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Conserved domains on  [gi|281363946|ref|NP_726074|]
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FK506-binding protein 14, isoform C [Drosophila melanogaster]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446598)

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;
37-130 7.63e-50

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 157.36  E-value: 7.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946   37 CEQKSKNGDSLTMHYTGTLQaDGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQG-AGN 115
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGP 79

                          90
                  ....*....|....*
gi 281363946  116 VIPPKATLLFDVELI 130
Cdd:pfam00254  80 VIPPNATLVFEVELL 94
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
142-208 2.74e-06

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946 142 FKEIDDNADKQLSREEVSEYLKKQMTAVEGQ-----------------DSEELKNMLAE---NDKLVEEIFQHEDKDKNG 201
Cdd:COG5126   39 FSEADTDGDGRISREEFVAGMESLFEATVEPfaraafdlldtdgdgkiSADEFRRLLTAlgvSEEEADELFARLDTDGDG 118


                 ....*..
gi 281363946 202 FISHDEF 208
Cdd:COG5126  119 KISFEEF 125
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
37-130 7.63e-50

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 157.36  E-value: 7.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946   37 CEQKSKNGDSLTMHYTGTLQaDGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQG-AGN 115
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGP 79

                          90
                  ....*....|....*
gi 281363946  116 VIPPKATLLFDVELI 130
Cdd:pfam00254  80 VIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 42-132 1.08e-48

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 154.57  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946  42 KNGDSLTMHYTGTLqADGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKA 121
Cdd:COG0545   15 KAGDTVTVHYTGTL-LDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                         90
                 ....*....|.
gi 281363946 122 TLLFDVELINI 132
Cdd:COG0545   94 TLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 45-132 1.90e-23

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 92.94  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946  45 DSLTMHYTGTLqADGKKFDSSFDRDQPFTFQLGAgqVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKATLL 124
Cdd:PRK11570 121 DRVRVHYTGKL-IDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 281363946 125 FDVELINI 132
Cdd:PRK11570 198 FEVELLEI 205
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
142-208 2.74e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946 142 FKEIDDNADKQLSREEVSEYLKKQMTAVEGQ-----------------DSEELKNMLAE---NDKLVEEIFQHEDKDKNG 201
Cdd:COG5126   39 FSEADTDGDGRISREEFVAGMESLFEATVEPfaraafdlldtdgdgkiSADEFRRLLTAlgvSEEEADELFARLDTDGDG 118


                 ....*..
gi 281363946 202 FISHDEF 208
Cdd:COG5126  119 KISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 141-208 3.75e-06

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: 42.92  E-value: 3.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363946 141 VFKEIDDNADKQLSREEVSEYLKKQMtavEGQDSEElknmlaendklVEEIFQHEDKDKNGFISHDEF 208
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALKSLG---EGLSEEE-----------IDEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
141-208 6.67e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 6.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363946  141 VFKEIDDNADKQLSREEVSEYLKKQMTAVEGQDSEelknmlaendklVEEIFQHEDKDKNGFISHDEF 208
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEE------------VEELFKEFDLDKDGRISFEEF 62
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
37-130 7.63e-50

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 157.36  E-value: 7.63e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946   37 CEQKSKNGDSLTMHYTGTLQaDGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQG-AGN 115
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGP 79

                          90
                  ....*....|....*
gi 281363946  116 VIPPKATLLFDVELI 130
Cdd:pfam00254  80 VIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 42-132 1.08e-48

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 154.57  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946  42 KNGDSLTMHYTGTLqADGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKA 121
Cdd:COG0545   15 KAGDTVTVHYTGTL-LDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNS 93

                         90
                 ....*....|.
gi 281363946 122 TLLFDVELINI 132
Cdd:COG0545   94 TLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 45-132 1.90e-23

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 92.94  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946  45 DSLTMHYTGTLqADGKKFDSSFDRDQPFTFQLGAgqVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNVIPPKATLL 124
Cdd:PRK11570 121 DRVRVHYTGKL-IDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 281363946 125 FDVELINI 132
Cdd:PRK11570 198 FEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 42-136 8.67e-23

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 92.90  E-value: 8.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946  42 KNGDSLTMHYTGTLqADGKKFDSSFDRDQPFTFQLGAgqVIKGWDQGLLNMCVGEKRKLTIPPQLGYGDQGAGNvIPPKA 121
Cdd:PRK10902 162 KDSDTVVVNYKGTL-IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANS 237

                         90
                 ....*....|....*
gi 281363946 122 TLLFDVELINIGNAP 136
Cdd:PRK10902 238 TLVFDVELLDVKPAP 252
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 42-110 2.63e-18

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 77.45  E-value: 2.63e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363946  42 KNGDSLTMHYTGTLqADGKKFDSSFDrDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYGD 110
Cdd:COG1047    2 EKGDVVTLHYTLKL-EDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
142-208 2.74e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946 142 FKEIDDNADKQLSREEVSEYLKKQMTAVEGQ-----------------DSEELKNMLAE---NDKLVEEIFQHEDKDKNG 201
Cdd:COG5126   39 FSEADTDGDGRISREEFVAGMESLFEATVEPfaraafdlldtdgdgkiSADEFRRLLTAlgvSEEEADELFARLDTDGDG 118


                 ....*..
gi 281363946 202 FISHDEF 208
Cdd:COG5126  119 KISFEEF 125
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 141-208 3.75e-06

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: 42.92  E-value: 3.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363946 141 VFKEIDDNADKQLSREEVSEYLKKQMtavEGQDSEElknmlaendklVEEIFQHEDKDKNGFISHDEF 208
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALKSLG---EGLSEEE-----------IDEMIREVDKDGDGKIDFEEF 58
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 42-109 3.78e-06

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 45.08  E-value: 3.78e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363946  42 KNGDSLTMHYTGTLQaDGKKFDSSFDRDQPFTFQLGAGQVIKGWDQGLLNMCVGEKRKLTIPPQLGYG 109
Cdd:PRK15095   6 QSNSAVLVHFTLKLD-DGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 140-208 3.91e-05

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 43.44  E-value: 3.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363946 140 NVFKEIDDNADKQLSREEVSEYLKKQMtavegqdSEELKNMLAENdklvEEIFQHEDKDKNGFISHDEF 208
Cdd:cd16225   38 EIFKKVDVNTDGFLSAEELEDWIMEKT-------QEHFQEAVEEN----EQIFKAVDTDKDGNVSWEEY 95
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 35-191 3.93e-05

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 43.58  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946  35 EVCEQKSKNGDSLTMHYTGTLqaDGKKFDSSFDRDqpFTFQLGAGQVIKGWDQGLLNMCVGEKR--KLTIPPqlgygDQG 112
Cdd:COG0544  152 VPVERAAEEGDRVTIDFEGTI--DGEEFEGGKAED--YSLELGSGSFIPGFEEQLVGMKAGEEKtfEVTFPE-----DYH 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946 113 AGNVIPPKATllFDVELINIgnappTTNVFKEIDDNADKQLS--------REEVSEYLKKQmtaVEGQDSEELKNMLAen 184
Cdd:COG0544  223 AEELAGKTAT--FKVTVKEV-----KEKELPELDDEFAKKLGefetleelKADIRENLERE---KKQRARAKLKDQVL-- 290


                 ....*..
gi 281363946 185 DKLVEEI 191
Cdd:COG0544  291 DALVENN 297
EF-hand_7 pfam13499
EF-hand domain pair;
141-208 6.67e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 6.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363946  141 VFKEIDDNADKQLSREEVSEYLKKQMTAVEGQDSEelknmlaendklVEEIFQHEDKDKNGFISHDEF 208
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEE------------VEELFKEFDLDKDGRISFEEF 62
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 188-208 5.79e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.53  E-value: 5.79e-03
                          10        20
                  ....*....|....*....|.
gi 281363946  188 VEEIFQHEDKDKNGFISHDEF 208
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEF 22
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 142-215 7.00e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 36.53  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363946 142 FKEIDDNADKQLSREEvseYLKKQMtaveGQDSEELKNMLAEND----KLVE---EIFQHEDKDKNGFISHDEFSGPKHD 214
Cdd:cd16227   78 FEEADEDGDGKVTWEE---YLADSF----GYDDEDNEEMIKDSTeddlKLLEddkEMFEAADLNKDGKLDKTEFSAFQHP 150


                 .
gi 281363946 215 E 215
Cdd:cd16227  151 E 151
 
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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