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Conserved domains on  [gi|61557297|ref|NP_001013228|]
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peptidyl-prolyl cis-trans isomerase FKBP14 precursor [Rattus norvegicus]

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 1.70e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 120.38  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297    38 CHRKTKGGDLMLVHYEGYLEkDGSLFHSTHKhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGK- 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYD--RGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLa 77

                          90
                  ....*....|....*..
gi 61557297   117 -GKIPPESTLIFNIDLL 132
Cdd:pfam00254  78 gPVIPPNATLVFEVELL 94
EF-hand_7 pfam13499
EF-hand domain pair;
141-204 3.59e-05

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 3.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61557297   141 HESFQEMDLNDDWKLSKHEVKVYLQNEFEkhgavvNESHHDALVEDIFDKEDEDKDGFISAREF 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 1.70e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 120.38  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297    38 CHRKTKGGDLMLVHYEGYLEkDGSLFHSTHKhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGK- 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYD--RGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLa 77

                          90
                  ....*....|....*..
gi 61557297   117 -GKIPPESTLIFNIDLL 132
Cdd:pfam00254  78 gPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 43-134 6.76e-35

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 119.13  E-value: 6.76e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297  43 KGGDLMLVHYEGYLEkDGSLFHSTHKHnnGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGKG-KIPP 121
Cdd:COG0545  15 KAGDTVTVHYTGTLL-DGTVFDSSYDR--GEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGgVIPP 91

                        90
                ....*....|...
gi 61557297 122 ESTLIFNIDLLEI 134
Cdd:COG0545  92 NSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 43-140 2.70e-18

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 80.58  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297   43 KGGDLMLVHYEGYLeKDGSLFHSTHKHnnGQPVWFTLGilEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGKGKIPPE 122
Cdd:PRK10902 162 KDSDTVVVNYKGTL-IDGKEFDNSYTR--GEPLSFRLD--GVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPAN 236

                         90
                 ....*....|....*...
gi 61557297  123 STLIFNIDLLEIRNGPRS 140
Cdd:PRK10902 237 STLVFDVELLDVKPAPKA 254
EF-hand_7 pfam13499
EF-hand domain pair;
141-204 3.59e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 3.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61557297   141 HESFQEMDLNDDWKLSKHEVKVYLQNEFEkhgavvNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEE------GEPLSDEEVEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
115-204 5.69e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 5.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297 115 GKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWKLSKhevkvylqNEFEKHGAVVNEShhDALVEDIFDKEDED 194
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISA--------DEFRRLLTALGVS--EEEADELFARLDTD 115

                        90
                ....*....|
gi 61557297 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 1.35e-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: 1.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557297 142 ESFQEMDLNDDWKLSKHEVKVYLQnefekhgaVVNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALK--------SLGEGLSEEEIDEMIREVDKDGDGKIDFEEF 58
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
38-132 1.70e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 120.38  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297    38 CHRKTKGGDLMLVHYEGYLEkDGSLFHSTHKhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGK- 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYD--RGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLa 77

                          90
                  ....*....|....*..
gi 61557297   117 -GKIPPESTLIFNIDLL 132
Cdd:pfam00254  78 gPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 43-134 6.76e-35

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 119.13  E-value: 6.76e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297  43 KGGDLMLVHYEGYLEkDGSLFHSTHKHnnGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGKG-KIPP 121
Cdd:COG0545  15 KAGDTVTVHYTGTLL-DGTVFDSSYDR--GEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGgVIPP 91

                        90
                ....*....|...
gi 61557297 122 ESTLIFNIDLLEI 134
Cdd:COG0545  92 NSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 43-140 2.70e-18

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 80.58  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297   43 KGGDLMLVHYEGYLeKDGSLFHSTHKHnnGQPVWFTLGilEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGKGKIPPE 122
Cdd:PRK10902 162 KDSDTVVVNYKGTL-IDGKEFDNSYTR--GEPLSFRLD--GVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPAN 236

                         90
                 ....*....|....*...
gi 61557297  123 STLIFNIDLLEIRNGPRS 140
Cdd:PRK10902 237 STLVFDVELLDVKPAPKA 254
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 46-134 4.00e-16

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 73.29  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297   46 DLMLVHYEGYLeKDGSLFHSTHKHnnGQPVWFTLGilEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKEGKG-KIPPEST 124
Cdd:PRK11570 121 DRVRVHYTGKL-IDGTVFDSSVAR--GEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFST 195

                         90
                 ....*....|
gi 61557297  125 LIFNIDLLEI 134
Cdd:PRK11570 196 LVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 45-112 2.24e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.96  E-value: 2.24e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61557297  45 GDLMLVHYEGYLEkDGSLFHSTHkhnNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYG 112
Cdd:COG1047   4 GDVVTLHYTLKLE-DGEVFDSTF---EGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 49-114 3.07e-07

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 48.16  E-value: 3.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61557297   49 LVHYEGYLEkDGSLFHSTHkhNNGQPVWFTLGILEVLKGWDQGLKGMCVGEKRKLTIPPALGYGKE 114
Cdd:PRK15095  12 LVHFTLKLD-DGSTAESTR--NNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
EF-hand_7 pfam13499
EF-hand domain pair;
141-204 3.59e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 3.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61557297   141 HESFQEMDLNDDWKLSKHEVKVYLQNEFEkhgavvNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEE------GEPLSDEEVEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
115-204 5.69e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 5.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557297 115 GKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWKLSKhevkvylqNEFEKHGAVVNEShhDALVEDIFDKEDED 194
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISA--------DEFRRLLTALGVS--EEEADELFARLDTD 115

                        90
                ....*....|
gi 61557297 195 KDGFISAREF 204
Cdd:COG5126 116 GDGKISFEEF 125
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
144-205 7.85e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.32  E-value: 7.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61557297 144 FQEMDLNDDWKLSKHEVKVYLQNEFEKHGAvvneshhdALVEDIFDKEDEDKDGFISAREFT 205
Cdd:COG5126  39 FSEADTDGDGRISREEFVAGMESLFEATVE--------PFARAAFDLLDTDGDGKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 142-204 1.35e-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: 1.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557297 142 ESFQEMDLNDDWKLSKHEVKVYLQnefekhgaVVNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALK--------SLGEGLSEEEIDEMIREVDKDGDGKIDFEEF 58
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 151-204 8.13e-03

S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. As is the case with many other members of S100 protein family, S100A1 is implicated in intracellular and extracellular regulatory activities, including interaction with myosin-associated twitchin kinase, actin-capping protein CapZ, sinapsin I, and tubulin. Structural data suggests that S100A1 proteins exist within cells as antiparallel homodimers, while heterodimers with S100A4 and S100B also has been reported. Upon binding calcium S100A1 changes conformation to expose a hydrophobic cleft which is the interaction site of S100A1 with its more that 20 known target proteins.


Pssm-ID: 240152 [Multi-domain]  Cd Length: 92  Bit Score: 34.48  E-value: 8.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 61557297 151 DDWKLSKHEVKVYLQNEFekhGAVVNESHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:cd05025  24 DKYKLSKKELKDLLQTEL---SDFLDAQKDADAVDKIMKELDENGDGEVDFQEF 74
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 139-204 8.41e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 36.41  E-value: 8.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61557297 139 RSHESFQEMDLNDDWKLSKHEVKVYLQNEFEKHgavvnesHHDALVEDIFDKEDEDKDGFISAREF 204
Cdd:cd16226 120 RDERRWKAADQDGDGKLTKEEFTAFLHPEEFPH-------MRDIVVQETLEDIDKNKDGFISLEEY 178
 
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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