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Conserved domains on  [gi|965468|gb|AAC37581|]
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calcineurin [Homo sapiens]

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;
13-105 2.43e-43

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 136.56  E-value: 2.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468      13 GRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 965468      92 IPPNATLIFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 2.43e-43

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 136.56  E-value: 2.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468      13 GRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 965468      92 IPPNATLIFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-106 3.69e-43

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 136.08  E-value: 3.69e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468     3 VEIETISPGDGRTfPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 965468    83 YGATGHPGVIPPNATLIFDVELLN 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
10-108 3.02e-26

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 97.91  E-value: 3.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468     10 PGDGRTfPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIgkQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHP 89
Cdd:PRK10902 155 EGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                         90
                 ....*....|....*....
gi 965468     90 GvIPPNATLIFDVELLNLE 108
Cdd:PRK10902 232 G-IPANSTLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 2.43e-43

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 136.56  E-value: 2.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468      13 GRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 965468      92 IPPNATLIFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-106 3.69e-43

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 136.08  E-value: 3.69e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468     3 VEIETISPGDGRTfPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 965468    83 YGATGHPGVIPPNATLIFDVELLN 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
10-108 3.02e-26

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 97.91  E-value: 3.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468     10 PGDGRTfPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIgkQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHP 89
Cdd:PRK10902 155 EGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                         90
                 ....*....|....*....
gi 965468     90 GvIPPNATLIFDVELLNLE 108
Cdd:PRK10902 232 G-IPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
2-107 1.30e-18

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 76.76  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468      2 GVEIETISPGDGrTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKqeVIKGFEEGAAQMSLGQRAKLTCTPDV 81
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                         90       100
                 ....*....|....*....|....*.
gi 965468     82 AYGATGHPGVIPPNATLIFDVELLNL 107
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
18-104 1.55e-12

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: 1.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 965468    18 KKGQTCVVHYTGMLQNGKKFDSSRDRnKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGatghpgviPPNAT 97
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72

                ....*..
gi 965468    98 LIFDVEL 104
Cdd:COG1047  73 LVQTVPR 79
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
25-99 9.22e-07

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 44.70  E-value: 9.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 965468     25 VHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGatghpgviPPNATLI 99
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG--------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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