: 83.12 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 3 LKPARLILALVAVVAIPAfaqnVATVNGKAIPSSRVDQVVK-QVVAQGKQADSPQlreaIKKDLIGREVLIQ-------E 74
Cdd:PRK03095 1 MKKAMLALAATSVIALSA----CGTSSSDKIVTSKAGDITKdEFYEQMKTQAGKQ----VLNNMVMEKVLIKnykvedkE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 75 ADKQGYGTRPEVKSQIDN-ARQSIIINALLADYVKKNPVKDAEI-KAEYDKFKAQAGDKEYHARHILVATEAEAKDIIAK 152
Cdd:PRK03095 73 VDKKYDEMKKQYGDQFDTlLKQQGIKEETLKTGVRAQLAQEKAIeKTITDKELKDNYKPEIKASHILVKDEATAKKVKEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 153 LKGGAKFEELAK-VSKD-GSAANGGDLDWASPASYVKPFSDAMVALKPGQITQtPVQTQFGYHVIKLEETRPTKLPaLEE 230
Cdd:PRK03095 153 LGQGKSFEELAKqYSEDtGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSE-PVKSQFGYHIIKVTDIKEPEKS-FEQ 230
|
250 260
....*....|....*....|....*.
gi 1224780290 231 VKGQVAESLQQKKL--AAYRDELLKK 254
Cdd:PRK03095 231 SKADIKKELVQKKAqdGEFMNDLMMK 256
|
|
| Rotamase |
pfam00639 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
137-219 |
1.42e-18 |
|
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: 78.11 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 137 HILVAT-------EAEAKDIIAKL-----KGGAKFEELA-KVSKD-GSAANGGDLDWASPASYVKPFSDAMVALKPGQIT 202
Cdd:pfam00639 1 HILIKTpeaserdRAEAKAKAEEIleqlkSGEDSFAELArKYSDDcPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80
|
90
....*....|....*..
gi 1224780290 203 QtPVQTQFGYHVIKLEE 219
Cdd:pfam00639 81 G-PVETRFGFHIIKLTD 96
|
|
| prsA |
PRK03002 |
peptidylprolyl isomerase PrsA; |
109-258 |
3.90e-18 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 101162 [Multi-domain] Cd Length: 285 Bit Score: 81.52 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 109 KNPVKDAEIKAEYDKfkaqagdkEYHARHILVATEAEAKDIIAKLKGGAKFEELAKV-SKD-GSAANGGDLDWASPASYV 186
Cdd:PRK03002 121 KKSVTEKDVKDHYKP--------EIKASHILVSDENEAKEIKKKLDAGASFEELAKQeSQDlLSKEKGGDLGYFNSGRMA 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224780290 187 KPFSDAMVALKPGQITQtPVQTQFGYHVIKLeeTRPTKLPALEEVKGQVAESLQQKKLA--AYRDELL----KKAKIQ 258
Cdd:PRK03002 193 PEFETAAYKLKVGQISN-PVKSPNGYHIIKL--TDKKDLKPYDEVKDSIRKNLEEERTAdpIFGKKLLqselKKANIK 267
|
|
| PRK10788 |
PRK10788 |
periplasmic folding chaperone; Provisional |
104-247 |
1.23e-17 |
|
periplasmic folding chaperone; Provisional
Pssm-ID: 182731 [Multi-domain] Cd Length: 623 Bit Score: 81.98 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 104 ADYVKKNPVKDAEIKAEYDKFKA---QAGDKEYHArhILVATEAEAKDIIAKLKGGAKFEELAKV-SKDG-SAANGGDLD 178
Cdd:PRK10788 241 ATMQQKITVSDADIQAYYDQHQDqftQPERKRYSI--IQTKTEAEAKAVLDELKKGADFATLAKEkSTDIiSARNGGDLG 318
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 179 WASPASYVKPFSDAMVALKpGQITQtPVQTQFGYHVIKLEETRPTKLPALEEVKGQVAESL-QQKKLAAY 247
Cdd:PRK10788 319 WLEPATTPDELKNAGLKEK-GQLSG-VIKSSVGFLIVRLDDIQPAKVKPLSEVRDDIAAKVkQEKALDAY 386
|
|
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
132-221 |
1.37e-16 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 78.24 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 132 EYHARHIL-----VATEAEAK----DIIAKLKGG-AKFEELAK-VSKD-GSAANGGDLDWASPASYVKPFSDAMVALKPG 199
Cdd:PRK10770 266 EVHARHILlkpspIMTDEQARakleQIAADIKSGkTTFAAAAKeFSQDpGSANQGGDLGWATPDIFDPAFRDALMRLNKG 345
|
90 100
....*....|....*....|..
gi 1224780290 200 QITQtPVQTQFGYHVIKLEETR 221
Cdd:PRK10770 346 QISA-PVHSSFGWHLIELLDTR 366
|
|
| prsA |
PRK04405 |
peptidylprolyl isomerase; Provisional |
8-217 |
2.95e-16 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 235295 [Multi-domain] Cd Length: 298 Bit Score: 76.36 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 8 LILALVAVVAIPAFA-----QNVATVNGKAIPSSRVDQVVKQVVAQGKQADSPQLREAIKKDLiGREVLIQEADKQGYGT 82
Cdd:PRK04405 9 ALAAASAGLALSLAGcssnqATVATYSGGKITQSQYYKEMKQSSAGKTVLANMIIYRALEKQY-GKKVSTKKVDKQYNSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 83 RPEVKSQIDNA-----------RQSIIINALLADYVKKN-PVKDAEIKAEYdkfkaqagdKEYHAR----HILVATEAEA 146
Cdd:PRK04405 88 KKQYGSSFDSVlsqngmttssfKQNLRTNLLSEAALKKLkKVTNSQLKKAW---------KSYQPKvtvqHILVSKKSTA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224780290 147 KDIIAKLKGGAKFEELAK-VSKDGSAAN-GGDLDW--ASPASYVKPFSDAMVALKPGQITQTPVQTQFGYHVIKL 217
Cdd:PRK04405 159 ETVIKKLKDGKDFAKLAKkYSTDTATKNkGGKLSAfdSTDTTLDSTFKTAAFKLKNGEYTTTPVKTTYGYEVIKM 233
|
|
| prsA |
PRK02998 |
peptidylprolyl isomerase; Reviewed |
109-244 |
1.06e-15 |
|
peptidylprolyl isomerase; Reviewed
Pssm-ID: 179522 [Multi-domain] Cd Length: 283 Bit Score: 74.62 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 109 KNPVKDAEIKAEYDKfkaqagdkEYHARHILVATEAEAKDIIAKLKGGAKFEELAK-VSKD-GSAANGGDLDWASPASYV 186
Cdd:PRK02998 119 KATVTEKDVKDNYKP--------EMKVSHILVKDEKTAKEVKEKVNNGEDFAALAKqYSEDtGSKEQGGEISGFAPGQTV 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1224780290 187 KPFSDAMVALKPGQITQtPVQTQFGYHVIKLeeTRPTKLPALEEVKGQVAESLQQKKL 244
Cdd:PRK02998 191 KEFEEAAYKLDAGQVSE-PVKTTYGYHIIKV--TDKKELKPFDEVKDSIRKDLEQQRL 245
|
|
| Rotamase_2 |
pfam13145 |
PPIC-type PPIASE domain; |
112-232 |
3.36e-15 |
|
PPIC-type PPIASE domain;
Pssm-ID: 432992 [Multi-domain] Cd Length: 121 Bit Score: 69.78 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 112 VKDAEIKAEYDKFKAQAGDKEYHARHILVATEAEAKDIIAKLKGGAKFEELAKVsKDGSAANGGDLDWASPASYV-KPFS 190
Cdd:pfam13145 1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAALALLKAGALEDFAAL-AKGEGIKAATLDIVESAELLpEELA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1224780290 191 DAMVALKPGQITqTPVQTQFGYHVIKLEETRPTKLPALEEVK 232
Cdd:pfam13145 80 KAAFALKPGEVS-GPIKTGNGYYVVRVTEIKPAQPLPFEEAK 120
|
|
| PTZ00356 |
PTZ00356 |
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional |
134-216 |
3.59e-12 |
|
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
Pssm-ID: 185573 [Multi-domain] Cd Length: 115 Bit Score: 61.58 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 134 HARHILVA------------------TEAEAKDIIAKL-----KGGAKFEELAKVSKD-GSAANGGDLDWASPASYVKPF 189
Cdd:PTZ00356 7 RAAHLLIKhtgsrnpvsrrtgkpvtrSKEEAIKELAKWreqivSGEKTFEEIARQRSDcGSAAKGGDLGFFGRGQMQKPF 86
|
90 100
....*....|....*....|....*..
gi 1224780290 190 SDAMVALKPGQITQtPVQTQFGYHVIK 216
Cdd:PTZ00356 87 EDAAFALKVGEISD-IVHTDSGVHIIL 112
|
|
| PRK15441 |
PRK15441 |
peptidyl-prolyl cis-trans isomerase C; Provisional |
131-217 |
9.63e-11 |
|
peptidyl-prolyl cis-trans isomerase C; Provisional
Pssm-ID: 185338 [Multi-domain] Cd Length: 93 Bit Score: 56.96 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 131 KEYHARHILVATEAEAKDIIAKLKGGAKFEELAKV-SKDGSAANGGDLDWASPASYVKPFsDAMVALKPGQITQTPVQTQ 209
Cdd:PRK15441 3 KTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKhSICPSGKRGGDLGEFRQGQMVPAF-DKVVFSCPVLEPTGPLHTQ 81
|
....*...
gi 1224780290 210 FGYHVIKL 217
Cdd:PRK15441 82 FGYHIIKV 89
|
|
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
26-221 |
1.72e-08 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 54.36 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 26 ATVNGKAIPSSRVDQVVKQVVAQGKQA-----DSPQLREAIKKDLIGREVLIQEADK-------------------QGYG 81
Cdd:PRK10770 12 AVVNNGVVLESDVDGLMQSVKLNAQQAgqqlpDDATLRHQILERLIMDNIILQMAQKmgvkisdeqldqaianiaaQNNM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 82 TRPEVKSQI-------DNARQSIIINALLADyVKKNPVK------DAEIKAEYDKFKAQ-AGDKEYHARHILVA------ 141
Cdd:PRK10770 92 TLDQMRSRLaydglnyNTYRNQIRKEMIISE-VRNNEVRrritilPQEVDSLAKQIGNQnDASTELNLSHILIPlpenpt 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 142 ------TEAEAKDIIAKLKGGAKFEELA-KVSKDGSAANGGDLDWASPASYVKPFSDAMVALKPGQITqTPVQTQFGYHV 214
Cdd:PRK10770 171 qdqvdeAESQARSIVDQARNGADFGKLAiAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIV-GPIRSGVGFHI 249
|
....*..
gi 1224780290 215 IKLEETR 221
Cdd:PRK10770 250 LKVNDLR 256
|
|
| SurA_N_3 |
pfam13624 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
6-90 |
1.60e-07 |
|
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
Pssm-ID: 433358 [Multi-domain] Cd Length: 162 Bit Score: 49.88 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 6 ARLILALVAVVAI--------PAFAQNVATVNGKAIPSSRVDQVVKQVVAQ----------GKQADSPQLREAIKKDLIG 67
Cdd:pfam13624 14 AKIILGLIILSFVfwgvgsyfSGGGGAVAKVNGEKISRAEFQRAYRRQLDQlrqqfgpnldAELLDELGLRQQVLDQLID 93
|
90 100
....*....|....*....|....
gi 1224780290 68 REVLIQEADKQGYG-TRPEVKSQI 90
Cdd:pfam13624 94 RALLLQEAKKLGLAvSDEEVRQAI 117
|
|
| SurA_N_2 |
pfam13623 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
6-92 |
7.70e-06 |
|
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.
Pssm-ID: 463938 Cd Length: 145 Bit Score: 44.49 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224780290 6 ARLILALVAVVAIPAFA----------------QNVATVNGKAIPSSRVDQVVKQVVAQGKQ----------ADSPQLRE 59
Cdd:pfam13623 8 SGGLLAIIIGLALLAFIigdlfgvgsylfggssNVVAEVNGEEISYQEFQQAVENQRNRLRQqlgqnfdpaeLDEAQLRE 87
|
90 100 110
....*....|....*....|....*....|....
gi 1224780290 60 AIKKDLIGREVLIQEADKQGYG-TRPEVKSQIDN 92
Cdd:pfam13623 88 QVWDQLVREKLLLQEAEKLGLTvSDEELVDAIQG 121
|
|
|