NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1378755051|gb|AWA42514|]
View 

molecular chaperone SurA [Pseudomonas fluorescens]

Protein Classification

peptidylprolyl isomerase family protein( domain architecture ID 1005302)

peptidylprolyl isomerase family protein such as peptidylprolyl isomerase SurA, a periplasmic molecular chaperone that facilitates correct folding of outer membrane porins, catalyzing the interconversion of cis- and trans-peptidylproline

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0042277|GO:0051082|GO:0006457
SCOP:  4002409

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10770 super family cl35947
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 13-423 9.06e-120

peptidyl-prolyl cis-trans isomerase SurA; Provisional


The actual alignment was detected with superfamily member PRK10770:

Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 354.82  E-value: 9.06e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  13 AAVQSIDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGLPPPGVLDQQVLERLIVENLQLQIGERSGIRITDEELNQA 92
Cdd:PRK10770    2 AAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  93 VGTIAQRNNMTPEQFRIALSRDGLSYEDAREQIRREMIISRVRQRRVAERIQVSEQEVKNfLASDLG-KMQLSEELHLAN 171
Cdd:PRK10770   82 IANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDS-LAKQIGnQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 172 ILIPTPESANSEAIQSAARKAMEVYQQLKQGADFGQMAVANSASDNALEGGDMGWRKAAQLPPPFDRELSSMTPGDITPP 251
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 252 ARTPGGFIILKLLEKRGGESQMR-DEVHVRHILVKPSPVRDEAKTKELAQSLYNRIEAGE-DFAELAKKYSEDPGSALNG 329
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGESQNISvTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKtTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 330 GDLNWIDPNALVPEFRAVMAKSPQGQLSKPFQTQYGWHVLEVLGRRATDSTEQAREQQAMTVLRNRKYDEELQTWLRQIR 409
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400

                         410
                  ....*....|....
gi 1378755051 410 DEAYVEIkLPGADQ 423
Cdd:PRK10770  401 ASAYVKI-LSNSNA 413
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 13-423 9.06e-120

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 354.82  E-value: 9.06e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  13 AAVQSIDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGLPPPGVLDQQVLERLIVENLQLQIGERSGIRITDEELNQA 92
Cdd:PRK10770    2 AAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  93 VGTIAQRNNMTPEQFRIALSRDGLSYEDAREQIRREMIISRVRQRRVAERIQVSEQEVKNfLASDLG-KMQLSEELHLAN 171
Cdd:PRK10770   82 IANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDS-LAKQIGnQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 172 ILIPTPESANSEAIQSAARKAMEVYQQLKQGADFGQMAVANSASDNALEGGDMGWRKAAQLPPPFDRELSSMTPGDITPP 251
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 252 ARTPGGFIILKLLEKRGGESQMR-DEVHVRHILVKPSPVRDEAKTKELAQSLYNRIEAGE-DFAELAKKYSEDPGSALNG 329
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGESQNISvTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKtTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 330 GDLNWIDPNALVPEFRAVMAKSPQGQLSKPFQTQYGWHVLEVLGRRATDSTEQAREQQAMTVLRNRKYDEELQTWLRQIR 409
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400

                         410
                  ....*....|....
gi 1378755051 410 DEAYVEIkLPGADQ 423
Cdd:PRK10770  401 ASAYVKI-LSNSNA 413
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 272-414 2.10e-49

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 164.36  E-value: 2.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 272 QMRDEVHVRHILVKPSPVRDEAKTKELAQSLYNRIEAGEDFAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKS 351
Cdd:COG0760     4 DSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1378755051 352 PQGQLSKPFQTQYGWHVLEVLGRRA--TDSTEQAREQqamtvLRNRKYDEELQTWLRQIRDEAYV 414
Cdd:COG0760    84 KPGEISGPVKTQFGYHIIKVEDRRPaeTPPFEEVKQQ-----IRQELFQQALEAWLEELRKKAKI 143
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 18-135 3.56e-46

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: 430518 [Multi-domain]  Cd Length: 118  Bit Score: 155.13  E-value: 3.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  18 IDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGLPPPGVLDQQVLERLIVENLQLQIGERSGIRITDEELNQAVGTIA 97
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1378755051  98 QRNNMTPEQFRIALSRDGLSYEDAREQIRREMIISRVR 135
Cdd:pfam09312  81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRLR 118
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 13-423 9.06e-120

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 354.82  E-value: 9.06e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  13 AAVQSIDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGLPPPGVLDQQVLERLIVENLQLQIGERSGIRITDEELNQA 92
Cdd:PRK10770    2 AAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  93 VGTIAQRNNMTPEQFRIALSRDGLSYEDAREQIRREMIISRVRQRRVAERIQVSEQEVKNfLASDLG-KMQLSEELHLAN 171
Cdd:PRK10770   82 IANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDS-LAKQIGnQNDASTELNLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 172 ILIPTPESANSEAIQSAARKAMEVYQQLKQGADFGQMAVANSASDNALEGGDMGWRKAAQLPPPFDRELSSMTPGDITPP 251
Cdd:PRK10770  161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 252 ARTPGGFIILKLLEKRGGESQMR-DEVHVRHILVKPSPVRDEAKTKELAQSLYNRIEAGE-DFAELAKKYSEDPGSALNG 329
Cdd:PRK10770  241 IRSGVGFHILKVNDLRGESQNISvTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKtTFAAAAKEFSQDPGSANQG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 330 GDLNWIDPNALVPEFRAVMAKSPQGQLSKPFQTQYGWHVLEVLGRRATDSTEQAREQQAMTVLRNRKYDEELQTWLRQIR 409
Cdd:PRK10770  321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400

                         410
                  ....*....|....
gi 1378755051 410 DEAYVEIkLPGADQ 423
Cdd:PRK10770  401 ASAYVKI-LSNSNA 413
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 272-414 2.10e-49

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 164.36  E-value: 2.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 272 QMRDEVHVRHILVKPSPVRDEAKTKELAQSLYNRIEAGEDFAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKS 351
Cdd:COG0760     4 DSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFAL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1378755051 352 PQGQLSKPFQTQYGWHVLEVLGRRA--TDSTEQAREQqamtvLRNRKYDEELQTWLRQIRDEAYV 414
Cdd:COG0760    84 KPGEISGPVKTQFGYHIIKVEDRRPaeTPPFEEVKQQ-----IRQELFQQALEAWLEELRKKAKI 143
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 18-135 3.56e-46

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: 430518 [Multi-domain]  Cd Length: 118  Bit Score: 155.13  E-value: 3.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  18 IDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGLPPPGVLDQQVLERLIVENLQLQIGERSGIRITDEELNQAVGTIA 97
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1378755051  98 QRNNMTPEQFRIALSRDGLSYEDAREQIRREMIISRVR 135
Cdd:pfam09312  81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRLR 118
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 260-375 1.71e-35

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: 127.10  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 260 ILKLLEKRggesQMRDEVHVRHILVK--PSPVRDEAKTKELAQSLYNRIEAGEDFAELAKKYSEDPGSALNGGDLNWIDP 337
Cdd:pfam13616   3 LSKLVDKK----SAPDSVKASHILISysQAVSRTEEEAKAKADSLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTK 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1378755051 338 NALVPEFRAVMAKSPQGQLSKPFQTQYGWHVLEVLGRR 375
Cdd:pfam13616  79 GQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 281-371 2.79e-31

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: 115.09  E-value: 2.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 281 HILVKPSPV--RDEAKTKELAQSLYNRIEAGED-FAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKSPQGQLS 357
Cdd:pfam00639   1 HILIKTPEAseRDRAEAKAKAEEILEQLKSGEDsFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....
gi 1378755051 358 KPFQTQYGWHVLEV 371
Cdd:pfam00639  81 GPVETRFGFHIIKL 94
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 160-286 9.15e-28

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 106.97  E-value: 9.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 160 KMQLSEELHLANILIPTPESANSEAiqsAARKAMEVYQQLKQGADFGQMAVANSAS-DNALEGGDMGWRKAAQLPPPFDR 238
Cdd:COG0760     2 QFDSPEEVRASHILVKVPPSEDRAK---AEAKAEELLAQLKAGADFAELAKEYSQDpGSAANGGDLGWFSRGQLVPEFEE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1378755051 239 ELSSMTPGDITPPARTPGGFIILKLLEKRGGESQMRDEV--HVRHILVKP 286
Cdd:COG0760    79 AAFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVkqQIRQELFQQ 128
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 172-265 1.95e-21

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: 88.13  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 172 ILIPTPEsANSEAIQSAARKAMEVYQQLKQGAD-FGQMAVANSASDN-ALEGGDMGWRKAAQLPPPFDRELSSMTPGDIT 249
Cdd:pfam00639   2 ILIKTPE-ASERDRAEAKAKAEEILEQLKSGEDsFAELARKYSDDCPsAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 1378755051 250 PPARTPGGFIILKLLE 265
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
prsA PRK00059
peptidylprolyl isomerase; Provisional
 275-404 2.91e-20

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 91.31  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 275 DEVHVRHILVKpspvrdeakTKELAQSLYNRIEAGEDFAELAKKYSEDPGSALNGGDLNWIDPN--ALVPEFRAVMAKSP 352
Cdd:PRK00059  195 NTMHLAHILVK---------TEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKDKGGDLGDVPYSdsGYDKEFMDGAKALK 265

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1378755051 353 QGQLSKPFQTQYGWHVLEVLGRR--ATDSTEQAREQQAMTVLRNRK---YDEELQTW 404
Cdd:PRK00059  266 EGEISAPVKTQFGYHIIKAIKKKeyPVKPFDSVKEDIKKQLLQEKQsevFKKKIEEW 322
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 276-411 4.15e-20

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 89.65  E-value: 4.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 276 EVHVRHILVKpspvrDEAKTKELAQSLYNrieaGEDFAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKSPQGQ 355
Cdd:PRK02998  134 EMKVSHILVK-----DEKTAKEVKEKVNN----GEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQ 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1378755051 356 LSKPFQTQYGWHVLEVLGRRATDSTEQAREQQAMTVLRNRKYDEELQtWLRQIRDE 411
Cdd:PRK02998  205 VSEPVKTTYGYHIIKVTDKKELKPFDEVKDSIRKDLEQQRLQDTTGK-WKQQVVND 259
prsA PRK03095
peptidylprolyl isomerase PrsA;
274-401 1.10e-17

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 82.73  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 274 RDEVHVRHILVKpspvrDEAKTKELAQSLynriEAGEDFAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKSPQ 353
Cdd:PRK03095  130 KPEIKASHILVK-----DEATAKKVKEEL----GQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKK 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1378755051 354 GQLSKPFQTQYGWHVLEVLGRRATDST-EQAREQQAMTVLRNRKYDEEL 401
Cdd:PRK03095  201 DEVSEPVKSQFGYHIIKVTDIKEPEKSfEQSKADIKKELVQKKAQDGEF 249
prsA PRK03002
peptidylprolyl isomerase PrsA;
276-376 1.87e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 76.13  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 276 EVHVRHILVKpspvrDEAKTKELAQSLynriEAGEDFAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKSPQGQ 355
Cdd:PRK03002  136 EIKASHILVS-----DENEAKEIKKKL----DAGASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQ 206

                          90       100
                  ....*....|....*....|.
gi 1378755051 356 LSKPFQTQYGWHVLEVLGRRA 376
Cdd:PRK03002  207 ISNPVKSPNGYHIIKLTDKKD 227
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 158-267 5.22e-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: 68.16  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 158 LGKMQLSEELHLANILIPTpESANSEAIQSAARKAMEVYQQLKQGADFGQMAVANSA-SDNALEGGDMGWRKAAQLPPPF 236
Cdd:pfam13616   7 VDKKSAPDSVKASHILISY-SQAVSRTEEEAKAKADSLLAALKNGADFAALAKTYSDdPASKNNGGDLGWFTKGQMVKEF 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1378755051 237 DRELSSMTPGDITPPARTPGGFIILKLLEKR 267
Cdd:pfam13616  86 EDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 6-135 8.56e-14

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: 68.75  E-value: 8.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051   6 FLGTAANAAVQSIDKVVAIVDNDVVMQSQLDQRVHEVQQTIAKR-GGGLPPPGV----LDQQVLERLIVENLQLQIGERS 80
Cdd:pfam13624  25 FVFWGVGSYFSGGGGAVAKVNGEKISRAEFQRAYRRQLDQLRQQfGPNLDAELLdelgLRQQVLDQLIDRALLLQEAKKL 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1378755051  81 GIRITDEELNQAVGTIA--QRNNM-TPEQFRIALSRDGLSYEDAREQIRREMIISRVR 135
Cdd:pfam13624 105 GLAVSDEEVRQAIASIPafQEDGKfDKERYRQLLRANGLTPAEFEASLRQDLLLQQLL 162
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 281-375 4.46e-13

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 64.66  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 281 HILVKpspvrdeakTKELAQSLYNRIEAGEDFAELAKKYSEDPgSALNGGDLNWIDPNALVPEFRAVMAKSPQGQLSKPF 360
Cdd:PRK15441    9 HILVK---------EEKLALDLLEQIKNGADFGKLAKKHSICP-SGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPL 78

                          90
                  ....*....|....*
gi 1378755051 361 QTQYGWHVLEVLGRR 375
Cdd:PRK15441   79 HTQFGYHIIKVLYRN 93
prsA PRK04405
peptidylprolyl isomerase; Provisional
 276-386 9.18e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 59.41  E-value: 9.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 276 EVHVRHILVkpspvrdeAKtKELAQSLYNRIEAGEDFAELAKKYSEDPGSALNGGDLNWIDP--NALVPEFRAVMAKSPQ 353
Cdd:PRK04405  144 KVTVQHILV--------SK-KSTAETVIKKLKDGKDFAKLAKKYSTDTATKNKGGKLSAFDStdTTLDSTFKTAAFKLKN 214

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1378755051 354 GQLSK-PFQTQYGWHVLEVLGRRA----TDSTEQAREQ 386
Cdd:PRK04405  215 GEYTTtPVKTTYGYEVIKMIKHPAkgtfSDHKKALTKQ 252
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 275-369 1.97e-09

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 55.03  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 275 DEVHVRHILVKPSPVR--------------DEAKTKELAQsLYNRIEAGE-DFAELAKKYSeDPGSALNGGDLNWIDPNA 339
Cdd:PTZ00356    4 DTVRAAHLLIKHTGSRnpvsrrtgkpvtrsKEEAIKELAK-WREQIVSGEkTFEEIARQRS-DCGSAAKGGDLGFFGRGQ 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1378755051 340 LVPEFRAVMAKSPQGQLSKPFQTQYGWHVL 369
Cdd:PTZ00356   82 MQKPFEDAAFALKVGEISDIVHTDSGVHII 111
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 59-297 3.20e-09

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 58.87  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  59 LDQQVLERLIVENLQLQIGERSGIRITDEELNQAVGTIA-----------------QRNNMTPEQFRIALSRD------- 114
Cdd:PRK10788   87 LRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPafqtdgkfdnnkylailNQMGMTADQYAQALRQQlttqqli 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 115 -GLSYED---AREQIRREMIISRVRQRRVA--------ERIQVSEQEVKNFL----------------------ASDLGK 160
Cdd:PRK10788  167 nGVAGTDfmlPGETDELAALVAQQRVVREAtidvnalaAKQTVTDEEIKSYYdqnknnfmapeqfkvsyikldaATMQQK 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 161 MQLSE-------ELHLANILipTPESANSEAIQSAARK-AMEVYQQLKQGADFGQMAVANSA-SDNALEGGDMGWRKAAQ 231
Cdd:PRK10788  247 ITVSDadiqayyDQHQDQFT--QPERKRYSIIQTKTEAeAKAVLDELKKGADFATLAKEKSTdIISARNGGDLGWLEPAT 324

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1378755051 232 LPPpfdrELSSMT---PGDITPPARTPGGFIILKLlekrggesqmrDEVHVRHilVKP-SPVRDE--AKTKE 297
Cdd:PRK10788  325 TPD----ELKNAGlkeKGQLSGVIKSSVGFLIVRL-----------DDIQPAK--VKPlSEVRDDiaAKVKQ 379
prsA PRK03002
peptidylprolyl isomerase PrsA;
83-277 3.78e-09

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 57.64  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  83 RITDEELNQAVgtiAQRNNMTPEQFRIALSRDGLSYE-DAREQIRREMIISRvrqrrvAERIQVSEQEVKNFLasdlgkm 161
Cdd:PRK03002   70 KVSDDDVDKEV---QKAKSQYGDQFKNVLKNNGLKDEaDFKNQIKFKLAMNE------AIKKSVTEKDVKDHY------- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 162 qlseelhlanilipTPESANSEAIQSAARKAMEVYQQLKQGADFGQMAVANSASDNALE-GGDMGWRKAAQLPPPFDREL 240
Cdd:PRK03002  134 --------------KPEIKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKEkGGDLGYFNSGRMAPEFETAA 199

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1378755051 241 SSMTPGDITPPARTPGGFIILKLLEKRggESQMRDEV 277
Cdd:PRK03002  200 YKLKVGQISNPVKSPNGYHIIKLTDKK--DLKPYDEV 234
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 192-267 1.91e-08

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 51.56  E-value: 1.91e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1378755051 192 AMEVYQQLKQGADFGQMAVANSASDNALEGGDMGWRKAAQLPPPFDRELSSMTPGDITPPARTPGGFIILKLLEKR 267
Cdd:PRK15441   18 ALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRN 93
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 294-366 1.96e-08

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 56.56  E-value: 1.96e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378755051 294 KTKELAQSLYNRIEAGEDFAELAKKYSEDPGSALNGGDLNWIDPNALVPEFRAVMAKSpQGQLSKPFQTQYGW 366
Cdd:PRK10788  279 KTEAEAKAVLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKE-KGQLSGVIKSSVGF 350
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
279-385 2.97e-07

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 48.98  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 279 VRHILVKPSPVRDEAKTKELAQslynriEAGEDFAELAKKYSEdpgsalNGGDLNWIDPNALVP-EFRAVMAKSPQGQLS 357
Cdd:pfam13145  24 LLEILVFKDQVAADAALALLKA------GALEDFAALAKGEGI------KAATLDIVESAELLPeELAKAAFALKPGEVS 91

                          90       100       110
                  ....*....|....*....|....*....|
gi 1378755051 358 KPFQTQYGWHVLEVLGRRATDST--EQARE 385
Cdd:pfam13145  92 GPIKTGNGYYVVRVTEIKPAQPLpfEEAKD 121
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
145-277 5.01e-07

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 48.21  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 145 VSEQEVKNFLasdlgkmqlseELHLANILipTPESANSEAIQSAARKAME-VYQQLKQGADFgqmAVANSASDNALEGGD 223
Cdd:pfam13145   1 VTEEELKAYY-----------EENKDEFS--TPEGRLLEILVFKDQVAADaALALLKAGALE---DFAALAKGEGIKAAT 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1378755051 224 MGW-RKAAQLPPPFDRELSSMTPGDITPPARTPGGFIILKLLEKRGGESQMRDEV 277
Cdd:pfam13145  65 LDIvESAELLPEELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEA 119
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 21-105 1.00e-05

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: 45.26  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  21 VVAIVDNDVVMQSQLDQRVHEVQQTIAKRGGGLPPPGVLD-----QQVLERLIVENLQLQIGERSGIRITDEELNQAVGT 95
Cdd:pfam13623  42 VVAEVNGEEISYQEFQQAVENQRNRLRQQLGQNFDPAELDeaqlrEQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQG 121

                          90
                  ....*....|.
gi 1378755051  96 I-AQRNNMTPE 105
Cdd:pfam13623 122 NpAILQQFQPQ 132
prsA PRK01326
foldase protein PrsA; Reviewed
 61-220 2.45e-04

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 42.88  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  61 QQVLERLIVENLqlqIGERSGIRITDEELNQAvgtIAQRNNMTPEQFRIALSRDGLSYEDAREQIRREMIIsrvrqrrva 140
Cdd:PRK01326   54 QQAMLNLTISRV---FEKQYGDKVSDKEVEKA---YAKTAKQYGASFSRALAQAGLTPETYKAQIRTSKLV--------- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 141 eriqvsEQEVKnflasDLGKMQLSEELHLANILIPTPESAnSEAIQ-SAARKAMEVYQQLK-QGADFGQMAVANS-ASDN 217
Cdd:PRK01326  119 ------EYAVK-----EAAKKELTDEAYKKAYEEYTPEVT-AQIIRlDNEDKAKSVLEEAKaEGADFAQIAKENTtTKEK 186


                  ...
gi 1378755051 218 ALE 220
Cdd:PRK01326  187 KGE 189
prsA PRK03095
peptidylprolyl isomerase PrsA;
58-276 6.20e-04

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 41.52  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051  58 VLDQQVLERLIVENLQLqigERSGIRITDEELNQAVGtiaqrnnmtpEQFRIALSRDGLSYEDAREQIRREMIisrvrQR 137
Cdd:PRK03095   52 VLNNMVMEKVLIKNYKV---EDKEVDKKYDEMKKQYG----------DQFDTLLKQQGIKEETLKTGVRAQLA-----QE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 138 RVAERiQVSEQEVKNflasdlgkmQLSEELHLANILIPTPESANseaiqsaarkamEVYQQLKQGADFGQMAVANSASDN 217
Cdd:PRK03095  114 KAIEK-TITDKELKD---------NYKPEIKASHILVKDEATAK------------KVKEELGQGKSFEELAKQYSEDTG 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378755051 218 ALE-GGDMGWRKAAQLPPPFDRELSSMTPGDITPPARTPGGFIILKLLEKRGGESQMRDE 276
Cdd:PRK03095  172 SKEkGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPEKSFEQS 231
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH