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Conserved domains on  [gi|197724894|pdb|2PPP|A]
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Chain A, FK506-binding protein 1A

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 ...
2-105 1.15e-47

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 147.64  E-value: 1.15e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A        2 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYA 81
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
2PPP_A       82 YGATGHPGIIPPHATLVFDVELLK 105
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-105 1.15e-47

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 147.64  E-value: 1.15e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A        2 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYA 81
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
2PPP_A       82 YGATGHPGIIPPHATLVFDVELLK 105
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
12-104 2.07e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 138.87  E-value: 2.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A         12 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 90
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
2PPP_A         91 IPPHATLVFDVELL 104
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
3-107 1.59e-29

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 106.39  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A         3 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWQEGVAQMSVGQRAKLTISPDYAY 82
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
                         90       100
                 ....*....|....*....|....*
2PPP_A        83 GATGHPGiIPPHATLVFDVELLKLE 107
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-105 1.15e-47

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 147.64  E-value: 1.15e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A        2 VQVETISPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYA 81
Cdd:COG0545   1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                        90       100
                ....*....|....*....|....
2PPP_A       82 YGATGHPGIIPPHATLVFDVELLK 105
Cdd:COG0545  80 YGERGAGGVIPPNSTLVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
12-104 2.07e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 138.87  E-value: 2.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A         12 GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYAYGATGH-PGI 90
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80
                          90
                  ....*....|....
2PPP_A         91 IPPHATLVFDVELL 104
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
3-107 1.59e-29

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 106.39  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A         3 QVEtiSPGDGRTfPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLgkQEVIRGWQEGVAQMSVGQRAKLTISPDYAY 82
Cdd:PRK10902 151 KVE--KEGTGEA-PKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAY 225
                         90       100
                 ....*....|....*....|....*
2PPP_A        83 GATGHPGiIPPHATLVFDVELLKLE 107
Cdd:PRK10902 226 GKAGVPG-IPANSTLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-106 1.07e-23

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 89.86  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A         1 GVQVETISPGDGrTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKqeVIRGWQEGVAQMSVGQRAKLTISPDY 80
Cdd:PRK11570 103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                         90       100
                 ....*....|....*....|....*.
2PPP_A        81 AYGATGHPGIIPPHATLVFDVELLKL 106
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
17-83 1.88e-12

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.96  E-value: 1.88e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2PPP_A       17 KRGQTCVVHYTGMLEDGKKFDSSRDRnKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYAYG 83
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
24-83 4.21e-07

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 45.47  E-value: 4.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
2PPP_A        24 VHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWQEGVAQMSVGQRAKLTISPDYAYG 83
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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