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Conserved domains on  [gi|1148626637|ref|WP_077371771|]
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MULTISPECIES: peptidylprolyl isomerase [Cobetia]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11437275)

FKBP-type peptidyl-prolyl cis-trans isomerase catalyzes the cis-trans isomerization of Xaa-Pro bonds of peptides, accelerating slow steps of protein folding and shortening the lifetime of intermediates

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0046872|GO:0006457|GO:0003755
SCOP:  4001062

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
8-138 4.11e-59

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


:

Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 180.30  E-value: 4.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626637   8 VVSLHYTLRTADGTVLDTSRDREPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEGLVQYFGRDAFGPG 87
Cdd:COG1047     6 VVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPREQFPED 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1148626637  88 -ELAPGMRFQARTPEGQ-RSVTVLEVGDQQVKVDANHPLAGQALSWDVEVLEV 138
Cdd:COG1047    86 eELEVGMQVEFQTPDGQeVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
 
Name Accession Description Interval E-value
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
8-138 4.11e-59

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 180.30  E-value: 4.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626637   8 VVSLHYTLRTADGTVLDTSRDREPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEGLVQYFGRDAFGPG 87
Cdd:COG1047     6 VVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPREQFPED 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1148626637  88 -ELAPGMRFQARTPEGQ-RSVTVLEVGDQQVKVDANHPLAGQALSWDVEVLEV 138
Cdd:COG1047    86 eELEVGMQVEFQTPDGQeVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
PRK10737 PRK10737
peptidylprolyl isomerase;
1-153 1.87e-40

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 135.07  E-value: 1.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626637   1 MSITVQQVVSLHYTLRTADGTVLDTSRDREPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEGLVQYFG 80
Cdd:PRK10737    1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626637  81 RDAF-GPGELAPGMRFQARTPEGQRSVTVLEVGDQQVKVDANHPLAGQALSWDVEVLEVRDATRAELAAGHPLG 153
Cdd:PRK10737   81 KDVFmGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHG 154
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
7-72 4.83e-10

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 53.35  E-value: 4.83e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626637   7 QVVSLHYTLRTADGTVLDTSRDR-EPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERD 72
Cdd:pfam00254   9 DRVTVHYTGTLEDGTVFDSSYDRgKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEG 75
 
Name Accession Description Interval E-value
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
8-138 4.11e-59

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 180.30  E-value: 4.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626637   8 VVSLHYTLRTADGTVLDTSRDREPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEGLVQYFGRDAFGPG 87
Cdd:COG1047     6 VVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPREQFPED 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1148626637  88 -ELAPGMRFQARTPEGQ-RSVTVLEVGDQQVKVDANHPLAGQALSWDVEVLEV 138
Cdd:COG1047    86 eELEVGMQVEFQTPDGQeVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
PRK10737 PRK10737
peptidylprolyl isomerase;
1-153 1.87e-40

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 135.07  E-value: 1.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626637   1 MSITVQQVVSLHYTLRTADGTVLDTSRDREPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEGLVQYFG 80
Cdd:PRK10737    1 MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626637  81 RDAF-GPGELAPGMRFQARTPEGQRSVTVLEVGDQQVKVDANHPLAGQALSWDVEVLEVRDATRAELAAGHPLG 153
Cdd:PRK10737   81 KDVFmGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHG 154
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-138 1.43e-24

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 92.85  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626637   1 MSITVQ--QVVSLHYTLRTADGTVLDTSRDR-EPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEGLVQ 77
Cdd:PRK15095    1 MSESVQsnSAVLVHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQ 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626637  78 YFGRDAF---GPGELAPGMRFQARTPEGQRSVtVLEVGDQQVKVDANHPLAGQALSWDVEVLEV 138
Cdd:PRK15095   81 YFSRRDFmdaGEPEIGAIMLFTAMDGSEMPGV-IREINGDSITVDFNHPLAGQTVHFDIEVLEI 143
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
7-72 4.83e-10

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 53.35  E-value: 4.83e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626637   7 QVVSLHYTLRTADGTVLDTSRDR-EPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERD 72
Cdd:pfam00254   9 DRVTVHYTGTLEDGTVFDSSYDRgKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEG 75
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-74 8.18e-07

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 45.17  E-value: 8.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148626637   2 SITVQQVVSLHYTLRTADGTVLDTSRDR-EPMDYLHGHDNILAALESALEGCSVGDSKVVNLTPAEGFGERDEG 74
Cdd:COG0545    13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRgEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAG 86
 
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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