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Conserved domains on  [gi|224809331|ref|NP_001139249|]
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peptidyl-prolyl cis-trans isomerase FKBP5 isoform 2 [Homo sapiens]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446751)

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 pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
43-135 1.76e-42

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 140.41  E-value: 1.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331   43 GEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLP-K 121
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80
                          90
                  ....*....|....
gi 224809331  122 IPSNATLFFEIELL 135
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C super family cl19519
FKBP-type peptidyl-prolyl cis-trans isomerase;
158-221 5.00e-06

FKBP-type peptidyl-prolyl cis-trans isomerase;


The actual alignment was detected with superfamily member pfam00254:

Pssm-ID: 473184  Cd Length: 94  Bit Score: 44.11  E-value: 5.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  158 GYSNPNEGATVEIHLEGRC-GGRMFDC-----RDVAFTVGEGEdhdIPIGIDKALEKMQREEQCILYLGP 221
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLeDGTVFDSsydrgKPFEFTLGSGQ---VIPGWDEGLVGMKVGEKRKLTIPP 67
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
43-135 1.76e-42

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 140.41  E-value: 1.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331   43 GEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLP-K 121
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80
                          90
                  ....*....|....
gi 224809331  122 IPSNATLFFEIELL 135
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
36-137 2.56e-41

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 137.62  E-value: 2.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  36 IVKRVGNGEEtPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGS 115
Cdd:COG0545    4 KVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                         90       100
                 ....*....|....*....|..
gi 224809331 116 AGSLPKIPSNATLFFEIELLDF 137
Cdd:COG0545   83 RGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
7-138 8.12e-27

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 104.85  E-value: 8.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331   7 AKNNEESPTATVAEQGEDITSKK-DRGVLKIVKRVGNGEeTPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLgKGq 85
Cdd:PRK10902 121 AADNEAKGKKYREKFAKEKGVKTtSTGLLYKVEKEGTGE-APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL-DG- 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224809331  86 VIKAWDIGVATMKKGEICHLLCKPEYAYGSAGsLPKIPSNATLFFEIELLDFK 138
Cdd:PRK10902 198 VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAG-VPGIPANSTLVFDVELLDVK 249
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
158-221 5.00e-06

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 44.11  E-value: 5.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  158 GYSNPNEGATVEIHLEGRC-GGRMFDC-----RDVAFTVGEGEdhdIPIGIDKALEKMQREEQCILYLGP 221
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLeDGTVFDSsydrgKPFEFTLGSGQ---VIPGWDEGLVGMKVGEKRKLTIPP 67
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
43-135 1.76e-42

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 140.41  E-value: 1.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331   43 GEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLP-K 121
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80
                          90
                  ....*....|....
gi 224809331  122 IPSNATLFFEIELL 135
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
36-137 2.56e-41

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 137.62  E-value: 2.56e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  36 IVKRVGNGEEtPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGS 115
Cdd:COG0545    4 KVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                         90       100
                 ....*....|....*....|..
gi 224809331 116 AGSLPKIPSNATLFFEIELLDF 137
Cdd:COG0545   83 RGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
7-138 8.12e-27

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 104.85  E-value: 8.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331   7 AKNNEESPTATVAEQGEDITSKK-DRGVLKIVKRVGNGEeTPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLgKGq 85
Cdd:PRK10902 121 AADNEAKGKKYREKFAKEKGVKTtSTGLLYKVEKEGTGE-APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL-DG- 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224809331  86 VIKAWDIGVATMKKGEICHLLCKPEYAYGSAGsLPKIPSNATLFFEIELLDFK 138
Cdd:PRK10902 198 VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAG-VPGIPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
47-136 7.03e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 65.97  E-value: 7.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  47 PMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKgqVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNA 126
Cdd:PRK11570 117 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFS 194
                         90
                 ....*....|
gi 224809331 127 TLFFEIELLD 136
Cdd:PRK11570 195 TLVFEVELLE 204
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
50-150 3.95e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 59.34  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  50 GDKVYVHYKGKLSNGKKFDSSHDRnEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGsagslpkiPSNATLF 129
Cdd:COG1047    4 GDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPELV 74
                         90       100
                 ....*....|....*....|.
gi 224809331 130 FEIELLDFKGEDLFEDGGIIR 150
Cdd:COG1047   75 QTVPREQFPEDEELEVGMQVE 95
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
158-221 5.00e-06

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 44.11  E-value: 5.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224809331  158 GYSNPNEGATVEIHLEGRC-GGRMFDC-----RDVAFTVGEGEdhdIPIGIDKALEKMQREEQCILYLGP 221
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLeDGTVFDSsydrgKPFEFTLGSGQ---VIPGWDEGLVGMKVGEKRKLTIPP 67
 
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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