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Conserved domains on  [gi|692318523|ref|WP_032129322|]
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MULTISPECIES: peptidyl-prolyl cis-trans isomerase [Stenotrophomonas]

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
 1-641 1.49e-74

periplasmic folding chaperone; Provisional


The actual alignment was detected with superfamily member PRK10788:

Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 251.08  E-value: 1.49e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523   1 MLQKLRDKTSGWIVTVILGLLMIPFLFVIDNSYLGGVGAQNVAKVSApptwwrsapswwpvrmlwqhHEISAQDFRTRFE 80
Cdd:PRK10788   1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNG--------------------QEISRAQLEQAFQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  81 QERMRERQQQGENFDPRAfeSTENKMA-----VLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPAFlDSNGKFNENN 155
Cdd:PRK10788  61 SERNRLQQQLGDQFSELA--ANEGYMKqlrqqVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAF-QTDGKFDNNK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 156 YRLALAGGNppRTPTQFQELVRESL--QQSVipSGLQNSGFVTQAETERLLKLLGETRDVELAALpEVPADTA--PVTDE 231
Cdd:PRK10788 138 YLAILNQMG--MTADQYAQALRQQLttQQLI--NGVAGTDFMLPGETDELAALVAQQRVVREATI-DVNALAAkqTVTDE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 232 QIKQWYDSHGKDFRQAESVSLEYVEINGANLPAPTAADEATLRKRYEDEKAKFTSPEQRQAAhILITGDGAEAKAnkiAT 311
Cdd:PRK10788 213 EIKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYS-IIQTKTEAEAKA---VL 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 312 EAKAAGADFAALAKANSEDPGSKDQGGDLGWVERGAMVKPFEDALFAAKaGDVIGPVKTDFGYHIIKVAAVRGGEGKSFE 391
Cdd:PRK10788 289 DELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLDDIQPAKVKPLS 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 392 EVRDTLAAE--QLKA-DGergFNELAGHLVDAINKSPSDLAAAAKEVNLPLQTLGPITRATASGIATDPAVLRAAFSEVL 468
Cdd:PRK10788 368 EVRDDIAAKvkQEKAlDA---YYALQQKVSDAASNDNESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFNGGL 444

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 469 VQD----GTASDPIALGGatNHSVVIRVAAHTPEQAMPLDKAREQVIAAIRADRQRQASDKAADAVLAKLKAGATLQSLA 544
Cdd:PRK10788 445 VGEngapGSNSDVITVDG--DRAFVLRISEHKPEAVKPLAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAMK 522

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 545 ASeKLQLSPMPGLPR-SQPVPTPEinrAIFSAPVPAEGKPSYGKV-DVNGHALLFAVNKVNPGdikEVTAEQQKQLKDQL 622
Cdd:PRK10788 523 AA-GLSFGEPKTLSRtSQDDPLSQ---AAFALPLPAKDKPSYGMAqDMQGNVVLIALDEVTPG---SMPEEQKKAMVQGI 595

                        650
                 ....*....|....*....
gi 692318523 623 SQIDGMAAAKAYVEAMRRK 641
Cdd:PRK10788 596 TQNNAQIAFEALMSNLRKE 614
 
Name Accession Description Interval E-value
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 1-641 1.49e-74

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 251.08  E-value: 1.49e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523   1 MLQKLRDKTSGWIVTVILGLLMIPFLFVIDNSYLGGVGAQNVAKVSApptwwrsapswwpvrmlwqhHEISAQDFRTRFE 80
Cdd:PRK10788   1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNG--------------------QEISRAQLEQAFQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  81 QERMRERQQQGENFDPRAfeSTENKMA-----VLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPAFlDSNGKFNENN 155
Cdd:PRK10788  61 SERNRLQQQLGDQFSELA--ANEGYMKqlrqqVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAF-QTDGKFDNNK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 156 YRLALAGGNppRTPTQFQELVRESL--QQSVipSGLQNSGFVTQAETERLLKLLGETRDVELAALpEVPADTA--PVTDE 231
Cdd:PRK10788 138 YLAILNQMG--MTADQYAQALRQQLttQQLI--NGVAGTDFMLPGETDELAALVAQQRVVREATI-DVNALAAkqTVTDE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 232 QIKQWYDSHGKDFRQAESVSLEYVEINGANLPAPTAADEATLRKRYEDEKAKFTSPEQRQAAhILITGDGAEAKAnkiAT 311
Cdd:PRK10788 213 EIKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYS-IIQTKTEAEAKA---VL 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 312 EAKAAGADFAALAKANSEDPGSKDQGGDLGWVERGAMVKPFEDALFAAKaGDVIGPVKTDFGYHIIKVAAVRGGEGKSFE 391
Cdd:PRK10788 289 DELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLDDIQPAKVKPLS 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 392 EVRDTLAAE--QLKA-DGergFNELAGHLVDAINKSPSDLAAAAKEVNLPLQTLGPITRATASGIATDPAVLRAAFSEVL 468
Cdd:PRK10788 368 EVRDDIAAKvkQEKAlDA---YYALQQKVSDAASNDNESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFNGGL 444

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 469 VQD----GTASDPIALGGatNHSVVIRVAAHTPEQAMPLDKAREQVIAAIRADRQRQASDKAADAVLAKLKAGATLQSLA 544
Cdd:PRK10788 445 VGEngapGSNSDVITVDG--DRAFVLRISEHKPEAVKPLAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAMK 522

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 545 ASeKLQLSPMPGLPR-SQPVPTPEinrAIFSAPVPAEGKPSYGKV-DVNGHALLFAVNKVNPGdikEVTAEQQKQLKDQL 622
Cdd:PRK10788 523 AA-GLSFGEPKTLSRtSQDDPLSQ---AAFALPLPAKDKPSYGMAqDMQGNVVLIALDEVTPG---SMPEEQKKAMVQGI 595

                        650
                 ....*....|....*....
gi 692318523 623 SQIDGMAAAKAYVEAMRRK 641
Cdd:PRK10788 596 TQNNAQIAFEALMSNLRKE 614
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 282-414 6.86e-34

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 126.23  E-value: 6.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 282 AKFTSPEQRQAAHILITGDG------AEAKANKIATEAKAAGADFAALaKANSEDPGSKDQGGDLGWVERGAMVKPFEDA 355
Cdd:COG0760    1 DQFDSPEEVRASHILVKVPPsedrakAEAKAEELLAQLKAGADFAELA-KEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 692318523 356 LFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEGKSFEEVRDTLAAEQLKADGERGFNELA 414
Cdd:COG0760   80 AFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELR 138
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 1-180 1.12e-32

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: 123.45  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523    1 MLQKLRDKTSGWIVTVILGLLMIPFLFVIDNSYLGGvGAQNVAKVsapptwwrsapswwpvrmlwQHHEISAQDFRTRFE 80
Cdd:pfam13624   1 MLEFIRKHAKSWIAKIILGLIILSFVFWGVGSYFSG-GGGAVAKV--------------------NGEKISRAEFQRAYR 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523   81 QERMRERQQQGENFDPRAFESTENKMAVLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPAFLDsNGKFNENNYRLAL 160
Cdd:pfam13624  60 RQLDQLRQQFGPNLDAELLDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPAFQE-DGKFDKERYRQLL 138

                         170       180
                  ....*....|....*....|
gi 692318523  161 AGGNPprTPTQFQELVRESL 180
Cdd:pfam13624 139 RANGL--TPAEFEASLRQDL 156
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 196-404 2.33e-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: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  196 TQAETERLLKLLGETRDVE---LAALPE----VPADTAPVTDEQIKQWYDSHGKDFRQAESVSLEYVEING------ANL 262
Cdd:TIGR02933  20 SPDQLQQFDQAWQRQRHIEqavVRAADEigvvIPPSLLEEAPQALAQALDEQALDAAERRAMLAHHLRLEAqlacvcAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  263 PAPtaaDEATLRKRYEDEKAKFTSPEQRQAAHILIT--GDGAEAKANKIAT---EAKAAGADFAALAKANSEDPgSKDQG 337
Cdd:TIGR02933 100 PQP---DDADVEAWYRRHAEQFKRPEQRLTRHLLLTvnEDDREAVRTRILAilrRLRGKPAAFAEQAMRHSHCP-TAMEG 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692318523  338 GDLGWVERGAMVKPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEGKSFEE----VRDTLAAEQLKA 404
Cdd:TIGR02933 176 GLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRPARPLTLEEalprARDRLQLRQQKA 246
 
Name Accession Description Interval E-value
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 1-641 1.49e-74

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 251.08  E-value: 1.49e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523   1 MLQKLRDKTSGWIVTVILGLLMIPFLFVIDNSYLGGVGAQNVAKVSApptwwrsapswwpvrmlwqhHEISAQDFRTRFE 80
Cdd:PRK10788   1 MMDNLRTAANSVVLKIILALIILSFILTGVGGYLIGGSNNYAAKVNG--------------------QEISRAQLEQAFQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  81 QERMRERQQQGENFDPRAfeSTENKMA-----VLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPAFlDSNGKFNENN 155
Cdd:PRK10788  61 SERNRLQQQLGDQFSELA--ANEGYMKqlrqqVLNRLIDEALLDQYARELGLGISDEQVKQAIFATPAF-QTDGKFDNNK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 156 YRLALAGGNppRTPTQFQELVRESL--QQSVipSGLQNSGFVTQAETERLLKLLGETRDVELAALpEVPADTA--PVTDE 231
Cdd:PRK10788 138 YLAILNQMG--MTADQYAQALRQQLttQQLI--NGVAGTDFMLPGETDELAALVAQQRVVREATI-DVNALAAkqTVTDE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 232 QIKQWYDSHGKDFRQAESVSLEYVEINGANLPAPTAADEATLRKRYEDEKAKFTSPEQRQAAhILITGDGAEAKAnkiAT 311
Cdd:PRK10788 213 EIKSYYDQNKNNFMAPEQFKVSYIKLDAATMQQKITVSDADIQAYYDQHQDQFTQPERKRYS-IIQTKTEAEAKA---VL 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 312 EAKAAGADFAALAKANSEDPGSKDQGGDLGWVERGAMVKPFEDALFAAKaGDVIGPVKTDFGYHIIKVAAVRGGEGKSFE 391
Cdd:PRK10788 289 DELKKGADFATLAKEKSTDIISARNGGDLGWLEPATTPDELKNAGLKEK-GQLSGVIKSSVGFLIVRLDDIQPAKVKPLS 367

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 392 EVRDTLAAE--QLKA-DGergFNELAGHLVDAINKSPSDLAAAAKEVNLPLQTLGPITRATASGIATDPAVLRAAFSEVL 468
Cdd:PRK10788 368 EVRDDIAAKvkQEKAlDA---YYALQQKVSDAASNDNESLASAEQAAGVKAVQTGWFSRDNVPAELNFKPVAQAIFNGGL 444

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 469 VQD----GTASDPIALGGatNHSVVIRVAAHTPEQAMPLDKAREQVIAAIRADRQRQASDKAADAVLAKLKAGATLQSLA 544
Cdd:PRK10788 445 VGEngapGSNSDVITVDG--DRAFVLRISEHKPEAVKPLAQVRDQVTELVKRQKAEQQAKVDAEKLLAALKAGKGEEAMK 522

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 545 ASeKLQLSPMPGLPR-SQPVPTPEinrAIFSAPVPAEGKPSYGKV-DVNGHALLFAVNKVNPGdikEVTAEQQKQLKDQL 622
Cdd:PRK10788 523 AA-GLSFGEPKTLSRtSQDDPLSQ---AAFALPLPAKDKPSYGMAqDMQGNVVLIALDEVTPG---SMPEEQKKAMVQGI 595

                        650
                 ....*....|....*....
gi 692318523 623 SQIDGMAAAKAYVEAMRRK 641
Cdd:PRK10788 596 TQNNAQIAFEALMSNLRKE 614
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 282-414 6.86e-34

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 126.23  E-value: 6.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 282 AKFTSPEQRQAAHILITGDG------AEAKANKIATEAKAAGADFAALaKANSEDPGSKDQGGDLGWVERGAMVKPFEDA 355
Cdd:COG0760    1 DQFDSPEEVRASHILVKVPPsedrakAEAKAEELLAQLKAGADFAELA-KEYSQDPGSAANGGDLGWFSRGQLVPEFEEA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 692318523 356 LFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEGKSFEEVRDTLAAEQLKADGERGFNELA 414
Cdd:COG0760   80 AFALKPGEISGPVKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQELFQQALEAWLEELR 138
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 1-180 1.12e-32

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: 123.45  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523    1 MLQKLRDKTSGWIVTVILGLLMIPFLFVIDNSYLGGvGAQNVAKVsapptwwrsapswwpvrmlwQHHEISAQDFRTRFE 80
Cdd:pfam13624   1 MLEFIRKHAKSWIAKIILGLIILSFVFWGVGSYFSG-GGGAVAKV--------------------NGEKISRAEFQRAYR 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523   81 QERMRERQQQGENFDPRAFESTENKMAVLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPAFLDsNGKFNENNYRLAL 160
Cdd:pfam13624  60 RQLDQLRQQFGPNLDAELLDELGLRQQVLDQLIDRALLLQEAKKLGLAVSDEEVRQAIASIPAFQE-DGKFDKERYRQLL 138

                         170       180
                  ....*....|....*....|
gi 692318523  161 AGGNPprTPTQFQELVRESL 180
Cdd:pfam13624 139 RANGL--TPAEFEASLRQDL 156
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 275-383 1.63e-25

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: 101.67  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  275 KRYEDEKakfTSPEQRQAAHILI--------TGDGAEAKANKIAtEAKAAGADFAALAKANSEDPGSKDQGGDLGWVERG 346
Cdd:pfam13616   4 SKLVDKK---SAPDSVKASHILIsysqavsrTEEEAKAKADSLL-AALKNGADFAALAKTYSDDPASKNNGGDLGWFTKG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 692318523  347 AMVKPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVR 383
Cdd:pfam13616  80 QMVKEFEDAVFSLKVGEISGVVKTQFGFHIIKVTDKK 116
SurA_N_2 pfam13623
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
 2-157 3.05e-25

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: 101.88  E-value: 3.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523    2 LQKLRDKTSGWIVtVILGLLMIPFL---FVIDNSYLGGVGAQNVAKVSApptwwrsapswwpvrmlwqhHEISAQDFRTR 78
Cdd:pfam13623   1 LQKIREKSGGLLA-IIIGLALLAFIigdLFGVGSYLFGGSSNVVAEVNG--------------------EEISYQEFQQA 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523   79 FEQERMRERQQQGENFDPRAFESTENKMAVLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPA----FLDSNGKFNEN 154
Cdd:pfam13623  60 VENQRNRLRQQLGQNFDPAELDEAQLREQVWDQLVREKLLLQEAEKLGLTVSDEELVDAIQGNPAilqqFQPQTGKFDKQ 139


                  ...
gi 692318523  155 NYR 157
Cdd:pfam13623 140 KYQ 142
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 294-379 3.70e-22

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: 91.21  E-value: 3.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  294 HILITGDG--------AEAKANKIATEAKAAGADFAALAKANSEDPGSKDQGGDLGWVERGAMVKPFEDALFAAKAGDVI 365
Cdd:pfam00639   1 HILIKTPEaserdraeAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....
gi 692318523  366 GPVKTDFGYHIIKV 379
Cdd:pfam00639  81 GPVETRFGFHIIKL 94
prsA PRK03095
peptidylprolyl isomerase PrsA;
268-407 4.16e-21

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 93.91  E-value: 4.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 268 ADEATLRKRYEDEKAKFTSPEQRQAAHILITGdgaEAKANKIaTEAKAAGADFAALAKANSEDPGSKDQGGDLGWVERGA 347
Cdd:PRK03095 111 AQEKAIEKTITDKELKDNYKPEIKASHILVKD---EATAKKV-KEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGK 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692318523 348 MVKPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEgKSFEEVRDTL---AAEQLKADGE 407
Cdd:PRK03095 187 MVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPE-KSFEQSKADIkkeLVQKKAQDGE 248
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 192-400 4.80e-21

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 93.88  E-value: 4.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 192 SGFVTQAETERLLKLLGETRDVELAALPEVPADTAPVTDE----QIKQWYDSHGKDFRQA-ESVSLEyveiNGANLP--- 263
Cdd:PRK02998  33 VGNITEKELSKELRQKYGESTLYQMVLSKALLDKYKVSDEeakkQVEEAKDKMGDNFKSTlEQVGLK----NEDELKekm 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 264 APTAADEATLRKRYEDEKAKFTSPEQRQAAHILITgdgaEAKANKIATEAKAAGADFAALAKANSEDPGSKDQGGDLGWV 343
Cdd:PRK02998 109 KPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVK----DEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEISGF 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 692318523 344 ERGAMVKPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVRggEGKSFEEVRDTLAAE 400
Cdd:PRK02998 185 APGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKK--ELKPFDEVKDSIRKD 239
prsA PRK00059
peptidylprolyl isomerase; Provisional
 87-395 3.56e-20

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 92.08  E-value: 3.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  87 RQQQGENF--DPRAFES-TENKMAVLDQLIDEQVVRLVGEQAGVVIGDGAVREYIATIPAFLDSNGKFNENNYRLAL-AG 162
Cdd:PRK00059  65 KQQYGDNYekNEQVKEQiKQQKEQILDSLITEKVLLQKAKELKLIPSEEELNKEVDKKINEIKKQFNNDEEQFEEALkAT 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 163 GnppRTPTQFQELVReslqqsvipsglqnsgfvTQAETERLLKLLgeTRDVElaalpevpadtapVTDEQIKQWYDSHgk 242
Cdd:PRK00059 145 G---FTEETFKEYLK------------------NQIIIEKVINEV--VKDVK-------------VTDKDAQKYYNEN-- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 243 dfrqaesvsleyveinganlpaptaadeatlrkryedeKAKFT-SPEQRQAAHILITgdgAEAKANKIATEAKAAGADFA 321
Cdd:PRK00059 187 --------------------------------------KSKFTeKPNTMHLAHILVK---TEDEAKKVKKRLDKGEDFAK 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692318523 322 ALaKANSEDPGSKDQGGDLGWV--ERGAMVKPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEGKSFEEVRD 395
Cdd:PRK00059 226 VA-KEVSQDPGSKDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKE 300
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
269-395 1.85e-15

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 72.86  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  269 DEATLRKRYEDEKAKFTSPEQRqAAHILITGDGAEAKANKIATEAKAAGADFAALAKANsedpgskDQGGDLGWVERGAM 348
Cdd:pfam13145   2 TEEELKAYYEENKDEFSTPEGR-LLEILVFKDQVAADAALALLKAGALEDFAALAKGEG-------IKAATLDIVESAEL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 692318523  349 V-KPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEGKSFEEVRD 395
Cdd:pfam13145  74 LpEELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPAQPLPFEEAKD 121
prsA PRK03002
peptidylprolyl isomerase PrsA;
278-397 2.23e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 74.20  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 278 EDEKAKFtSPEQRqAAHILITGdgaEAKANKIATEAKAAGADFAALaKANSEDPGSKDQGGDLGWVERGAMVKPFEDALF 357
Cdd:PRK03002 127 KDVKDHY-KPEIK-ASHILVSD---ENEAKEIKKKLDAGASFEELA-KQESQDLLSKEKGGDLGYFNSGRMAPEFETAAY 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 692318523 358 AAKAGDVIGPVKTDFGYHIIKVAAVRggEGKSFEEVRDTL 397
Cdd:PRK03002 201 KLKVGQISNPVKSPNGYHIIKLTDKK--DLKPYDEVKDSI 238
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 330-378 1.93e-12

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 64.28  E-value: 1.93e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 692318523 330 DPGSKDQGGDLGWVERGAMVKPFEDALFAAKAGDVIGPVKTDFGYHIIK 378
Cdd:PTZ00356  64 DCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 196-404 2.33e-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: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  196 TQAETERLLKLLGETRDVE---LAALPE----VPADTAPVTDEQIKQWYDSHGKDFRQAESVSLEYVEING------ANL 262
Cdd:TIGR02933  20 SPDQLQQFDQAWQRQRHIEqavVRAADEigvvIPPSLLEEAPQALAQALDEQALDAAERRAMLAHHLRLEAqlacvcAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523  263 PAPtaaDEATLRKRYEDEKAKFTSPEQRQAAHILIT--GDGAEAKANKIAT---EAKAAGADFAALAKANSEDPgSKDQG 337
Cdd:TIGR02933 100 PQP---DDADVEAWYRRHAEQFKRPEQRLTRHLLLTvnEDDREAVRTRILAilrRLRGKPAAFAEQAMRHSHCP-TAMEG 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692318523  338 GDLGWVERGAMVKPFEDALFAAKAGDVIGPVKTDFGYHIIKVAAVRGGEGKSFEE----VRDTLAAEQLKA 404
Cdd:TIGR02933 176 GLLGWVSRGLLYPQLDAALFQLAEGELSPPIESEIGWHLLLCEAIRPARPLTLEEalprARDRLQLRQQKA 246
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 292-383 3.71e-11

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 65.53  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 292 AAHILI------TGDGAEAKANKIATEAKAAGADFAALAKANSEDPGSKDQGGDLGWVERGAMVKPFEDALFAAKAGDVI 365
Cdd:PRK10770 269 ARHILLkpspimTDEQARAKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKGQIS 348

                         90
                 ....*....|....*...
gi 692318523 366 GPVKTDFGYHIIKVAAVR 383
Cdd:PRK10770 349 APVHSSFGWHLIELLDTR 366
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 325-379 4.27e-08

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 51.18  E-value: 4.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 692318523 325 KANSEDPGSKdQGGDLGWVERGAMVKPFEDALFAAKAGDVIGPVKTDFGYHIIKV 379
Cdd:PRK15441  36 KKHSICPSGK-RGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKV 89
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 293-385 2.94e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 50.12  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692318523 293 AHILI---------TGDGAEAKANKIATEAKAAGADFAALAkANSEDPGSKdQGGDLGWVERGAMVKPFEDALFAAKAGD 363
Cdd:PRK10770 159 SHILIplpenptqdQVDEAESQARSIVDQARNGADFGKLAI-AYSADQQAL-KGGQMGWGRIQELPGLFAQALSTAKKGD 236

                         90       100
                 ....*....|....*....|..
gi 692318523 364 VIGPVKTDFGYHIIKVAAVRGG 385
Cdd:PRK10770 237 IVGPIRSGVGFHILKVNDLRGE 258
 
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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