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Conserved domains on  [gi|1038986347|ref|NP_001315490|]
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FKBP prolyl isomerase 1Aa [Danio rerio]

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 4.51e-45

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 141.09  E-value: 4.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347   3 VEVETITPGDGSTfPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFA 82
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                          90       100
                  ....*....|....*....|....
gi 1038986347  83 YGSKGHPGVIPPNATLIFDVELIG 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 4.51e-45

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 141.09  E-value: 4.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347   3 VEVETITPGDGSTfPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFA 82
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                          90       100
                  ....*....|....*....|....
gi 1038986347  83 YGSKGHPGVIPPNATLIFDVELIG 106
Cdd:COG0545    80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 4.95e-45

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 140.79  E-value: 4.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347  13 GSTFPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFAYGSKGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 1038986347  92 IPPNATLIFDVELI 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
10-105 2.18e-27

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 100.99  E-value: 2.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347  10 PGDGSTfPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIgkQEVIRGWDEGVAQMSVGQRAKLTCTPDFAYGSKGHP 89
Cdd:PRK10902  155 EGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                          90
                  ....*....|....*.
gi 1038986347  90 GvIPPNATLIFDVELI 105
Cdd:PRK10902  232 G-IPANSTLVFDVELL 246
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
3-106 4.51e-45

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 141.09  E-value: 4.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347   3 VEVETITPGDGSTfPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFA 82
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                          90       100
                  ....*....|....*....|....
gi 1038986347  83 YGSKGHPGVIPPNATLIFDVELIG 106
Cdd:COG0545    80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-105 4.95e-45

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 140.79  E-value: 4.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347  13 GSTFPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFAYGSKGH-PGV 91
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
gi 1038986347  92 IPPNATLIFDVELI 105
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
10-105 2.18e-27

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 100.99  E-value: 2.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347  10 PGDGSTfPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIgkQEVIRGWDEGVAQMSVGQRAKLTCTPDFAYGSKGHP 89
Cdd:PRK10902  155 EGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                          90
                  ....*....|....*.
gi 1038986347  90 GvIPPNATLIFDVELI 105
Cdd:PRK10902  232 G-IPANSTLVFDVELL 246
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
2-105 4.31e-23

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 88.32  E-value: 4.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347   2 GVEVETITPGDGStFPKKGQTCVVHYVGSLTDGRKFDSSRDRGKPFKFKIGKqeVIRGWDEGVAQMSVGQRAKLTCTPDF 81
Cdd:PRK11570  103 GLQFRVLTQGEGA-IPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                          90       100
                  ....*....|....*....|....
gi 1038986347  82 AYGSKGHPGVIPPNATLIFDVELI 105
Cdd:PRK11570  180 AYGERGAGASIPPFSTLVFEVELL 203
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
18-104 3.43e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 55.88  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1038986347  18 KKGQTCVVHYVGSLTDGRKFDSSRDRgKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFAYGskghpgviPPNAT 97
Cdd:COG1047     2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ERDPE 72

                  ....*..
gi 1038986347  98 LIFDVEL 104
Cdd:COG1047    73 LVQTVPR 79
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
25-99 2.87e-05

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 40.46  E-value: 2.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1038986347  25 VHYVGSLTDGRKFDSSRDRGKPFKFKIGKQEVIRGWDEGVAQMSVGQRAKLTCTPDFAYGskghpgviPPNATLI 99
Cdd:PRK15095   13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG--------VPSPDLI 79
 
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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