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Conserved domains on  [gi|18394580|ref|NP_564048|]
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FKBP-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

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|GO:0000413|GO:0061077
PubMed:  27664121
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;
134-239 5.95e-23

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 89.18  E-value: 5.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580   134 GGATPRAGDLVVIDLKGQVQGtGQVFVDTFgtkdkKKMKPLALVVGSKPYSKGLCEGidyvLRSMKAGGKRRVIVPPSLG 213
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLED-GTVFDSSY-----DRGKPFEFTLGSGQVIPGWDEG----LVGMKVGEKRKLTIPPELA 70
                          90       100
                  ....*....|....*....|....*.
gi 18394580   214 FGVDGAElesGLQIPPNASLEYIVEI 239
Cdd:pfam00254  71 YGEEGLA---GPVIPPNATLVFEVEL 93
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
134-239 5.95e-23

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 89.18  E-value: 5.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580   134 GGATPRAGDLVVIDLKGQVQGtGQVFVDTFgtkdkKKMKPLALVVGSKPYSKGLCEGidyvLRSMKAGGKRRVIVPPSLG 213
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLED-GTVFDSSY-----DRGKPFEFTLGSGQVIPGWDEG----LVGMKVGEKRKLTIPPELA 70
                          90       100
                  ....*....|....*....|....*.
gi 18394580   214 FGVDGAElesGLQIPPNASLEYIVEI 239
Cdd:pfam00254  71 YGEEGLA---GPVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
125-239 6.56e-18

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 76.37  E-value: 6.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580 125 IRYYDQRVGGGATPRAGDLVVIDLKGQVqGTGQVFVDTFgtkdkKKMKPLALVVGSKPYSKGLCEGidyvLRSMKAGGKR 204
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTL-LDGTVFDSSY-----DRGEPATFPLGVGQVIPGWDEG----LQGMKVGGKR 70
                        90       100       110
                ....*....|....*....|....*....|....*
gi 18394580 205 RVIVPPSLGFGVDGAelesGLQIPPNASLEYIVEI 239
Cdd:COG0545  71 RLVIPPELAYGERGA----GGVIPPNSTLVFEVEL 101
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
104-247 9.56e-07

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 48.61  E-value: 9.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580  104 SQEVANTRDVEEEKeivlpNGIRYYDQRVGGGATPRAGDLVVIDLKGQVQgTGQVFVDTFgtkdkKKMKPLALVV-GSKP 182
Cdd:PRK10902 132 REKFAKEKGVKTTS-----TGLLYKVEKEGTGEAPKDSDTVVVNYKGTLI-DGKEFDNSY-----TRGEPLSFRLdGVIP 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394580  183 yskGLCEGIDYVlrsmKAGGKRRVIVPPSLGFGvdgaelESGLQ-IPPNASLEYIVEIdrVSIAPA 247
Cdd:PRK10902 201 ---GWTEGLKNI----KKGGKIKLVIPPELAYG------KAGVPgIPANSTLVFDVEL--LDVKPA 251
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
134-239 5.95e-23

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 89.18  E-value: 5.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580   134 GGATPRAGDLVVIDLKGQVQGtGQVFVDTFgtkdkKKMKPLALVVGSKPYSKGLCEGidyvLRSMKAGGKRRVIVPPSLG 213
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLED-GTVFDSSY-----DRGKPFEFTLGSGQVIPGWDEG----LVGMKVGEKRKLTIPPELA 70
                          90       100
                  ....*....|....*....|....*.
gi 18394580   214 FGVDGAElesGLQIPPNASLEYIVEI 239
Cdd:pfam00254  71 YGEEGLA---GPVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
125-239 6.56e-18

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 76.37  E-value: 6.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580 125 IRYYDQRVGGGATPRAGDLVVIDLKGQVqGTGQVFVDTFgtkdkKKMKPLALVVGSKPYSKGLCEGidyvLRSMKAGGKR 204
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTL-LDGTVFDSSY-----DRGEPATFPLGVGQVIPGWDEG----LQGMKVGGKR 70
                        90       100       110
                ....*....|....*....|....*....|....*
gi 18394580 205 RVIVPPSLGFGVDGAelesGLQIPPNASLEYIVEI 239
Cdd:COG0545  71 RLVIPPELAYGERGA----GGVIPPNSTLVFEVEL 101
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
104-247 9.56e-07

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 48.61  E-value: 9.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18394580  104 SQEVANTRDVEEEKeivlpNGIRYYDQRVGGGATPRAGDLVVIDLKGQVQgTGQVFVDTFgtkdkKKMKPLALVV-GSKP 182
Cdd:PRK10902 132 REKFAKEKGVKTTS-----TGLLYKVEKEGTGEAPKDSDTVVVNYKGTLI-DGKEFDNSY-----TRGEPLSFRLdGVIP 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394580  183 yskGLCEGIDYVlrsmKAGGKRRVIVPPSLGFGvdgaelESGLQ-IPPNASLEYIVEIdrVSIAPA 247
Cdd:PRK10902 201 ---GWTEGLKNI----KKGGKIKLVIPPELAYG------KAGVPgIPANSTLVFDVEL--LDVKPA 251
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
140-215 3.07e-03

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 37.00  E-value: 3.07e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18394580 140 AGDLVVIDLKGQVQGtGQVFVDTFGTKdkkkmkPLALVVGSKPYSKGLCEGidyvLRSMKAGGKRRVIVPPSLGFG 215
Cdd:COG1047   3 KGDVVTLHYTLKLED-GEVFDSTFEGE------PLEFLHGAGQLIPGLEEA----LEGMEVGDKKTVTLPPEEAYG 67
 
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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