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Conserved domains on  [gi|24655568|ref|NP_523792|]
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FK506-binding protein 12kD [Drosophila melanogaster]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11425492)

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
SCOP:  4001062

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-107 3.21e-47

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 146.48  E-value: 3.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568   3 VQVVPIAPGDGSTyPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....*
gi 24655568  83 YGSRGHPGVIPPNSTLTFDVELLKV 107
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-107 3.21e-47

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 146.48  E-value: 3.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568   3 VQVVPIAPGDGSTyPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....*
gi 24655568  83 YGSRGHPGVIPPNSTLTFDVELLKV 107
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 6.51e-46

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 142.72  E-value: 6.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568    13 GSTYPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYAYGSRGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 24655568    92 IPPNSTLTFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
10-108 1.54e-28

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 103.69  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568   10 PGDGSTyPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIgKGeVIRGWDEGVAQLSVGQRAKLICSPDYAYGSRGHP 89
Cdd:PRK10902 155 EGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL-DG-VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                         90
                 ....*....|....*....
gi 24655568   90 GvIPPNSTLTFDVELLKVE 108
Cdd:PRK10902 232 G-IPANSTLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-107 3.21e-47

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 146.48  E-value: 3.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568   3 VQVVPIAPGDGSTyPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....*
gi 24655568  83 YGSRGHPGVIPPNSTLTFDVELLKV 107
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 6.51e-46

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 142.72  E-value: 6.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568    13 GSTYPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYAYGSRGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 24655568    92 IPPNSTLTFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
10-108 1.54e-28

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 103.69  E-value: 1.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568   10 PGDGSTyPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIgKGeVIRGWDEGVAQLSVGQRAKLICSPDYAYGSRGHP 89
Cdd:PRK10902 155 EGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL-DG-VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                         90
                 ....*....|....*....
gi 24655568   90 GvIPPNSTLTFDVELLKVE 108
Cdd:PRK10902 232 G-IPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
2-107 2.62e-24

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 91.40  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655568    2 GVQVVPIAPGDGSTyPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKgeVIRGWDEGVAQLSVGQRAKLICSPDY 81
Cdd:PRK11570 103 GLQFRVLTQGEGAI-PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                         90       100
                 ....*....|....*....|....*.
gi 24655568   82 AYGSRGHPGVIPPNSTLTFDVELLKV 107
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
18-86 2.02e-15

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 66.66  E-value: 2.02e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24655568  18 KNGQKVTVHYTGTLDDGTKFDSSRDRnKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYAYGSR 86
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
14-86 7.47e-08

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 47.39  E-value: 7.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24655568   14 STYPKNGQKVTVHYTGTLDDGTKFDSSRDRNKPFKFTIGKGEVIRGWDEGVAQLSVGQRAKLICSPDYAYGSR 86
Cdd:PRK15095   2 SESVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
 
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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