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Conserved domains on  [gi|4503725|ref|NP_000792|]
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peptidyl-prolyl cis-trans isomerase FKBP1A isoform a [Homo sapiens]

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 ...
3-106 1.76e-47

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 147.25  E-value: 1.76e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725    3 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 4503725   83 YGATGHPGIIPPHATLVFDVELLK 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-106 1.76e-47

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 147.25  E-value: 1.76e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725    3 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 4503725   83 YGATGHPGIIPPHATLVFDVELLK 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 3.30e-45

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 3.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725     13 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 4503725     92 IPPHATLVFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
4-108 1.64e-29

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 106.39  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725     4 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 83
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
                         90       100
                 ....*....|....*....|....*
gi 4503725    84 GATGHPGiIPPHATLVFDVELLKLE 108
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-106 1.76e-47

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 147.25  E-value: 1.76e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725    3 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 4503725   83 YGATGHPGIIPPHATLVFDVELLK 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 3.30e-45

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 3.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725     13 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 4503725     92 IPPHATLVFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
4-108 1.64e-29

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 106.39  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725     4 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWEEGVAQMSVGQRAKLTISPDYAY 83
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
                         90       100
                 ....*....|....*....|....*
gi 4503725    84 GATGHPGiIPPHATLVFDVELLKLE 108
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
2-107 1.27e-23

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 89.47  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725     2 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKqeVIRGWEEGVAQMSVGQRAKLTISPDY 81
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                         90       100
                 ....*....|....*....|....*.
gi 4503725    82 AYGATGHPGIIPPHATLVFDVELLKL 107
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
18-84 9.05e-14

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 62.43  E-value: 9.05e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503725   18 KRGQTCVVHYTGMLEDGKKFDSSRDRnKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 84
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
25-84 6.46e-08

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 47.78  E-value: 6.46e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503725    25 VHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYG 84
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
 
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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