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Conserved domains on  [gi|18420509|ref|NP_568067|]
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FK506-binding protein 16-2 [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;
106-205 1.02e-32

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509   106 GDEAP-RGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKLAYGPE 184
Cdd:pfam00254   1 GPEKAkKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVG------MKVGEKRKLTIPPELAYGEE 74
                          90       100
                  ....*....|....*....|.
gi 18420509   185 PAgcfsGDCNIPGNATLLYDI 205
Cdd:pfam00254  75 GL----AGPVIPPNATLVFEV 91
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
106-205 1.02e-32

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509   106 GDEAP-RGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKLAYGPE 184
Cdd:pfam00254   1 GPEKAkKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVG------MKVGEKRKLTIPPELAYGEE 74
                          90       100
                  ....*....|....*....|.
gi 18420509   185 PAgcfsGDCNIPGNATLLYDI 205
Cdd:pfam00254  75 GL----AGPVIPPNATLVFEV 91
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
100-210 5.03e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.50  E-value: 5.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509 100 DLDVGFGDEAPRGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKL 179
Cdd:COG0545   5 VLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQG------MKVGGKRRLVIPPEL 78
                        90       100       110
                ....*....|....*....|....*....|.
gi 18420509 180 AYGPEPAGcfsgdCNIPGNATLLYDINFVEI 210
Cdd:COG0545  79 AYGERGAG-----GVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
113-212 1.59e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 75.96  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509  113 VLVNihYTARFADGTLFDSSYKRARPLTMRigvgkvirgLDqGILGG--EGVPPMRVGGKRKLQIPPKLAYGPepagcfS 190
Cdd:PRK10902 167 VVVN--YKGTLIDGKEFDNSYTRGEPLSFR---------LD-GVIPGwtEGLKNIKKGGKIKLVIPPELAYGK------A 228
                         90       100
                 ....*....|....*....|..
gi 18420509  191 GDCNIPGNATLLYDINFVEIYP 212
Cdd:PRK10902 229 GVPGIPANSTLVFDVELLDVKP 250
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
106-205 1.02e-32

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509   106 GDEAP-RGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKLAYGPE 184
Cdd:pfam00254   1 GPEKAkKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVG------MKVGEKRKLTIPPELAYGEE 74
                          90       100
                  ....*....|....*....|.
gi 18420509   185 PAgcfsGDCNIPGNATLLYDI 205
Cdd:pfam00254  75 GL----AGPVIPPNATLVFEV 91
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
100-210 5.03e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.50  E-value: 5.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509 100 DLDVGFGDEAPRGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKL 179
Cdd:COG0545   5 VLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQG------MKVGGKRRLVIPPEL 78
                        90       100       110
                ....*....|....*....|....*....|.
gi 18420509 180 AYGPEPAGcfsgdCNIPGNATLLYDINFVEI 210
Cdd:COG0545  79 AYGERGAG-----GVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
113-212 1.59e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 75.96  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509  113 VLVNihYTARFADGTLFDSSYKRARPLTMRigvgkvirgLDqGILGG--EGVPPMRVGGKRKLQIPPKLAYGPepagcfS 190
Cdd:PRK10902 167 VVVN--YKGTLIDGKEFDNSYTRGEPLSFR---------LD-GVIPGwtEGLKNIKKGGKIKLVIPPELAYGK------A 228
                         90       100
                 ....*....|....*....|..
gi 18420509  191 GDCNIPGNATLLYDINFVEIYP 212
Cdd:PRK10902 229 GVPGIPANSTLVFDVELLDVKP 250
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
90-210 3.18e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 71.37  E-value: 3.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18420509   90 SYAKSGLGFCDLDVGFGDEAPRGVLVNIHYTARFADGTLFDSSYKRARPLTMRIGvgkvirgldqGILGG--EGVPPMRV 167
Cdd:PRK11570  98 NSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN----------GVIPGwiEALTLMPV 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18420509  168 GGKRKLQIPPKLAYGPEPAGcfsgdCNIPGNATLLYDINFVEI 210
Cdd:PRK11570 168 GSKWELTIPHELAYGERGAG-----ASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
115-183 3.55e-15

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 69.36  E-value: 3.55e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18420509 115 VNIHYTARFADGTLFDSSYKRaRPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKLAYGP 183
Cdd:COG1047   7 VTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEG------MEVGDKKTVTLPPEEAYGE 68
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
112-184 7.60e-08

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 50.09  E-value: 7.60e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18420509  112 GVLVniHYTARFADGTLFDSSYKRARPLTMRIGVGKVIRGLDQGILGgegvppMRVGGKRKLQIPPKLAYGPE 184
Cdd:PRK15095  10 AVLV--HFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLG------LKVGDKKTFSLEPEAAFGVP 74
 
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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