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Conserved domains on  [gi|1820395062|ref|NP_001365745|]
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peptidyl-prolyl cis-trans isomerase FKBP1B isoform 2 [Mus musculus]

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;
18-94 1.26e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 121.53  E-value: 1.26e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820395062 18 GMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGH-PGVIPPNATLIFDVELL 94
Cdd:pfam00254 17 GTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIPPNATLVFEVELL 94
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
18-94 1.26e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 121.53  E-value: 1.26e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820395062 18 GMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGH-PGVIPPNATLIFDVELL 94
Cdd:pfam00254 17 GTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 18-95 3.03e-35

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 115.66  E-value: 3.03e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820395062  18 GMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLS 95
Cdd:COG0545    26 GTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 18-97 1.27e-21

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 85.20  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820395062  18 GMLQNGKKFDSSRDRNKPFKFRIgkQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGvIPPNATLIFDVELLSLE 97
Cdd:PRK10902  173 GTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
18-94 1.26e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 121.53  E-value: 1.26e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820395062 18 GMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGH-PGVIPPNATLIFDVELL 94
Cdd:pfam00254 17 GTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 18-95 3.03e-35

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 115.66  E-value: 3.03e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820395062  18 GMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLS 95
Cdd:COG0545    26 GTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 18-97 1.27e-21

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 85.20  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820395062  18 GMLQNGKKFDSSRDRNKPFKFRIgkQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGvIPPNATLIFDVELLSLE 97
Cdd:PRK10902  173 GTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 16-96 2.67e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 62.12  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820395062  16 WIGMLQNGKKFDSSRDRNKPFKFRIGKqeVIKGFEEGTAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLS 95
Cdd:PRK11570  127 YTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLE 204


                  .
gi 1820395062  96 L 96
Cdd:PRK11570  205 I 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 14-93 5.06e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 52.41  E-value: 5.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820395062  14 LTWIGMLQNGKKFDSSRDRnKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGatghpgviPPNATLIFDVEL 93
Cdd:COG1047     9 LHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPELVQTVPR 79
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 13-88 7.59e-05

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 38.92  E-value: 7.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820395062  13 LLTWIGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGTAQMSLGQRAKLTCTPDVAYGatghpgviPPNATLI 88
Cdd:PRK15095   12 LVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG--------VPSPDLI 79
 
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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