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Conserved domains on  [gi|23956366|ref|NP_705801|]
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peptidyl-prolyl cis-trans isomerase FKBP14 isoform 1 precursor [Mus musculus]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11991627)

FKBP-type peptidyl-prolyl cis-trans isomerase, with EF-hand calcium binding motifs, acts as a PPIase that accelerates the folding of proteins; similar to Mus musculus peptidyl-prolyl cis-trans isomerase FKBP14

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;
38-132 4.62e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 119.22  E-value: 4.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366    38 CHRKTKGGDLMLVHYEGYLEkDGSLFHSTHKhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGK- 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYD--RGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLa 77
                          90
                  ....*....|....*..
gi 23956366   117 -GKIPPESTLIFNIDLL 132
Cdd:pfam00254  78 gPVIPPNATLVFEVELL 94
EF-hand_7 pfam13499
EF-hand domain pair;
141-204 3.77e-05

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 3.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956366   141 HESFQEMDLNDDWRLSKHEVKVYLQKEFEkhgavvNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEE------GEPLSDEEVEELFKEFDLDKDGRISFEEF 62
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
38-132 4.62e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 119.22  E-value: 4.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366    38 CHRKTKGGDLMLVHYEGYLEkDGSLFHSTHKhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGK- 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYD--RGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLa 77
                          90
                  ....*....|....*..
gi 23956366   117 -GKIPPESTLIFNIDLL 132
Cdd:pfam00254  78 gPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
43-134 2.80e-34

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 117.59  E-value: 2.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366  43 KGGDLMLVHYEGYLEkDGSLFHSTHKHnnGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGKG-KIPP 121
Cdd:COG0545  15 KAGDTVTVHYTGTLL-DGTVFDSSYDR--GEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGgVIPP 91
                        90
                ....*....|...
gi 23956366 122 ESTLIFNIDLLEI 134
Cdd:COG0545  92 NSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
43-140 1.31e-17

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366   43 KGGDLMLVHYEGYLeKDGSLFHSTHKHnnGQPVWFTLGilEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGKGKIPPE 122
Cdd:PRK10902 162 KDSDTVVVNYKGTL-IDGKEFDNSYTR--GEPLSFRLD--GVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPAN 236
                         90
                 ....*....|....*...
gi 23956366  123 STLIFNIDLLEIRNGPRS 140
Cdd:PRK10902 237 STLVFDVELLDVKPAPKA 254
EF-hand_7 pfam13499
EF-hand domain pair;
141-204 3.77e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 3.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956366   141 HESFQEMDLNDDWRLSKHEVKVYLQKEFEkhgavvNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEE------GEPLSDEEVEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
115-204 6.65e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 6.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366 115 GKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWRLSKHEVKVYLqkefEKHGAvvneshHDALVEDIFDKEDED 194
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----TALGV------SEEEADELFARLDTD 115
                        90
                ....*....|
gi 23956366 195 KDGFISAREF 204
Cdd:COG5126 116 GDGKISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
142-204 1.13e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 1.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956366 142 ESFQEMDLNDDWRLSKHEVKVYLQKEFEKHGavvneshhDALVEDIFDKEDEDKDGFISAREF 204
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLS--------EEEIDEMIREVDKDGDGKIDFEEF 58
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
38-132 4.62e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 119.22  E-value: 4.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366    38 CHRKTKGGDLMLVHYEGYLEkDGSLFHSTHKhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGK- 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYD--RGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLa 77
                          90
                  ....*....|....*..
gi 23956366   117 -GKIPPESTLIFNIDLL 132
Cdd:pfam00254  78 gPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
43-134 2.80e-34

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 117.59  E-value: 2.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366  43 KGGDLMLVHYEGYLEkDGSLFHSTHKHnnGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGKG-KIPP 121
Cdd:COG0545  15 KAGDTVTVHYTGTLL-DGTVFDSSYDR--GEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGgVIPP 91
                        90
                ....*....|...
gi 23956366 122 ESTLIFNIDLLEI 134
Cdd:COG0545  92 NSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
43-140 1.31e-17

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366   43 KGGDLMLVHYEGYLeKDGSLFHSTHKHnnGQPVWFTLGilEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGKGKIPPE 122
Cdd:PRK10902 162 KDSDTVVVNYKGTL-IDGKEFDNSYTR--GEPLSFRLD--GVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPAN 236
                         90
                 ....*....|....*...
gi 23956366  123 STLIFNIDLLEIRNGPRS 140
Cdd:PRK10902 237 STLVFDVELLDVKPAPKA 254
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
46-134 1.42e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 72.14  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366   46 DLMLVHYEGYLeKDGSLFHSTHKHnnGQPVWFTLGilEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKEGKG-KIPPEST 124
Cdd:PRK11570 121 DRVRVHYTGKL-IDGTVFDSSVAR--GEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFST 195
                         90
                 ....*....|
gi 23956366  125 LIFNIDLLEI 134
Cdd:PRK11570 196 LVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
45-112 4.16e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.57  E-value: 4.16e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956366  45 GDLMLVHYEGYLEkDGSLFHSTHkhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYG 112
Cdd:COG1047   4 GDVVTLHYTLKLE-DGEVFDSTF---EGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
49-114 3.97e-07

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 47.78  E-value: 3.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956366   49 LVHYEGYLEkDGSLFHSTHkhNNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTVPPALGYGKE 114
Cdd:PRK15095  12 LVHFTLKLD-DGSTAESTR--NNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
EF-hand_7 pfam13499
EF-hand domain pair;
141-204 3.77e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 3.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956366   141 HESFQEMDLNDDWRLSKHEVKVYLQKEFEkhgavvNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEE------GEPLSDEEVEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
115-204 6.65e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 6.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956366 115 GKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWRLSKHEVKVYLqkefEKHGAvvneshHDALVEDIFDKEDED 194
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----TALGV------SEEEADELFARLDTD 115
                        90
                ....*....|
gi 23956366 195 KDGFISAREF 204
Cdd:COG5126 116 GDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
144-205 1.14e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 1.14e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956366 144 FQEMDLNDDWRLSKhevkvylqKEFEKHGAVVNESHHDALVEDIFDKEDEDKDGFISAREFT 205
Cdd:COG5126  39 FSEADTDGDGRISR--------EEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
142-204 1.13e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 1.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956366 142 ESFQEMDLNDDWRLSKHEVKVYLQKEFEKHGavvneshhDALVEDIFDKEDEDKDGFISAREF 204
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEGLS--------EEEIDEMIREVDKDGDGKIDFEEF 58
 
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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