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Conserved domains on  [gi|157833731|pdb|1ROU|A]
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Chain A, FKBP59-I

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446594)

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|GO:0000413|GO:0061077
PubMed:  27664121
SCOP:  4001062

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-133 1.66e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A         42 GTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGSAGS-PPK 120
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|...
1ROU_A        121 IPPNATLVFEVEL 133
Cdd:pfam00254  81 IPPNATLVFEVEL 93
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-133 1.66e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A         42 GTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGSAGS-PPK 120
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|...
1ROU_A        121 IPPNATLVFEVEL 133
Cdd:pfam00254  81 IPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
35-133 6.67e-43

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 137.24  E-value: 6.67e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A       35 VIKREGTGtETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGS 114
Cdd:COG0545   4 KVLKEGTG-AKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                        90
                ....*....|....*....
1ROU_A      115 AGSPPKIPPNATLVFEVEL 133
Cdd:COG0545  83 RGAGGVIPPNSTLVFEVEL 101
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
27-137 7.67e-22

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 87.90  E-value: 7.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A        27 KQDEGVLKVIKREGTGtETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKgeVIKAWDIAVATMKVGELCRITC 106
Cdd:PRK10902 143 TTSTGLLYKVEKEGTG-EAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVI 219
                         90       100       110
                 ....*....|....*....|....*....|.
1ROU_A       107 KPEYAYGSAGSpPKIPPNATLVFEVELFEFK 137
Cdd:PRK10902 220 PPELAYGKAGV-PGIPANSTLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-133 1.66e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A         42 GTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGSAGS-PPK 120
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|...
1ROU_A        121 IPPNATLVFEVEL 133
Cdd:pfam00254  81 IPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
35-133 6.67e-43

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 137.24  E-value: 6.67e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A       35 VIKREGTGtETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGS 114
Cdd:COG0545   4 KVLKEGTG-AKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                        90
                ....*....|....*....
1ROU_A      115 AGSPPKIPPNATLVFEVEL 133
Cdd:COG0545  83 RGAGGVIPPNSTLVFEVEL 101
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
27-137 7.67e-22

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 87.90  E-value: 7.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A        27 KQDEGVLKVIKREGTGtETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKgeVIKAWDIAVATMKVGELCRITC 106
Cdd:PRK10902 143 TTSTGLLYKVEKEGTG-EAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVI 219
                         90       100       110
                 ....*....|....*....|....*....|.
1ROU_A       107 KPEYAYGSAGSpPKIPPNATLVFEVELFEFK 137
Cdd:PRK10902 220 PPELAYGKAGV-PGIPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
46-135 6.11e-19

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 79.07  E-value: 6.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A        46 PMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKgeVIKAWDIAVATMKVGELCRITCKPEYAYGSAGSPPKIPPNA 125
Cdd:PRK11570 117 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFS 194
                         90
                 ....*....|
1ROU_A       126 TLVFEVELFE 135
Cdd:PRK11570 195 TLVFEVELLE 204
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
49-140 1.81e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 55.11  E-value: 1.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ROU_A       49 GDRVFVHYTGWLLDGTKFDSSLDRkDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGsagsppkiPPNATLV 128
Cdd:COG1047   4 GDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPELV 74
                        90
                ....*....|..
1ROU_A      129 FEVELFEFKGED 140
Cdd:COG1047  75 QTVPREQFPEDE 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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