|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10788 |
PRK10788 |
periplasmic folding chaperone; Provisional |
1-619 |
0e+00 |
|
periplasmic folding chaperone; Provisional
Pssm-ID: 182731 [Multi-domain] Cd Length: 623 Bit Score: 1138.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 1 MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLIGGGNNYAAKVNGQEISRGQFENAFNSERNRMQQQLGDQYSELAAN 80
Cdd:PRK10788 1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNGQEISRAQLEQAFQSERNRLQQQLGDQFSELAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 81 EGYMKTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQAIFATPAFQVDGKFDNSRYNAILNQMGMSADQYAQALRNQL 160
Cdd:PRK10788 81 EGYMKQLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNNKYLAILNQMGMTADQYAQALRQQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 161 TTQQLINGIAGTDFMLKGETDELAALVSQQRVVREATIDVNAKAEKQQVSDAEITSYYDQHKNNFVTPEQFRVSYIMLDA 240
Cdd:PRK10788 161 TTQQLINGVAGTDFMLPGETDELAALVAQQRVVREATIDVNALAAKQTVTDEEIKSYYDQNKNNFMAPEQFKVSYIKLDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 241 ANIQQ--PVSDADIQAYYDQHQDQFTQPQRVRYSIIQTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWL 318
Cdd:PRK10788 241 ATMQQkiTVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKAVLDELKKGADFATLAKEKSTDIISARNGGDLGWL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 319 EDSTTPQELKDAGLKDKGQLSGVIKSSVGFLVVRLDDVQPAKVKTLAEVRDDIAAKVKHEKALDAYYALQQKVSDAASND 398
Cdd:PRK10788 321 EPATTPDELKNAGLKEKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRDDIAAKVKQEKALDAYYALQQKVSDAASND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 399 TESLAGAEQAAGVKAKETGWFSQQNLPEELNFKPVADAIFSGSLVGENGTPGSNSDIITVDGDRAFVLRVSEHKAEAIKP 478
Cdd:PRK10788 401 NESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFNGGLVGENGAPGSNSDVITVDGDRAFVLRISEHKPEAVKP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 479 LSEVKDQVKALVQHDKAEQQAKLEAEKLLVELKAGKGVDAMRAAGLQFGEQKTLSRSGQ-DPVSLAAFALGLPEKDKPSY 557
Cdd:PRK10788 481 LAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAMKAAGLSFGEPKTLSRTSQdDPLSQAAFALPLPAKDKPSY 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1881369383 558 GMATNTQGNVVLLALDEVKAGTMPEAQKQALVQGITQNNAQIVFEALMSNLRKEAKIKIGDA 619
Cdd:PRK10788 561 GMAQDMQGNVVLIALDEVTPGSMPEEQKKAMVQGITQNNAQIAFEALMSNLRKEAKIKIGDA 622
|
|
| SurA_N_3 |
pfam13624 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
1-166 |
7.89e-61 |
|
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: 199.72 E-value: 7.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 1 MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLiGGGNNYAAKVNGQEISRGQFENAFNSERNRMQQQLGDQYSELAAN 80
Cdd:pfam13624 1 MLEFIRKHAKSWIAKIILGLIILSFVFWGVGSYF-SGGGGAVAKVNGEKISRAEFQRAYRRQLDQLRQQFGPNLDAELLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 81 EgymKTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQAIFATPAFQVDGKFDNSRYNAILNQMGMSADQYAQALRNQL 160
Cdd:pfam13624 80 E---LGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPAFQEDGKFDKERYRQLLRANGLTPAEFEASLRQDL 156
|
....*.
gi 1881369383 161 TTQQLI 166
Cdd:pfam13624 157 LLQQLL 162
|
|
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
261-392 |
2.79e-28 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 110.05 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 261 DQFTQPQRVRYSII---------QTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWLEDSTTPQELKDA- 330
Cdd:COG0760 1 DQFDSPEEVRASHIlvkvppsedRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAa 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1881369383 331 -GLKdKGQLSGVIKSSVGFLVVRLDDVQPAKVKTLAEVRDDIAAKVKHEKALDAYYALQQKVS 392
Cdd:COG0760 81 fALK-PGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAK 142
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10788 |
PRK10788 |
periplasmic folding chaperone; Provisional |
1-619 |
0e+00 |
|
periplasmic folding chaperone; Provisional
Pssm-ID: 182731 [Multi-domain] Cd Length: 623 Bit Score: 1138.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 1 MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLIGGGNNYAAKVNGQEISRGQFENAFNSERNRMQQQLGDQYSELAAN 80
Cdd:PRK10788 1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNGQEISRAQLEQAFQSERNRLQQQLGDQFSELAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 81 EGYMKTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQAIFATPAFQVDGKFDNSRYNAILNQMGMSADQYAQALRNQL 160
Cdd:PRK10788 81 EGYMKQLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNNKYLAILNQMGMTADQYAQALRQQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 161 TTQQLINGIAGTDFMLKGETDELAALVSQQRVVREATIDVNAKAEKQQVSDAEITSYYDQHKNNFVTPEQFRVSYIMLDA 240
Cdd:PRK10788 161 TTQQLINGVAGTDFMLPGETDELAALVAQQRVVREATIDVNALAAKQTVTDEEIKSYYDQNKNNFMAPEQFKVSYIKLDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 241 ANIQQ--PVSDADIQAYYDQHQDQFTQPQRVRYSIIQTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWL 318
Cdd:PRK10788 241 ATMQQkiTVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKAVLDELKKGADFATLAKEKSTDIISARNGGDLGWL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 319 EDSTTPQELKDAGLKDKGQLSGVIKSSVGFLVVRLDDVQPAKVKTLAEVRDDIAAKVKHEKALDAYYALQQKVSDAASND 398
Cdd:PRK10788 321 EPATTPDELKNAGLKEKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRDDIAAKVKQEKALDAYYALQQKVSDAASND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 399 TESLAGAEQAAGVKAKETGWFSQQNLPEELNFKPVADAIFSGSLVGENGTPGSNSDIITVDGDRAFVLRVSEHKAEAIKP 478
Cdd:PRK10788 401 NESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFNGGLVGENGAPGSNSDVITVDGDRAFVLRISEHKPEAVKP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 479 LSEVKDQVKALVQHDKAEQQAKLEAEKLLVELKAGKGVDAMRAAGLQFGEQKTLSRSGQ-DPVSLAAFALGLPEKDKPSY 557
Cdd:PRK10788 481 LAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAMKAAGLSFGEPKTLSRTSQdDPLSQAAFALPLPAKDKPSY 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1881369383 558 GMATNTQGNVVLLALDEVKAGTMPEAQKQALVQGITQNNAQIVFEALMSNLRKEAKIKIGDA 619
Cdd:PRK10788 561 GMAQDMQGNVVLIALDEVTPGSMPEEQKKAMVQGITQNNAQIAFEALMSNLRKEAKIKIGDA 622
|
|
| SurA_N_3 |
pfam13624 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
1-166 |
7.89e-61 |
|
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: 199.72 E-value: 7.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 1 MMDSLRTAANSLVLKIIFGIIIVSFILTGVSGYLiGGGNNYAAKVNGQEISRGQFENAFNSERNRMQQQLGDQYSELAAN 80
Cdd:pfam13624 1 MLEFIRKHAKSWIAKIILGLIILSFVFWGVGSYF-SGGGGAVAKVNGEKISRAEFQRAYRRQLDQLRQQFGPNLDAELLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 81 EgymKTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQAIFATPAFQVDGKFDNSRYNAILNQMGMSADQYAQALRNQL 160
Cdd:pfam13624 80 E---LGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPAFQEDGKFDKERYRQLLRANGLTPAEFEASLRQDL 156
|
....*.
gi 1881369383 161 TTQQLI 166
Cdd:pfam13624 157 LLQQLL 162
|
|
| SurA_N_2 |
pfam13623 |
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ... |
2-142 |
7.85e-34 |
|
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: 125.77 E-value: 7.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 2 MDSLRTAANSLVLKIIfGIIIVSFI---LTGVSGYLIGGGNNYAAKVNGQEISRGQFENAFNSERNRMQQQLGDQYSELA 78
Cdd:pfam13623 1 LQKIREKSGGLLAIII-GLALLAFIigdLFGVGSYLFGGSSNVVAEVNGEEISYQEFQQAVENQRNRLRQQLGQNFDPAE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1881369383 79 ANegyMKTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQAIFATPAF-----QVDGKFDNSRYNAIL 142
Cdd:pfam13623 80 LD---EAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQGNPAIlqqfqPQTGKFDKQKYQQFL 145
|
|
| prsA |
PRK00059 |
peptidylprolyl isomerase; Provisional |
43-384 |
1.74e-33 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 234605 [Multi-domain] Cd Length: 336 Bit Score: 130.99 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 43 AKVNGQEISRGQFENAFNSER--NRMQQQLGDQYSELAANEGYMKTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQA 120
Cdd:PRK00059 39 ATVNGEKITRGDLDKDPKMQQvlEQLKQQYGDNYEKNEQVKEQIKQQKEQILDSLITEKVLLQKAKELKLIPSEEELNKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 121 IFATPA-FQVDGKFDNSRYNAILNQMGMSADQYAQALRNQLTTQQLINgiagtdfmlkgetdelaalvsqqrvvrEATID 199
Cdd:PRK00059 119 VDKKINeIKKQFNNDEEQFEEALKATGFTEETFKEYLKNQIIIEKVIN---------------------------EVVKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 200 VNakaekqqvsdaeitsyydqhknnfvtpeqfrvsyimldaaniqqpVSDADIQAYYDQHQDQFT-QPQRVRYSIIQTKT 278
Cdd:PRK00059 172 VK---------------------------------------------VTDKDAQKYYNENKSKFTeKPNTMHLAHILVKT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 279 ENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWL--EDSTTPQELKDAGLKDK-GQLSGVIKSSVGFLVVRLDD 355
Cdd:PRK00059 207 EDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKDKGGDLGDVpySDSGYDKEFMDGAKALKeGEISAPVKTQFGYHIIKAIK 286
|
330 340
....*....|....*....|....*....
gi 1881369383 356 VQPAKVKTLAEVRDDIAAKVKHEKALDAY 384
Cdd:PRK00059 287 KKEYPVKPFDSVKEDIKKQLLQEKQSEVF 315
|
|
| SurA |
COG0760 |
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ... |
261-392 |
2.79e-28 |
|
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440523 [Multi-domain] Cd Length: 143 Bit Score: 110.05 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 261 DQFTQPQRVRYSII---------QTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWLEDSTTPQELKDA- 330
Cdd:COG0760 1 DQFDSPEEVRASHIlvkvppsedRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAa 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1881369383 331 -GLKdKGQLSGVIKSSVGFLVVRLDDVQPAKVKTLAEVRDDIAAKVKHEKALDAYYALQQKVS 392
Cdd:COG0760 81 fALK-PGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELRKKAK 142
|
|
| Rotamase_2 |
pfam13145 |
PPIC-type PPIASE domain; |
247-369 |
1.70e-21 |
|
PPIC-type PPIASE domain;
Pssm-ID: 432992 [Multi-domain] Cd Length: 121 Bit Score: 90.19 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 247 VSDADIQAYYDQHQDQFTQPQRVRYSIIQTKTENEAKAVlDALNNGGDFAELAKEKSADIIsarNGGDLGWLE-DSTTPQ 325
Cdd:pfam13145 1 VTEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAA-LALLKAGALEDFAALAKGEGI---KAATLDIVEsAELLPE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1881369383 326 ELKDA--GLKdKGQLSGVIKSSVGFLVVRLDDVQPAKVKTLAEVRD 369
Cdd:pfam13145 77 ELAKAafALK-PGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
|
|
| Rotamase_3 |
pfam13616 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
269-357 |
1.09e-14 |
|
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: 70.47 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 269 VRYSIIQTKTENEAKA----VLDALNNGGDFAELAKEKSADIISARNGGDLGWLEDSTTPQELKDAGLK-DKGQLSGVIK 343
Cdd:pfam13616 23 ISYSQAVSRTEEEAKAkadsLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQMVKEFEDAVFSlKVGEISGVVK 102
|
90
....*....|....
gi 1881369383 344 SSVGFLVVRLDDVQ 357
Cdd:pfam13616 103 TQFGFHIIKVTDKK 116
|
|
| prsA |
PRK03002 |
peptidylprolyl isomerase PrsA; |
181-400 |
1.54e-14 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 101162 [Multi-domain] Cd Length: 285 Bit Score: 74.59 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 181 DELAALVSQQRVVREATI---DVNAKAEKQQvsdaeiTSYYDQHK----NNFVTPE-----QFRVSYIMLDAanIQQPVS 248
Cdd:PRK03002 54 DMLYEMMAQDVITKKYKVsddDVDKEVQKAK------SQYGDQFKnvlkNNGLKDEadfknQIKFKLAMNEA--IKKSVT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 249 DADIQAYYdqhqdqftQPQrVRYSIIQTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWLEDSTTPQELK 328
Cdd:PRK03002 126 EKDVKDHY--------KPE-IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1881369383 329 DAGLKDK-GQLSGVIKSSVGFLVVRLDDVQpaKVKTLAEVRDDIAAKVKHEKALDAYYA---LQQ--KVSDAASNDTE 400
Cdd:PRK03002 197 TAAYKLKvGQISNPVKSPNGYHIIKLTDKK--DLKPYDEVKDSIRKNLEEERTADPIFGkklLQSelKKANIKINDSE 272
|
|
| Rotamase |
pfam00639 |
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ... |
275-355 |
3.46e-14 |
|
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: 68.48 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 275 QTKTENEAKAVLDALNNGGD-FAELAKEKSADIISARNGGDLGWLEDSTTPQELKDA--GLKdKGQLSGVIKSSVGFLVV 351
Cdd:pfam00639 14 RAEAKAKAEEILEQLKSGEDsFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAafALK-PGEISGPVETRFGFHII 92
|
....
gi 1881369383 352 RLDD 355
Cdd:pfam00639 93 KLTD 96
|
|
| prsA |
PRK02998 |
peptidylprolyl isomerase; Reviewed |
205-391 |
1.62e-13 |
|
peptidylprolyl isomerase; Reviewed
Pssm-ID: 179522 [Multi-domain] Cd Length: 283 Bit Score: 71.54 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 205 EKQQVSDAEITSYYDQHK----NNF-VTPEQFRVS-----------YIMLDAAnIQQPVSDADIQAYYdqhqdqftQPQr 268
Cdd:PRK02998 65 DKYKVSDEEAKKQVEEAKdkmgDNFkSTLEQVGLKnedelkekmkpEIAFEKA-IKATVTEKDVKDNY--------KPE- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 269 VRYSIIQTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWLEDSTTPQELKDAGLK-DKGQLSGVIKSSVG 347
Cdd:PRK02998 135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKlDAGQVSEPVKTTYG 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1881369383 348 FLVVRLDDVQpaKVKTLAEVRDDIAAKVKHEKALDAYYALQQKV 391
Cdd:PRK02998 215 YHIIKVTDKK--ELKPFDEVKDSIRKDLEQQRLQDTTGKWKQQV 256
|
|
| prsA |
PRK03095 |
peptidylprolyl isomerase PrsA; |
243-385 |
1.30e-11 |
|
peptidylprolyl isomerase PrsA;
Pssm-ID: 179537 [Multi-domain] Cd Length: 287 Bit Score: 65.79 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 243 IQQPVSDADIQAYYDQhqdqftqpqRVRYSIIQTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWLEDST 322
Cdd:PRK03095 116 IEKTITDKELKDNYKP---------EIKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1881369383 323 TPQELKDAGLK-DKGQLSGVIKSSVGFLVVRLDDVQpAKVKTLAEVRDDIAAKVKHEKALDAYY 385
Cdd:PRK03095 187 MVKEFEDAAYKlKKDEVSEPVKSQFGYHIIKVTDIK-EPEKSFEQSKADIKKELVQKKAQDGEF 249
|
|
| PRK10770 |
PRK10770 |
peptidyl-prolyl cis-trans isomerase SurA; Provisional |
85-357 |
4.10e-10 |
|
peptidyl-prolyl cis-trans isomerase SurA; Provisional
Pssm-ID: 236758 [Multi-domain] Cd Length: 413 Bit Score: 62.07 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 85 KTLRQQVLNRLIDEALLDQYSRDLKLGISDEQVKQAIfATPAFQVDGKFDNSRYNaiLNQMGMSADQYaqalRNQLTTQQ 164
Cdd:PRK10770 46 ATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQAI-ANIAAQNNMTLDQMRSR--LAYDGLNYNTY----RNQIRKEM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 165 LIngiagtdfmlkgetdelaALVSQQRVVREATI---DVNAKAekQQVSDaeitsyydQHKNNfvtpEQFRVSYIMLdaa 241
Cdd:PRK10770 119 II------------------SEVRNNEVRRRITIlpqEVDSLA--KQIGN--------QNDAS----TELNLSHILI--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 242 niqqPVSDADIQAYYDqhqdqftqpqrvrysiiqtKTENEAKAVLDALNNGGDFAELAKEKSADiISARNGGDLGWLEDS 321
Cdd:PRK10770 164 ----PLPENPTQDQVD-------------------EAESQARSIVDQARNGADFGKLAIAYSAD-QQALKGGQMGWGRIQ 219
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1881369383 322 TTP----QELKDAglkDKGQLSGVIKSSVGFLVVRLDDVQ 357
Cdd:PRK10770 220 ELPglfaQALSTA---KKGDIVGPIRSGVGFHILKVNDLR 256
|
|
| prsA |
PRK04405 |
peptidylprolyl isomerase; Provisional |
203-383 |
5.75e-05 |
|
peptidylprolyl isomerase; Provisional
Pssm-ID: 235295 [Multi-domain] Cd Length: 298 Bit Score: 45.54 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 203 KAEKQQVsDAEITSYYDQHKNNFVT------------PEQFRVSYIMLDAANIQQPVSDADIQAYYDQHQDQFTQPQrvr 270
Cdd:PRK04405 74 KVSTKKV-DKQYNSYKKQYGSSFDSvlsqngmttssfKQNLRTNLLSEAALKKLKKVTNSQLKKAWKSYQPKVTVQH--- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 271 ysiIQTKTENEAKAVLDALNNGGDFAELAKEKSADIISARNGGDLGWLE--DSTTPQELKDA--GLKDKGQLSGVIKSSV 346
Cdd:PRK04405 150 ---ILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKNKGGKLSAFDstDTTLDSTFKTAafKLKNGEYTTTPVKTTY 226
|
170 180 190
....*....|....*....|....*....|....*..
gi 1881369383 347 GFLVVRLDDvQPAKVKTlaevrddiaakVKHEKALDA 383
Cdd:PRK04405 227 GYEVIKMIK-HPAKGTF-----------SDHKKALTK 251
|
|
| prsA |
PRK01326 |
foldase protein PrsA; Reviewed |
187-345 |
2.64e-04 |
|
foldase protein PrsA; Reviewed
Pssm-ID: 179281 [Multi-domain] Cd Length: 310 Bit Score: 43.26 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 187 VSQQRVVREATIDVNAKAEKQQVSDAEITSYY----DQHKNNF--------VTPEQFR--------VSYIMLDAAniQQP 246
Cdd:PRK01326 52 SAQQAMLNLTISRVFEKQYGDKVSDKEVEKAYaktaKQYGASFsralaqagLTPETYKaqirtsklVEYAVKEAA--KKE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 247 VSDADIQAYYDQHQDQFTQpqrvrySIIQTKTENEAKAVLDALN-NGGDFAELAKEKSAdiiSARNGGDLGWLEDSTT-P 324
Cdd:PRK01326 130 LTDEAYKKAYEEYTPEVTA------QIIRLDNEDKAKSVLEEAKaEGADFAQIAKENTT---TKEKKGEYKFDSGSTNvP 200
|
170 180
....*....|....*....|..
gi 1881369383 325 QELKDAGLK-DKGQLSGVIKSS 345
Cdd:PRK01326 201 EQVKKAAFAlDEDGVSDVISVL 222
|
|
| PRK12450 |
PRK12450 |
foldase protein PrsA; Reviewed |
169-303 |
8.68e-04 |
|
foldase protein PrsA; Reviewed
Pssm-ID: 138982 [Multi-domain] Cd Length: 309 Bit Score: 42.00 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1881369383 169 IAGTDFMLKGETDELAALVSQQRVVREATIDVNAKaekqQVSDAEITSYY----DQHKNNF--------VTPEQFR---- 232
Cdd:PRK12450 40 ITVSDFYNETKNTELAQKAMLSLVISRVFETQYAN----KVSDKEVEKAYkqtaDQYGTSFktvlaqsgLTPETYKkqir 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1881369383 233 ----VSYIMLDAANiQQPVSDADIQAYYDQHQDQFTQpqrvrySIIQTKTENEAKAVLDALN-NGGDFAELAKEKS 303
Cdd:PRK12450 116 ltklVEYAVKEQAK-NETISKKDYRQAYDAYTPTMTA------EIMQFEKEEDAKAALEAVKaEGADFAAIAKEKT 184
|
|
|