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Conserved domains on  [gi|489575275|ref|WP_003479721|]
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peptidylprolyl isomerase [Xanthomonas translucens]

Protein Classification

peptidyl-prolyl isomerase family protein( domain architecture ID 1001049)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; may be partial

EC:  5.2.1.8
Gene Ontology:  GO:0003755
PubMed:  19866485

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10788 super family cl32577
periplasmic folding chaperone; Provisional
 1-656 5.51e-75

periplasmic folding chaperone; Provisional


The actual alignment was detected with superfamily member PRK10788:

Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 252.62  E-value: 5.51e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275   1 MLQKLREKTSGWIATAIIGLLMIPFLFVIDSSYLGGVGANNVAKVQAppswwssapswwpvsflwrhHEVSTEQFRLRFE 80
Cdd:PRK10788   1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNG--------------------QEISRAQLEQAFQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  81 EARQQAREQQGENFDprefESADNK-------RKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIATIPAFQKDGKFDPE 153
Cdd:PRK10788  61 SERNRLQQQLGDQFS----ELAANEgymkqlrQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 154 RYrLALASGTPpRTPAMFDQLVRDGL-QQSLIpSALMESAFATKQETERLLKMLGETRDVDLALLPEQP-ADTAPVSDAQ 231
Cdd:PRK10788 137 KY-LAILNQMG-MTADQYAQALRQQLtTQQLI-NGVAGTDFMLPGETDELAALVAQQRVVREATIDVNAlAAKQTVTDEE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 232 VQQWYDAHQADFKQPERVSIAYVELDASKLPPAKPADEAALRKRYEDEKARFVEPDQRLASHILISAGKDPASqkaaeak 311
Cdd:PRK10788 214 IKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKA------- 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 312 aaklAAEAKQPGADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKaGDIVGPVKSEFGYHVIQLREIKGG 391
Cdd:PRK10788 287 ----VLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLDDIQPA 361

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 392 KGKRFEQVRDQLAGEQQQADNEKVYSDLSGRLVDLVLKSPTALAPAAKQVGLPVQSLGPFSRANASGIAGQPAVLRAAFS 471
Cdd:PRK10788 362 KVKPLSEVRDDIAAKVKQEKALDAYYALQQKVSDAASNDNESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFN 441

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 472 DTLVQD----GTVSDPITLGPNHTVLIRVTQHLPEQTQPLAKVREQVAAAVHADRTAKAAAAKADALLERLRKGETLQAL 547
Cdd:PRK10788 442 GGLVGEngapGSNSDVITVDGDRAFVLRISEHKPEAVKPLAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAM 521

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 548 --AGpekLQINPMPGLPRTvPMPSPEANrAIFSAPLPAAGKPSVGKVELSANGVpggakryALFVLNKVNPGdlsKVPAE 625
Cdd:PRK10788 522 kaAG---LSFGEPKTLSRT-SQDDPLSQ-AAFALPLPAKDKPSYGMAQDMQGNV-------VLIALDEVTPG---SMPEE 586

                        650       660       670
                 ....*....|....*....|....*....|.
gi 489575275 626 QQATLKQQLGQIEGAAAAKAYIDAMRKRYKV 656
Cdd:PRK10788 587 QKKAMVQGITQNNAQIAFEALMSNLRKEAKI 617
 
Name Accession Description Interval E-value
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 1-656 5.51e-75

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 252.62  E-value: 5.51e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275   1 MLQKLREKTSGWIATAIIGLLMIPFLFVIDSSYLGGVGANNVAKVQAppswwssapswwpvsflwrhHEVSTEQFRLRFE 80
Cdd:PRK10788   1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNG--------------------QEISRAQLEQAFQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  81 EARQQAREQQGENFDprefESADNK-------RKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIATIPAFQKDGKFDPE 153
Cdd:PRK10788  61 SERNRLQQQLGDQFS----ELAANEgymkqlrQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 154 RYrLALASGTPpRTPAMFDQLVRDGL-QQSLIpSALMESAFATKQETERLLKMLGETRDVDLALLPEQP-ADTAPVSDAQ 231
Cdd:PRK10788 137 KY-LAILNQMG-MTADQYAQALRQQLtTQQLI-NGVAGTDFMLPGETDELAALVAQQRVVREATIDVNAlAAKQTVTDEE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 232 VQQWYDAHQADFKQPERVSIAYVELDASKLPPAKPADEAALRKRYEDEKARFVEPDQRLASHILISAGKDPASqkaaeak 311
Cdd:PRK10788 214 IKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKA------- 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 312 aaklAAEAKQPGADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKaGDIVGPVKSEFGYHVIQLREIKGG 391
Cdd:PRK10788 287 ----VLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLDDIQPA 361

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 392 KGKRFEQVRDQLAGEQQQADNEKVYSDLSGRLVDLVLKSPTALAPAAKQVGLPVQSLGPFSRANASGIAGQPAVLRAAFS 471
Cdd:PRK10788 362 KVKPLSEVRDDIAAKVKQEKALDAYYALQQKVSDAASNDNESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFN 441

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 472 DTLVQD----GTVSDPITLGPNHTVLIRVTQHLPEQTQPLAKVREQVAAAVHADRTAKAAAAKADALLERLRKGETLQAL 547
Cdd:PRK10788 442 GGLVGEngapGSNSDVITVDGDRAFVLRISEHKPEAVKPLAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAM 521

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 548 --AGpekLQINPMPGLPRTvPMPSPEANrAIFSAPLPAAGKPSVGKVELSANGVpggakryALFVLNKVNPGdlsKVPAE 625
Cdd:PRK10788 522 kaAG---LSFGEPKTLSRT-SQDDPLSQ-AAFALPLPAKDKPSYGMAQDMQGNV-------VLIALDEVTPG---SMPEE 586

                        650       660       670
                 ....*....|....*....|....*....|.
gi 489575275 626 QQATLKQQLGQIEGAAAAKAYIDAMRKRYKV 656
Cdd:PRK10788 587 QKKAMVQGITQNNAQIAFEALMSNLRKEAKI 617
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 1-179 1.37e-37

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: 137.32  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275    1 MLQKLREKTSGWIATAIIGLLMIPFLFVIDSSYLGGvGANNVAKVqappswwssapswwpvsflwRHHEVSTEQFRLRFE 80
Cdd:pfam13624   1 MLEFIRKHAKSWIAKIILGLIILSFVFWGVGSYFSG-GGGAVAKV--------------------NGEKISRAEFQRAYR 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275   81 EARQQAREQQGENFDPREFESADNKRKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIATIPAFQKDGKFDPERYRLALA 160
Cdd:pfam13624  60 RQLDQLRQQFGPNLDAELLDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPAFQEDGKFDKERYRQLLR 139

                         170       180
                  ....*....|....*....|
gi 489575275  161 S-GTpprTPAMFDQLVRDGL 179
Cdd:pfam13624 140 AnGL---TPAEFEASLRQDL 156
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 281-419 2.93e-37

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 135.86  E-value: 2.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 281 ARFVEPDQRLASHILISAgkDPASQKAAEAKAAKLAAEAKQPGADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFED 360
Cdd:COG0760    1 DQFDSPEEVRASHILVKV--PPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489575275 361 ALFAMKAGDIVGPVKSEFGYHVIQLREIKGGKGKRFEQVRDQLAGEQQQADNEKVYSDL 419
Cdd:COG0760   79 AAFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEEL 137
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 221-410 7.56e-13

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: 69.11  E-value: 7.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  221 PADTAPVSDAQVQQWYDahQADFKQPERVSI----AYVELDASKLPPAKPA-DEAALRKRYEDEKARFVEPDQRLASHIL 295
Cdd:TIGR02933  53 PPSLLEEAPQALAQALD--EQALDAAERRAMlahhLRLEAQLACVCAQAPQpDDADVEAWYRRHAEQFKRPEQRLTRHLL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  296 ISAGKDpASQKAAEAKAAKLAAEAKQPGAdFAALARANSEDPgSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDIVGPVK 375
Cdd:TIGR02933 131 LTVNED-DREAVRTRILAILRRLRGKPAA-FAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIE 207

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 489575275  376 SEFGYHVIQLREIKGG----KGKRFEQVRDQLAGEQQQA 410
Cdd:TIGR02933 208 SEIGWHLLLCEAIRPArpltLEEALPRARDRLQLRQQKA 246
 
Name Accession Description Interval E-value
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 1-656 5.51e-75

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 252.62  E-value: 5.51e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275   1 MLQKLREKTSGWIATAIIGLLMIPFLFVIDSSYLGGVGANNVAKVQAppswwssapswwpvsflwrhHEVSTEQFRLRFE 80
Cdd:PRK10788   1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNG--------------------QEISRAQLEQAFQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  81 EARQQAREQQGENFDprefESADNK-------RKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIATIPAFQKDGKFDPE 153
Cdd:PRK10788  61 SERNRLQQQLGDQFS----ELAANEgymkqlrQQVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAFQTDGKFDNN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 154 RYrLALASGTPpRTPAMFDQLVRDGL-QQSLIpSALMESAFATKQETERLLKMLGETRDVDLALLPEQP-ADTAPVSDAQ 231
Cdd:PRK10788 137 KY-LAILNQMG-MTADQYAQALRQQLtTQQLI-NGVAGTDFMLPGETDELAALVAQQRVVREATIDVNAlAAKQTVTDEE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 232 VQQWYDAHQADFKQPERVSIAYVELDASKLPPAKPADEAALRKRYEDEKARFVEPDQRLASHILISAGKDPASqkaaeak 311
Cdd:PRK10788 214 IKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYSIIQTKTEAEAKA------- 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 312 aaklAAEAKQPGADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKaGDIVGPVKSEFGYHVIQLREIKGG 391
Cdd:PRK10788 287 ----VLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLDDIQPA 361

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 392 KGKRFEQVRDQLAGEQQQADNEKVYSDLSGRLVDLVLKSPTALAPAAKQVGLPVQSLGPFSRANASGIAGQPAVLRAAFS 471
Cdd:PRK10788 362 KVKPLSEVRDDIAAKVKQEKALDAYYALQQKVSDAASNDNESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFN 441

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 472 DTLVQD----GTVSDPITLGPNHTVLIRVTQHLPEQTQPLAKVREQVAAAVHADRTAKAAAAKADALLERLRKGETLQAL 547
Cdd:PRK10788 442 GGLVGEngapGSNSDVITVDGDRAFVLRISEHKPEAVKPLAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAM 521

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 548 --AGpekLQINPMPGLPRTvPMPSPEANrAIFSAPLPAAGKPSVGKVELSANGVpggakryALFVLNKVNPGdlsKVPAE 625
Cdd:PRK10788 522 kaAG---LSFGEPKTLSRT-SQDDPLSQ-AAFALPLPAKDKPSYGMAQDMQGNV-------VLIALDEVTPG---SMPEE 586

                        650       660       670
                 ....*....|....*....|....*....|.
gi 489575275 626 QQATLKQQLGQIEGAAAAKAYIDAMRKRYKV 656
Cdd:PRK10788 587 QKKAMVQGITQNNAQIAFEALMSNLRKEAKI 617
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 1-179 1.37e-37

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: 137.32  E-value: 1.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275    1 MLQKLREKTSGWIATAIIGLLMIPFLFVIDSSYLGGvGANNVAKVqappswwssapswwpvsflwRHHEVSTEQFRLRFE 80
Cdd:pfam13624   1 MLEFIRKHAKSWIAKIILGLIILSFVFWGVGSYFSG-GGGAVAKV--------------------NGEKISRAEFQRAYR 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275   81 EARQQAREQQGENFDPREFESADNKRKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIATIPAFQKDGKFDPERYRLALA 160
Cdd:pfam13624  60 RQLDQLRQQFGPNLDAELLDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPAFQEDGKFDKERYRQLLR 139

                         170       180
                  ....*....|....*....|
gi 489575275  161 S-GTpprTPAMFDQLVRDGL 179
Cdd:pfam13624 140 AnGL---TPAEFEASLRQDL 156
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 281-419 2.93e-37

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 135.86  E-value: 2.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 281 ARFVEPDQRLASHILISAgkDPASQKAAEAKAAKLAAEAKQPGADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFED 360
Cdd:COG0760    1 DQFDSPEEVRASHILVKV--PPSEDRAKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489575275 361 ALFAMKAGDIVGPVKSEFGYHVIQLREIKGGKGKRFEQVRDQLAGEQQQADNEKVYSDL 419
Cdd:COG0760   79 AAFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEEL 137
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 274-389 1.03e-30

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: 116.31  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  274 KRYEDEKarfVEPDQRLASHILISAGKDPASQKAAEAKAAKLAAEAKQPGADFAALARANSEDPGSKNAGGDLGWVEKGV 353
Cdd:pfam13616   4 SKLVDKK---SAPDSVKASHILISYSQAVSRTEEEAKAKADSLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489575275  354 MVKPFEDALFAMKAGDIVGPVKSEFGYHVIQLREIK 389
Cdd:pfam13616  81 MVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 2-156 1.87e-26

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: 105.35  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275    2 LQKLREKTSGWIAtAIIGLLMIPFL---FVIDSSYLGGVGANNVAKVQAppswwssapswwpvsflwrhHEVSTEQFRLR 78
Cdd:pfam13623   1 LQKIREKSGGLLA-IIIGLALLAFIigdLFGVGSYLFGGSSNVVAEVNG--------------------EEISYQEFQQA 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275   79 FEEARQQAREQQGENFDPREFESADNKRKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIATIPAF-----QKDGKFDPE 153
Cdd:pfam13623  60 VENQRNRLRQQLGQNFDPAELDEAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQGNPAIlqqfqPQTGKFDKQ 139


                  ...
gi 489575275  154 RYR 156
Cdd:pfam13623 140 KYQ 142
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 293-387 3.31e-24

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: 96.99  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  293 HILISAGKDPASQKAAEAKAAKLAAEAKQPGAD-FAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDIV 371
Cdd:pfam00639   1 HILIKTPEASERDRAEAKAKAEEILEQLKSGEDsFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 489575275  372 GPVKSEFGYHVIQLRE 387
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
prsA PRK00059
peptidylprolyl isomerase; Provisional
 77-418 1.10e-22

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 99.79  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  77 LRFEEARQQAREQQGENFDPREfESADN----KRKVLDQLIDEQVVKLAAEQAHVVVGDAAVRDYIAT-IPAFQKDGKFD 151
Cdd:PRK00059  55 PKMQQVLEQLKQQYGDNYEKNE-QVKEQikqqKEQILDSLITEKVLLQKAKELKLIPSEEELNKEVDKkINEIKKQFNND 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 152 PERYRLAL-ASGTpprTPAMFDQLVRDglqqSLIPSALMESAfatkqeterllkmlgeTRDVDlallpeqpadtapVSDA 230
Cdd:PRK00059 134 EEQFEEALkATGF---TEETFKEYLKN----QIIIEKVINEV----------------VKDVK-------------VTDK 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 231 QVQQWYDAHQADFkqpervsiayveldasklppakpadeaalrkryedekarFVEPDQRLASHILISAgKDPASQKAAEA 310
Cdd:PRK00059 178 DAQKYYNENKSKF---------------------------------------TEKPNTMHLAHILVKT-EDEAKKVKKRL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 311 kaaklaaeakQPGADFAALARANSEDPGSKNAGGDLGWV--EKGVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQLREI 388
Cdd:PRK00059 218 ----------DKGEDFAKVAKEVSQDPGSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKK 287

                        330       340       350
                 ....*....|....*....|....*....|
gi 489575275 389 KGGKGKRFEQVRDQLAGEQQQADNEKVYSD 418
Cdd:PRK00059 288 KEYPVKPFDSVKEDIKKQLLQEKQSEVFKK 317
prsA PRK03095
peptidylprolyl isomerase PrsA;
264-419 2.43e-21

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 94.68  E-value: 2.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 264 AKPADEAALRKRYEDEKARFVEPDQRLASHILIsagKDPASQKAAEAKAAKlaaeakqpGADFAALARANSEDPGSKNAG 343
Cdd:PRK03095 108 AQLAQEKAIEKTITDKELKDNYKPEIKASHILV---KDEATAKKVKEELGQ--------GKSFEELAKQYSEDTGSKEKG 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489575275 344 GDLGWVEKGVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQLREIKGGKgKRFEQVRDQLAGE--QQQADNEKVYSDL 419
Cdd:PRK03095 177 GDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPE-KSFEQSKADIKKElvQKKAQDGEFMNDL 253
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 323-409 1.25e-18

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 86.56  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 323 GADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQLREIKggKGKRFEQVRDQ 402
Cdd:PRK02998 158 GEDFAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK--ELKPFDEVKDS 235


                 ....*..
gi 489575275 403 LAGEQQQ 409
Cdd:PRK02998 236 IRKDLEQ 242
prsA PRK03002
peptidylprolyl isomerase PrsA;
291-403 3.84e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 76.51  E-value: 3.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 291 ASHILISaGKDPASQKAAEAKAaklaaeakqpGADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDI 370
Cdd:PRK03002 139 ASHILVS-DENEAKEIKKKLDA----------GASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQI 207

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489575275 371 VGPVKSEFGYHVIQLREIKggKGKRFEQVRDQL 403
Cdd:PRK03002 208 SNPVKSPNGYHIIKLTDKK--DLKPYDEVKDSI 238
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
268-401 2.16e-14

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 70.16  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  268 DEAALRKRYEDEKARFVEPDQRLASHILISAGKDPASQKAAEAKAAklaaeakqpGADFAALARANSEDpgsknaGGDLG 347
Cdd:pfam13145   2 TEEELKAYYEENKDEFSTPEGRLLEILVFKDQVAADAALALLKAGA---------LEDFAALAKGEGIK------AATLD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489575275  348 WVEK-GVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQLREIKGGKGKRFEQVRD 401
Cdd:pfam13145  67 IVESaELLPEELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 324-385 4.37e-13

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 71.70  E-value: 4.37e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489575275 324 ADFAALARANSEDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQL 385
Cdd:PRK10770 301 TTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKGQISAPVHSSFGWHLIEL 362
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 221-410 7.56e-13

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: 69.11  E-value: 7.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  221 PADTAPVSDAQVQQWYDahQADFKQPERVSI----AYVELDASKLPPAKPA-DEAALRKRYEDEKARFVEPDQRLASHIL 295
Cdd:TIGR02933  53 PPSLLEEAPQALAQALD--EQALDAAERRAMlahhLRLEAQLACVCAQAPQpDDADVEAWYRRHAEQFKRPEQRLTRHLL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  296 ISAGKDpASQKAAEAKAAKLAAEAKQPGAdFAALARANSEDPgSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDIVGPVK 375
Cdd:TIGR02933 131 LTVNED-DREAVRTRILAILRRLRGKPAA-FAEQAMRHSHCP-TAMEGGLLGWVSRGLLYPQLDAALFQLAEGELSPPIE 207

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 489575275  376 SEFGYHVIQLREIKGG----KGKRFEQVRDQLAGEQQQA 410
Cdd:TIGR02933 208 SEIGWHLLLCEAIRPArpltLEEALPRARDRLQLRQQKA 246
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 326-384 1.21e-12

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 64.66  E-value: 1.21e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489575275 326 FAALARANSeDPGSKNAGGDLGWVEKGVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQ 384
Cdd:PTZ00356  55 FEEIARQRS-DCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 292-484 1.82e-10

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 63.22  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 292 SHILISAGKDPAS-QKAAEAKAAKLAAEAKQPGADFAALARANSEDPGSKNaGGDLGWVEKGVMVKPFEDALFAMKAGDI 370
Cdd:PRK10770 159 SHILIPLPENPTQdQVDEAESQARSIVDQARNGADFGKLAIAYSADQQALK-GGQMGWGRIQELPGLFAQALSTAKKGDI 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275 371 VGPVKSEFGYHVIQLREIKGG-KGKRFEQVRDQ---------LAGEQQQADNEKVYSDL-SGRlvdlvlkspTALAPAAK 439
Cdd:PRK10770 238 VGPIRSGVGFHILKVNDLRGEsQNISVTEVHARhillkpspiMTDEQARAKLEQIAADIkSGK---------TTFAAAAK 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489575275 440 QVglpvqSLGPFSrANASGIAG--QPAVLRAAFSDTLVQ--DGTVSDPI 484
Cdd:PRK10770 309 EF-----SQDPGS-ANQGGDLGwaTPDIFDPAFRDALMRlnKGQISAPV 351
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 323-385 6.56e-09

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 53.49  E-value: 6.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489575275 323 GADFAALARANSEDPGSKNaGGDLGWVEKGVMVKPFEDALFAMKAGDIVGPVKSEFGYHVIQL 385
Cdd:PRK15441  28 GADFGKLAKKHSICPSGKR-GGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKV 89
prsA PRK04405
peptidylprolyl isomerase; Provisional
 323-394 5.19e-07

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 51.71  E-value: 5.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489575275 323 GADFAALARANSEDPGSKNAGGDLGWVE--KGVMVKPFEDALFAMKAGDIVG-PVKSEFGYHVIQLreIKG-GKGK 394
Cdd:PRK04405 168 GKDFAKLAKKYSTDTATKNKGGKLSAFDstDTTLDSTFKTAAFKLKNGEYTTtPVKTTYGYEVIKM--IKHpAKGT 241
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
389-512 4.89e-03

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 37.42  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489575275  389 KGGKGKRFEQVRDQLAGEQQQADNEKvysdlsgrlvdlvlKSPTALAPAAKQVGLPVQSLGPFSRANASGiagqPAVLRA 468
Cdd:pfam13145  20 PEGRLLEILVFKDQVAADAALALLKA--------------GALEDFAALAKGEGIKAATLDIVESAELLP----EELAKA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489575275  469 AFSdtlVQDGTVSDPITlGPNHTVLIRVTQHLPEQTQPLAKVRE 512
Cdd:pfam13145  82 AFA---LKPGEVSGPIK-TGNGYYVVRVTEIKPAQPLPFEEAKD 121
 
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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