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Conserved domains on  [gi|491491605|ref|WP_005349338|]
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MULTISPECIES: peptidylprolyl isomerase SurA [Aeromonas]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK10770 super family cl35947
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 22-427 7.36e-173

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: 490.02  E-value: 7.36e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  22 LAAPELMDKVLAVVNKDVVLSSQQDALVNKVKLSAQESGQSLPDDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQ 101
Cdd:PRK10770   1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 102 AIQGIAADNKMTLDQLRAQLAREGMTYAQYREEVRREILMNEVRRNQVRRRINISEQEVKQVVEILKKQGQQQNEYHVGH 181
Cdd:PRK10770  81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 182 IQIALPDNPTAAQLDAAKSKIERILAALKQGADFRKLAIAESNGPKALEGGDWGWMSPQEMPTLMAEAVQGAKKGDIVGP 261
Cdd:PRK10770 161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 262 LRSGAGLHIVKVFDTKGQ-QQVMQTEVKARHILIKPSIILSEEKAKGMLDGILHDIKSGKASFASMAEKYSEDPGSAVQG 340
Cdd:PRK10770 241 IRSGVGFHILKVNDLRGEsQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 341 GELGWSDPNVYVPEFRDMVNRLQPGQISAPFRTSHGWHIVQVEDRRSQDATDKAQEQRAYQLIYNRRFVEESQAWLDELR 420
Cdd:PRK10770 321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400


                 ....*..
gi 491491605 421 DEAYIQI 427
Cdd:PRK10770 401 ASAYVKI 407
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 22-427 7.36e-173

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 490.02  E-value: 7.36e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  22 LAAPELMDKVLAVVNKDVVLSSQQDALVNKVKLSAQESGQSLPDDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQ 101
Cdd:PRK10770   1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 102 AIQGIAADNKMTLDQLRAQLAREGMTYAQYREEVRREILMNEVRRNQVRRRINISEQEVKQVVEILKKQGQQQNEYHVGH 181
Cdd:PRK10770  81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 182 IQIALPDNPTAAQLDAAKSKIERILAALKQGADFRKLAIAESNGPKALEGGDWGWMSPQEMPTLMAEAVQGAKKGDIVGP 261
Cdd:PRK10770 161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 262 LRSGAGLHIVKVFDTKGQ-QQVMQTEVKARHILIKPSIILSEEKAKGMLDGILHDIKSGKASFASMAEKYSEDPGSAVQG 340
Cdd:PRK10770 241 IRSGVGFHILKVNDLRGEsQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 341 GELGWSDPNVYVPEFRDMVNRLQPGQISAPFRTSHGWHIVQVEDRRSQDATDKAQEQRAYQLIYNRRFVEESQAWLDELR 420
Cdd:PRK10770 321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400


                 ....*..
gi 491491605 421 DEAYIQI 427
Cdd:PRK10770 401 ASAYVKI 407
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 279-425 1.54e-43

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 149.34  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 279 QQQVMQTEVKARHILIKPSIILSEEKAKGMLDGILHDIKSGkASFASMAEKYSEDPGSAVQGGELGWSDPNVYVPEFRDM 358
Cdd:COG0760    1 DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491491605 359 VNRLQPGQISAPFRTSHGWHIVQVEDRR-SQDATDKAQEQRAYQLIYNRRFveesQAWLDELRDEAYI 425
Cdd:COG0760   80 AFALKPGEISGPVKTQFGYHIIKVEDRRpAETPPFEEVKQQIRQELFQQAL----EAWLEELRKKAKI 143
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 28-145 3.10e-41

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: 142.42  E-value: 3.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605   28 MDKVLAVVNKDVVLSSQQDALVNKVKLSAQESGQSLPDDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQAIQGIA 107
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 491491605  108 ADNKMTLDQLRAQLAREGMTYAQYREEVRREILMNEVR 145
Cdd:pfam09312  81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRLR 118
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 279-419 1.36e-12

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 67.56  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  279 QQQVMQTEVK-ARHILIKPSIILSEeKAKGMLDGILHDIKSGKASFASMAEKYSEDPgSAVQGGELGWSDPNVYVPEFRD 357
Cdd:TIGR02933 115 AEQFKRPEQRlTRHLLLTVNEDDRE-AVRTRILAILRRLRGKPAAFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDA 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491491605  358 MVNRLQPGQISAPFRTSHGWHIVQVEDRRSqdATDKAQEQ---RAYQLIYNRRFVEESQAWLDEL 419
Cdd:TIGR02933 193 ALFQLAEGELSPPIESEIGWHLLLCEAIRP--ARPLTLEEalpRARDRLQLRQQKAYQRQWLVQL 255
 
Name Accession Description Interval E-value
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 22-427 7.36e-173

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 490.02  E-value: 7.36e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  22 LAAPELMDKVLAVVNKDVVLSSQQDALVNKVKLSAQESGQSLPDDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQ 101
Cdd:PRK10770   1 FAAPQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAQQAGQQLPDDATLRHQILERLIMDNIILQMAQKMGVKISDEQLDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 102 AIQGIAADNKMTLDQLRAQLAREGMTYAQYREEVRREILMNEVRRNQVRRRINISEQEVKQVVEILKKQGQQQNEYHVGH 181
Cdd:PRK10770  81 AIANIAAQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVDSLAKQIGNQNDASTELNLSH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 182 IQIALPDNPTAAQLDAAKSKIERILAALKQGADFRKLAIAESNGPKALEGGDWGWMSPQEMPTLMAEAVQGAKKGDIVGP 261
Cdd:PRK10770 161 ILIPLPENPTQDQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 262 LRSGAGLHIVKVFDTKGQ-QQVMQTEVKARHILIKPSIILSEEKAKGMLDGILHDIKSGKASFASMAEKYSEDPGSAVQG 340
Cdd:PRK10770 241 IRSGVGFHILKVNDLRGEsQNISVTEVHARHILLKPSPIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 341 GELGWSDPNVYVPEFRDMVNRLQPGQISAPFRTSHGWHIVQVEDRRSQDATDKAQEQRAYQLIYNRRFVEESQAWLDELR 420
Cdd:PRK10770 321 GDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIELLDTRQVDKTDAAQKDRAYRMLFNRKFSEEAQTWMQEQR 400


                 ....*..
gi 491491605 421 DEAYIQI 427
Cdd:PRK10770 401 ASAYVKI 407
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 279-425 1.54e-43

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 149.34  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 279 QQQVMQTEVKARHILIKPSIILSEEKAKGMLDGILHDIKSGkASFASMAEKYSEDPGSAVQGGELGWSDPNVYVPEFRDM 358
Cdd:COG0760    1 DQFDSPEEVRASHILVKVPPSEDRAKAEAKAEELLAQLKAG-ADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491491605 359 VNRLQPGQISAPFRTSHGWHIVQVEDRR-SQDATDKAQEQRAYQLIYNRRFveesQAWLDELRDEAYI 425
Cdd:COG0760   80 AFALKPGEISGPVKTQFGYHIIKVEDRRpAETPPFEEVKQQIRQELFQQAL----EAWLEELRKKAKI 143
SurA_N pfam09312
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 28-145 3.10e-41

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: 142.42  E-value: 3.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605   28 MDKVLAVVNKDVVLSSQQDALVNKVKLSAQESGQSLPDDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQAIQGIA 107
Cdd:pfam09312   1 LDRIVAVVNDGVILQSELDRRVDTVKRNLQQQGTQLPPDAVLERQVLERLILERIQLQMAEKTGIRVDDAELNQAIARIA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 491491605  108 ADNKMTLDQLRAQLAREGMTYAQYREEVRREILMNEVR 145
Cdd:pfam09312  81 QQNNLTLDQLRQALAADGLSYDKFREQIRKEIIISRLR 118
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 291-384 2.11e-30

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: 112.78  E-value: 2.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  291 HILIK--PSIILSEEKAKGMLDGILHDIKSGKASFASMAEKYSEDPGSAVQGGELGWSDPNVYVPEFRDMVNRLQPGQIS 368
Cdd:pfam00639   1 HILIKtpEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 491491605  369 APFRTSHGWHIVQVED 384
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 268-386 1.25e-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: 108.61  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  268 LHIVKVFDTKGQQQvmqtEVKARHILIK--PSIILSEEKAKGMLDGILHDIKSGkASFASMAEKYSEDPGSAVQGGELGW 345
Cdd:pfam13616   1 YSLSKLVDKKSAPD----SVKASHILISysQAVSRTEEEAKAKADSLLAALKNG-ADFAALAKTYSDDPASKNNGGDLGW 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 491491605  346 SDPNVYVPEFRDMVNRLQPGQISAPFRTSHGWHIVQVEDRR 386
Cdd:pfam13616  76 FTKGQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 169-296 1.04e-24

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 98.88  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 169 KQGQQQNEYHVGHIQIALPDNptaAQLDAAKSKIERILAALKQGADFRKLAIAESNGPK-ALEGGDWGWMSPQEMPTLMA 247
Cdd:COG0760    1 DQFDSPEEVRASHILVKVPPS---EDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGsAANGGDLGWFSRGQLVPEFE 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491491605 248 EAVQGAKKGDIVGPLRSGAGLHIVKVFDTKGQQQVMQTEVK--ARHILIKP 296
Cdd:COG0760   78 EAAFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKqqIRQELFQQ 128
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 181-275 1.32e-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: 88.90  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  181 HIQIALPDnPTAAQLDAAKSKIERILAALKQGAD-FRKLAIAESN-GPKALEGGDWGWMSPQEMPTLMAEAVQGAKKGDI 258
Cdd:pfam00639   1 HILIKTPE-ASERDRAEAKAKAEEILEQLKSGEDsFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEI 79

                          90
                  ....*....|....*..
gi 491491605  259 VGPLRSGAGLHIVKVFD 275
Cdd:pfam00639  80 SGPVETRFGFHIIKLTD 96
prsA PRK00059
peptidylprolyl isomerase; Provisional
 3-306 8.52e-19

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 87.07  E-value: 8.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605   3 KTLIALLTAGMFgAMSQAALA----APELMDK-VLAVVNKDVVLSSQQDALVNKVKLSAQ---ESGQSLPDDA------- 67
Cdd:PRK00059   5 KKLVASLLVGVF-IFSAVGCNmiekTPEAIAKsTVATVNGEKITRGDLDKDPKMQQVLEQlkqQYGDNYEKNEqvkeqik 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  68 TLRKQALDRLIQESLQLQLAERQGLKISDTQL----EQAIQGIAADNKMTLDQLRAQLAREGMTYAQYREEVRREILMNE 143
Cdd:PRK00059  84 QQKEQILDSLITEKVLLQKAKELKLIPSEEELnkevDKKINEIKKQFNNDEEQFEEALKATGFTEETFKEYLKNQIIIEK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 144 VRrNQVRRRINISEQEVKQVVEILK-KQGQQQNEYHVGHIqialpdnptaaqLDAAKSKIERILAALKQGADFRKLAIAE 222
Cdd:PRK00059 164 VI-NEVVKDVKVTDKDAQKYYNENKsKFTEKPNTMHLAHI------------LVKTEDEAKKVKKRLDKGEDFAKVAKEV 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 223 SNGPKALE-GGDWGWMsPQEMPTLMAEAVQGA---KKGDIVGPLRSGAGLHIVKVFDTKGQQQVMQTEVKARhilIKpSI 298
Cdd:PRK00059 231 SQDPGSKDkGGDLGDV-PYSDSGYDKEFMDGAkalKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKED---IK-KQ 305


                 ....*...
gi 491491605 299 ILSEEKAK 306
Cdd:PRK00059 306 LLQEKQSE 313
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 31-145 2.06e-17

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: 79.15  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605   31 VLAVVNKDVVLSSQ-QDALVNKVKLSAQESGQSLP----DDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQAIQG 105
Cdd:pfam13624  40 AVAKVNGEKISRAEfQRAYRRQLDQLRQQFGPNLDaellDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIAS 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 491491605  106 IAA---DNKMTLDQLRAQLAREGMTYAQYREEVRREILMNEVR 145
Cdd:pfam13624 120 IPAfqeDGKFDKERYRQLLRANGLTPAEFEASLRQDLLLQQLL 162
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 167-277 6.65e-17

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: 76.25  E-value: 6.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  167 LKKQGQQQNEYHVGHIQIALPDNPTAAQlDAAKSKIERILAALKQGADFRKLAIAESNGPKALE-GGDWGWMSPQEMPTL 245
Cdd:pfam13616   6 LVDKKSAPDSVKASHILISYSQAVSRTE-EEAKAKADSLLAALKNGADFAALAKTYSDDPASKNnGGDLGWFTKGQMVKE 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 491491605  246 MAEAVQGAKKGDIVGPLRSGAGLHIVKVFDTK 277
Cdd:pfam13616  85 FEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 68-289 1.26e-16

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 81.98  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  68 TLRKQALDRLIQESLQLQLAERQGLKISDTQLEQAIQGIAA---DNKMTLDQLRAQLAREGMTYAQYREEVRRE------ 138
Cdd:PRK10788  86 QLRQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAfqtDGKFDNNKYLAILNQMGMTADQYAQALRQQlttqql 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 139 ---------ILMNEVRRN--------QVR----------RRINISEQEVKQVVEILKKQGQQQNEYHVGHIQI---ALPD 188
Cdd:PRK10788 166 ingvagtdfMLPGETDELaalvaqqrVVReatidvnalaAKQTVTDEEIKSYYDQNKNNFMAPEQFKVSYIKLdaaTMQQ 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 189 NPTAAQLDAAK---------SKIER----------------ILAALKQGADFRKLAIAESNGP-KALEGGDWGWMSPQEM 242
Cdd:PRK10788 246 KITVSDADIQAyydqhqdqfTQPERkrysiiqtkteaeakaVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATT 325

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 491491605 243 PTLMAEAvqGAK-KGDIVGPLRSGAGLHIVKVFDTKGQQQVMQTEVKA 289
Cdd:PRK10788 326 PDELKNA--GLKeKGQLSGVIKSSVGFLIVRLDDIQPAKVKPLSEVRD 371
prsA PRK03095
peptidylprolyl isomerase PrsA;
286-391 7.57e-16

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 77.73  E-value: 7.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 286 EVKARHILIKpsiilSEEKAKGMLDgilhDIKSGKaSFASMAEKYSEDPGSAVQGGELGWSDPNVYVPEFRDMVNRLQPG 365
Cdd:PRK03095 132 EIKASHILVK-----DEATAKKVKE----ELGQGK-SFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKD 201

                         90       100
                 ....*....|....*....|....*.
gi 491491605 366 QISAPFRTSHGWHIVQVEDRRSQDAT 391
Cdd:PRK03095 202 EVSEPVKSQFGYHIIKVTDIKEPEKS 227
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 286-396 1.39e-15

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 76.55  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 286 EVKARHILIKPSIILSEEKAKgmldgilhdIKSGKaSFASMAEKYSEDPGSAVQGGELGWSDPNVYVPEFRDMVNRLQPG 365
Cdd:PRK02998 134 EMKVSHILVKDEKTAKEVKEK---------VNNGE-DFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAG 203

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491491605 366 QISAPFRTSHGWHIVQVEDRRSQDATDKAQE 396
Cdd:PRK02998 204 QVSEPVKTTYGYHIIKVTDKKELKPFDEVKD 234
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 283-381 3.01e-15

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 71.60  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 283 MQTE-VKARHILIKPS-------------IILSEEKAKGMLDGILHDIKSGKASFASMAEKYSeDPGSAVQGGELGWSDP 348
Cdd:PTZ00356   1 MEGDtVRAAHLLIKHTgsrnpvsrrtgkpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRS-DCGSAAKGGDLGFFGR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491491605 349 NVYVPEFRDMVNRLQPGQISAPFRTSHGWHIVQ 381
Cdd:PTZ00356  80 GQMQKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
prsA PRK03002
peptidylprolyl isomerase PrsA;
286-396 8.67e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 71.50  E-value: 8.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 286 EVKARHILIKpsiilSEEKAKGmldgILHDIKSGkASFASMAEKYSEDPGSAVQGGELGWSDPNVYVPEFRDMVNRLQPG 365
Cdd:PRK03002 136 EIKASHILVS-----DENEAKE----IKKKLDAG-ASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVG 205

                         90       100       110
                 ....*....|....*....|....*....|.
gi 491491605 366 QISAPFRTSHGWHIVQVEDRRSQDATDKAQE 396
Cdd:PRK03002 206 QISNPVKSPNGYHIIKLTDKKDLKPYDEVKD 236
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 279-419 1.36e-12

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 67.56  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  279 QQQVMQTEVK-ARHILIKPSIILSEeKAKGMLDGILHDIKSGKASFASMAEKYSEDPgSAVQGGELGWSDPNVYVPEFRD 357
Cdd:TIGR02933 115 AEQFKRPEQRlTRHLLLTVNEDDRE-AVRTRILAILRRLRGKPAAFAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDA 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491491605  358 MVNRLQPGQISAPFRTSHGWHIVQVEDRRSqdATDKAQEQ---RAYQLIYNRRFVEESQAWLDEL 419
Cdd:TIGR02933 193 ALFQLAEGELSPPIESEIGWHLLLCEAIRP--ARPLTLEEalpRARDRLQLRQQKAYQRQWLVQL 255
prsA PRK03002
peptidylprolyl isomerase PrsA;
71-277 2.92e-06

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 48.78  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  71 KQALDRLIQESLQLQLAE---RQGLKISDTQLEQAIQGIaadNKMTLDQLRAQLAREGMT-YAQYREEVRREILMNEVRR 146
Cdd:PRK03002  45 KQLKDRYGKDMLYEMMAQdviTKKYKVSDDDVDKEVQKA---KSQYGDQFKNVLKNNGLKdEADFKNQIKFKLAMNEAIK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 147 NqvrrriNISEQEVKQvveilkkqgQQQNEYHVGHIqialpdnptaaqLDAAKSKIERILAALKQGADFRKLAIAESNGP 226
Cdd:PRK03002 122 K------SVTEKDVKD---------HYKPEIKASHI------------LVSDENEAKEIKKKLDAGASFEELAKQESQDL 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491491605 227 KALE-GGDWGWMSPQEMPTLMAEAVQGAKKGDIVGPLRSGAGLHIVKVFDTK 277
Cdd:PRK03002 175 LSKEkGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTDKK 226
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 205-274 3.17e-06

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 45.40  E-value: 3.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 205 ILAALKQGADFRKLAIAESNGPKALEGGDWGWMSPQEMPTLMAEAVQGAKKGDIVGPLRSGAGLHIVKVF 274
Cdd:PRK15441  21 LLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVL 90
prsA PRK04405
peptidylprolyl isomerase; Provisional
 269-382 3.40e-06

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 48.63  E-value: 3.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 269 HIVKVFDTKGQQQ--VMQTEVKARHILIKpsiilseekAKGMLDGILHDIKSGKaSFASMAEKYSEDPGSAVQGGELGWS 346
Cdd:PRK04405 125 KLKKVTNSQLKKAwkSYQPKVTVQHILVS---------KKSTAETVIKKLKDGK-DFAKLAKKYSTDTATKNKGGKLSAF 194

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491491605 347 DP--NVYVPEFRDMVNRLQPGQISA-PFRTSHGWHIVQV 382
Cdd:PRK04405 195 DStdTTLDSTFKTAAFKLKNGEYTTtPVKTTYGYEVIKM 233
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 57-106 7.80e-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: 45.26  E-value: 7.80e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491491605   57 QESGQSLPDDATLRKQALDRLIQESLQLQLAERQGLKISDTQLEQAIQGI 106
Cdd:pfam13623  73 QNFDPAELDEAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQGN 122
prsA PRK03095
peptidylprolyl isomerase PrsA;
130-289 1.19e-05

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 46.91  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 130 QYREEVRREILMNEVRRNQVRRRInISEQEVKQVVEILKKQGQQQNEYHVGHIQIAlpDNPTAaqldaakskiERILAAL 209
Cdd:PRK03095  87 QFDTLLKQQGIKEETLKTGVRAQL-AQEKAIEKTITDKELKDNYKPEIKASHILVK--DEATA----------KKVKEEL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 210 KQGADFRKLAIAESNGPKALE-GGDWGWMSPQEMPTLMAEAVQGAKKGDIVGPLRSGAGLHIVKVFDTKGQQQVMQtEVK 288
Cdd:PRK03095 154 GQGKSFEELAKQYSEDTGSKEkGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPEKSFE-QSK 232


                 .
gi 491491605 289 A 289
Cdd:PRK03095 233 A 233
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 188-272 2.47e-05

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 43.48  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605 188 DNPTAAQLDAAKSKIERILAALKQGA-DFRKLAIAESNGPKALEGGDWGWMSPQEMPTLMAEAVQGAKKGDIVGPLRSGA 266
Cdd:PTZ00356  27 GKPVTRSKEEAIKELAKWREQIVSGEkTFEEIARQRSDCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDS 106


                 ....*.
gi 491491605 267 GLHIVK 272
Cdd:PTZ00356 107 GVHIIL 112
prsA PRK04405
peptidylprolyl isomerase; Provisional
 1-219 4.34e-04

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 42.08  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605   1 MKKTLIALLTAGMfgAMSQAALaapelmdkvlavvnkdvvlSSQQDALVNKV--KLSAQESGQSLPDDATlRKQALDRLI 78
Cdd:PRK04405   5 MKKWALAAASAGL--ALSLAGC-------------------SSNQATVATYSggKITQSQYYKEMKQSSA-GKTVLANMI 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491491605  79 qesLQLQLAERQGLKISDTQLEQAIQGIaadNKMTLDQLRAQLAREGMTYAQYREEVRREILmnevrrnqvrrriniSEQ 158
Cdd:PRK04405  63 ---IYRALEKQYGKKVSTKKVDKQYNSY---KKQYGSSFDSVLSQNGMTTSSFKQNLRTNLL---------------SEA 121

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491491605 159 EVKQVVEILKKQGQQQ-NEYH----VGHIqialpdnptaaqLDAAKSKIERILAALKQGADFRKLA 219
Cdd:PRK04405 122 ALKKLKKVTNSQLKKAwKSYQpkvtVQHI------------LVSKKSTAETVIKKLKDGKDFAKLA 175
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
197-273 1.14e-03

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 38.58  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491491605  197 AAKSKIERILAALKQGADFRKLAIAESNGPKAlEGGDWGwMSPQEMPTLMAEAVQGAKKGDIVGPLRSGAGLHIVKV 273
Cdd:pfam13145  31 KDQVAADAALALLKAGALEDFAALAKGEGIKA-ATLDIV-ESAELLPEELAKAAFALKPGEVSGPIKTGNGYYVVRV 105
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
335-386 6.34e-03

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 36.65  E-value: 6.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491491605  335 GSAVQGGELGWSDPNVYVP-EFRDMVNRLQPGQISAPFRTSHGWHIVQVEDRR 386
Cdd:pfam13145  57 GEGIKAATLDIVESAELLPeELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIK 109
 
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.
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