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Conserved domains on  [gi|6679803|ref|NP_032045|]
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peptidyl-prolyl cis-trans isomerase FKBP1A isoform 1 [Mus musculus]

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 6.99e-48

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 148.02  E-value: 6.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803    3 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 6679803   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 6.99e-48

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 148.02  E-value: 6.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803    3 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 6679803   83 YGATGHPGIIPPHATLVFDVELLK 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 1.55e-45

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.95  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803     13 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYGATGH-PGI 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 6679803     92 IPPHATLVFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
4-108 1.79e-28

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 103.69  E-value: 1.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803     4 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLgkQEVIRGWEEGVAQMSVGQRAKLIISSDYAY 83
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
                         90       100
                 ....*....|....*....|....*
gi 6679803    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 6.99e-48

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 148.02  E-value: 6.99e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803    3 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYA 82
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
gi 6679803   83 YGATGHPGIIPPHATLVFDVELLK 106
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 1.55e-45

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.95  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803     13 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYGATGH-PGI 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 6679803     92 IPPHATLVFDVELL 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
4-108 1.79e-28

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 103.69  E-value: 1.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803     4 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLgkQEVIRGWEEGVAQMSVGQRAKLIISSDYAY 83
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
                         90       100
                 ....*....|....*....|....*
gi 6679803    84 GATGHPGiIPPHATLVFDVELLKLE 108
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
2-107 9.49e-24

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 89.86  E-value: 9.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803     2 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKqeVIRGWEEGVAQMSVGQRAKLIISSDY 81
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                         90       100
                 ....*....|....*....|....*.
gi 6679803    82 AYGATGHPGIIPPHATLVFDVELLKL 107
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
18-84 3.84e-12

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.19  E-value: 3.84e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679803   18 KRGQTCVVHYTGMLEDGKKFDSSRDRnKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYG 84
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
25-84 1.06e-05

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 41.62  E-value: 1.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679803    25 VHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGWEEGVAQMSVGQRAKLIISSDYAYG 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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