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Conserved domains on  [gi|475995|gb|AAA18574|]
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sensitivity to lysis gene [Escherichia coli]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10013629)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins, such as Escherichia coli FKBP-type peptidyl-prolyl cis-trans isomerase SlyD

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-196 1.95e-120

peptidylprolyl isomerase;


:

Pssm-ID: 236748  Cd Length: 196  Bit Score: 338.84  E-value: 1.95e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995      1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995     81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHH 160
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHH 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 475995    161 DHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH 196
Cdd:PRK10737 161 DHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH 196
 
Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-196 1.95e-120

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 338.84  E-value: 1.95e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995      1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995     81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHH 160
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHH 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 475995    161 DHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH 196
Cdd:PRK10737 161 DHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH 196
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
3-139 1.13e-54

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 170.28  E-value: 1.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995     3 VAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVPKD 82
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPRE 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 475995    83 VFMGVDELQVGMRFLAETDQG-PVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAI 139
Cdd:COG1047  81 QFPEDEELEVGMQVEFQTPDGqEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-70 6.24e-05

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 40.26  E-value: 6.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 475995       2 KVAKDLVVSLAYQVRTEDGVLVDES-----PVSAPLdylhGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQ 70
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSydrgkPFEFTL----GSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
 
Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-196 1.95e-120

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 338.84  E-value: 1.95e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995      1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995     81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHH 160
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHH 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 475995    161 DHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH 196
Cdd:PRK10737 161 DHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH 196
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
3-139 1.13e-54

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 170.28  E-value: 1.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995     3 VAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVPKD 82
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPRE 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 475995    83 VFMGVDELQVGMRFLAETDQG-PVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAI 139
Cdd:COG1047  81 QFPEDEELEVGMQVEFQTPDGqEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-148 6.47e-16

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 71.28  E-value: 6.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 475995      1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSA-PLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRV 79
Cdd:PRK15095   3 ESVQSNSAVLVHFTLKLDDGSTAESTRNNGkPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQYF 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 475995     80 PKDVFMGVDELQVG--MRFLAeTDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELA 148
Cdd:PRK15095  83 SRRDFMDAGEPEIGaiMLFTA-MDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEAVHA 152
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-70 6.24e-05

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 40.26  E-value: 6.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 475995       2 KVAKDLVVSLAYQVRTEDGVLVDES-----PVSAPLdylhGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQ 70
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSydrgkPFEFTL----GSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-69 4.28e-03

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 35.54  E-value: 4.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 475995     2 KVAKDLVVSLAYQVRTEDGVLVDES-----PVSAPLdylhGHGSLISGLETALEGHEVGDKFDVAVGANDAYG 69
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSydrgePATFPL----GVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYG 81
 
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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