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Conserved domains on  [gi|515672066|ref|WP_017104666|]
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MULTISPECIES: peptidylprolyl isomerase [Vibrio]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 139723)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755
SCOP:  4001062

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FKBP_C super family cl19519
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-157 1.90e-71

FKBP-type peptidyl-prolyl cis-trans isomerase;


The actual alignment was detected with superfamily member PRK10737:

Pssm-ID: 473184  Cd Length: 196  Bit Score: 215.19  E-value: 1.90e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066   1 MKIEKNVVVSVAYQVKLEDGVVVDQSTAEAPLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGDHNDDLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515672066  81 ADVFQGVEQIEVGMRFLADTDQGPIPVEVTEVDGDEVVVDGNHMLAGQTLTFDVEVVAVREATEEEVQHGHVHQEGG 157
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHD 157
 
Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-157 1.90e-71

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 215.19  E-value: 1.90e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066   1 MKIEKNVVVSVAYQVKLEDGVVVDQSTAEAPLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGDHNDDLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515672066  81 ADVFQGVEQIEVGMRFLADTDQGPIPVEVTEVDGDEVVVDGNHMLAGQTLTFDVEVVAVREATEEEVQHGHVHQEGG 157
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHD 157
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
3-139 4.10e-58

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 179.14  E-value: 4.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066   3 IEKNVVVSVAYQVKLEDGVVVDQSTAEAPLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGDHNDDLVQRVPAD 82
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPRE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515672066  83 VFQGVEQIEVGMRFLADTDQG-PIPVEVTEVDGDEVVVDGNHMLAGQTLTFDVEVVAV 139
Cdd:COG1047   81 QFPEDEELEVGMQVEFQTPDGqEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-70 7.39e-07

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 45.65  E-value: 7.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066    2 KIEKNVVVSVAYQVKLEDGVVVDQSTAEA-PLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGD 70
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
 
Name Accession Description Interval E-value
PRK10737 PRK10737
peptidylprolyl isomerase;
1-157 1.90e-71

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 215.19  E-value: 1.90e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066   1 MKIEKNVVVSVAYQVKLEDGVVVDQSTAEAPLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGDHNDDLVQRVP 80
Cdd:PRK10737   1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515672066  81 ADVFQGVEQIEVGMRFLADTDQGPIPVEVTEVDGDEVVVDGNHMLAGQTLTFDVEVVAVREATEEEVQHGHVHQEGG 157
Cdd:PRK10737  81 KDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHD 157
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
3-139 4.10e-58

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 179.14  E-value: 4.10e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066   3 IEKNVVVSVAYQVKLEDGVVVDQSTAEAPLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGDHNDDLVQRVPAD 82
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPRE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515672066  83 VFQGVEQIEVGMRFLADTDQG-PIPVEVTEVDGDEVVVDGNHMLAGQTLTFDVEVVAV 139
Cdd:COG1047   81 QFPEDEELEVGMQVEFQTPDGqEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-146 1.26e-23

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 91.69  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066   1 MKIEKNVVVSVAYQVKLEDGVVVDQSTAEA-PLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGDHNDDLVQRV 79
Cdd:PRK15095   3 ESVQSNSAVLVHFTLKLDDGSTAESTRNNGkPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQYF 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515672066  80 PADVF--QGVEQIEVGMRFLAdTDQGPIPVEVTEVDGDEVVVDGNHMLAGQTLTFDVEVVAVREATEEE 146
Cdd:PRK15095  83 SRRDFmdAGEPEIGAIMLFTA-MDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEAV 150
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-70 7.39e-07

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 45.65  E-value: 7.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672066    2 KIEKNVVVSVAYQVKLEDGVVVDQSTAEA-PLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGD 70
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
8-70 8.32e-05

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 40.17  E-value: 8.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515672066   8 VVSVAYQVKLEDGVVVDQSTAE-APLDYLHGHNNLITGLEKELEGKVAGDKFSATVTPEDAYGD 70
Cdd:COG0545   19 TVTVHYTGTLLDGTVFDSSYDRgEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
 
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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