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Conserved domains on  [gi|88192842]
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Chain A, AtFKBP42

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446594)

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
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
62-156 3.90e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 82.63  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88192842    62 SKPSKYSTCFLHYRAWTKNSQhKFEDTWHEQQPIELVLGKEKKeLAGLAIGVASMKSGERALVHVGWELAYGKEGNfSFP 141
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGT-VFDSSYDRGKPFEFTLGSGQV-IPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL-AGP 79
                          90
                  ....*....|....*
gi 88192842   142 NVPPMADLLYEVEVI 156
Cdd:pfam00254  80 VIPPNATLVFEVELL 94
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
62-156 3.90e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 82.63  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88192842    62 SKPSKYSTCFLHYRAWTKNSQhKFEDTWHEQQPIELVLGKEKKeLAGLAIGVASMKSGERALVHVGWELAYGKEGNfSFP 141
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGT-VFDSSYDRGKPFEFTLGSGQV-IPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL-AGP 79
                          90
                  ....*....|....*
gi 88192842   142 NVPPMADLLYEVEVI 156
Cdd:pfam00254  80 VIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
54-158 5.72e-18

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 74.83  E-value: 5.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88192842  54 QIIKEGHGSKPSKYSTCFLHYRAWTKNSQhKFEDTWHEQQPIELVLGKEKkELAGLAIGVASMKSGERALVHVGWELAYG 133
Cdd:COG0545   4 KVLKEGTGAKPKAGDTVTVHYTGTLLDGT-VFDSSYDRGEPATFPLGVGQ-VIPGWDEGLQGMKVGGKRRLVIPPELAYG 81
                        90       100
                ....*....|....*....|....*
gi 88192842 134 KEGNfsFPNVPPMADLLYEVEVIGF 158
Cdd:COG0545  82 ERGA--GGVIPPNSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
62-156 3.90e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 82.63  E-value: 3.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88192842    62 SKPSKYSTCFLHYRAWTKNSQhKFEDTWHEQQPIELVLGKEKKeLAGLAIGVASMKSGERALVHVGWELAYGKEGNfSFP 141
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGT-VFDSSYDRGKPFEFTLGSGQV-IPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL-AGP 79
                          90
                  ....*....|....*
gi 88192842   142 NVPPMADLLYEVEVI 156
Cdd:pfam00254  80 VIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
54-158 5.72e-18

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 74.83  E-value: 5.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88192842  54 QIIKEGHGSKPSKYSTCFLHYRAWTKNSQhKFEDTWHEQQPIELVLGKEKkELAGLAIGVASMKSGERALVHVGWELAYG 133
Cdd:COG0545   4 KVLKEGTGAKPKAGDTVTVHYTGTLLDGT-VFDSSYDRGEPATFPLGVGQ-VIPGWDEGLQGMKVGGKRRLVIPPELAYG 81
                        90       100
                ....*....|....*....|....*
gi 88192842 134 KEGNfsFPNVPPMADLLYEVEVIGF 158
Cdd:COG0545  82 ERGA--GGVIPPNSTLVFEVELLDV 104
 
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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