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Conserved domains on  [gi|499457344|ref|WP_011144808|]
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MULTISPECIES: peptidylprolyl isomerase [Photorhabdus]

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;
1-153 2.02e-98

peptidylprolyl isomerase;


:

Pssm-ID: 236748  Cd Length: 196  Bit Score: 282.99  E-value: 2.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499457344   1 MKVAKDLVVSLAYQVRTEDGVLVDESPASAPLDYLHGRGSLISGLEKALEGREAGESFDVSVQADDAYGQYDDNLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499457344  81 KDVFVGVDELEVGMRFLADTDMGPVPVEITAVEGEHVVVDGNHMLAGQNLKFNVEVIAIREATEEELAHGHVH 153
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVH 153
 
Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-153 2.02e-98

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 282.99  E-value: 2.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499457344   1 MKVAKDLVVSLAYQVRTEDGVLVDESPASAPLDYLHGRGSLISGLEKALEGREAGESFDVSVQADDAYGQYDDNLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499457344  81 KDVFVGVDELEVGMRFLADTDMGPVPVEITAVEGEHVVVDGNHMLAGQNLKFNVEVIAIREATEEELAHGHVH 153
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVH 153
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
3-139 5.01e-54

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 168.36  E-value: 5.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499457344   3 VAKDLVVSLAYQVRTEDGVLVDESPASAPLDYLHGRGSLISGLEKALEGREAGESFDVSVQADDAYGQYDDNLVQRVPKD 82
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPRE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499457344  83 VFVGVDELEVGMRFLADTDMG-PVPVEITAVEGEHVVVDGNHMLAGQNLKFNVEVIAI 139
Cdd:COG1047   81 QFPEDEELEVGMQVEFQTPDGqEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-70 6.48e-05

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 40.26  E-value: 6.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499457344    2 KVAKDLVVSLAYQVRTEDGVLVDES-----PASAPLdylhGRGSLISGLEKALEGREAGESFDVSVQADDAYGQ 70
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSydrgkPFEFTL----GSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
 
Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-153 2.02e-98

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 282.99  E-value: 2.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499457344   1 MKVAKDLVVSLAYQVRTEDGVLVDESPASAPLDYLHGRGSLISGLEKALEGREAGESFDVSVQADDAYGQYDDNLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499457344  81 KDVFVGVDELEVGMRFLADTDMGPVPVEITAVEGEHVVVDGNHMLAGQNLKFNVEVIAIREATEEELAHGHVH 153
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVH 153
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
3-139 5.01e-54

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 168.36  E-value: 5.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499457344   3 VAKDLVVSLAYQVRTEDGVLVDESPASAPLDYLHGRGSLISGLEKALEGREAGESFDVSVQADDAYGQYDDNLVQRVPKD 82
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPRE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499457344  83 VFVGVDELEVGMRFLADTDMG-PVPVEITAVEGEHVVVDGNHMLAGQNLKFNVEVIAI 139
Cdd:COG1047   81 QFPEDEELEVGMQVEFQTPDGqEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-146 4.07e-17

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 74.36  E-value: 4.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499457344   1 MKVAKDLVVSLAYQVRTEDGVLVDESPASA-PLDYLHGRGSLISGLEKALEGREAGESFDVSVQADDAYGQYDDNLVQRV 79
Cdd:PRK15095   3 ESVQSNSAVLVHFTLKLDDGSTAESTRNNGkPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQYF 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499457344  80 PKDVFVGVDELEVG--MRFLAdTDMGPVPVEITAVEGEHVVVDGNHMLAGQNLKFNVEVIAIREATEEE 146
Cdd:PRK15095  83 SRRDFMDAGEPEIGaiMLFTA-MDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEAV 150
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-70 6.48e-05

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 40.26  E-value: 6.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499457344    2 KVAKDLVVSLAYQVRTEDGVLVDES-----PASAPLdylhGRGSLISGLEKALEGREAGESFDVSVQADDAYGQ 70
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSydrgkPFEFTL----GSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-69 6.16e-03

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 34.77  E-value: 6.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499457344   2 KVAKDLVVSLAYQVRTEDGVLVDES-----PASAPLdylhGRGSLISGLEKALEGREAGESFDVSVQADDAYG 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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