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Conserved domains on  [gi|1229782803|ref|XP_022144686|]
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peptidyl-prolyl cis-trans isomerase FKBP16-4, chloroplastic [Momordica charantia]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-215 4.17e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 102.27  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 117 GGTKAVIGSRVAVHYVAKWR-GITFMTSRqglgvGGGTPYGFDVGQserGTVLKGLDLGVQGMRVGGQRLLIVPPELAYG 195
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEdGTVFDSSY-----DRGKPFEFTLGS---GQVIPGWDEGLVGMKVGEKRKLTIPPELAYG 72
                          90       100
                  ....*....|....*....|..
gi 1229782803 196 SKGVQE--IPPNATIELDVELL 215
Cdd:pfam00254  73 EEGLAGpvIPPNATLVFEVELL 94
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-215 4.17e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 102.27  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 117 GGTKAVIGSRVAVHYVAKWR-GITFMTSRqglgvGGGTPYGFDVGQserGTVLKGLDLGVQGMRVGGQRLLIVPPELAYG 195
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEdGTVFDSSY-----DRGKPFEFTLGS---GQVIPGWDEGLVGMKVGEKRKLTIPPELAYG 72
                          90       100
                  ....*....|....*....|..
gi 1229782803 196 SKGVQE--IPPNATIELDVELL 215
Cdd:pfam00254  73 EEGLAGpvIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
108-217 7.21e-27

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 99.10  E-value: 7.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 108 LKYYDLKVGGGTKAVIGSRVAVHYVAK-WRGITFMTSRQGlgvggGTPYGFDVGQSErgtVLKGLDLGVQGMRVGGQRLL 186
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTlLDGTVFDSSYDR-----GEPATFPLGVGQ---VIPGWDEGLQGMKVGGKRRL 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1229782803 187 IVPPELAYGSKGVQE-IPPNATIELDVELLAI 217
Cdd:COG0545    73 VIPPELAYGERGAGGvIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
167-221 6.24e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.55  E-value: 6.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1229782803 167 VLKGLDLGVQGMRVGGQRLLIVPPELAYGSKGVQEIPPNATIELDVELLAIKQSP 221
Cdd:PRK10902  198 VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDVKPAP 252
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-215 4.17e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 102.27  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 117 GGTKAVIGSRVAVHYVAKWR-GITFMTSRqglgvGGGTPYGFDVGQserGTVLKGLDLGVQGMRVGGQRLLIVPPELAYG 195
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEdGTVFDSSY-----DRGKPFEFTLGS---GQVIPGWDEGLVGMKVGEKRKLTIPPELAYG 72
                          90       100
                  ....*....|....*....|..
gi 1229782803 196 SKGVQE--IPPNATIELDVELL 215
Cdd:pfam00254  73 EEGLAGpvIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
108-217 7.21e-27

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 99.10  E-value: 7.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 108 LKYYDLKVGGGTKAVIGSRVAVHYVAK-WRGITFMTSRQGlgvggGTPYGFDVGQSErgtVLKGLDLGVQGMRVGGQRLL 186
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTlLDGTVFDSSYDR-----GEPATFPLGVGQ---VIPGWDEGLQGMKVGGKRRL 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1229782803 187 IVPPELAYGSKGVQE-IPPNATIELDVELLAI 217
Cdd:COG0545    73 VIPPELAYGERGAGGvIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
167-221 6.24e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.55  E-value: 6.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1229782803 167 VLKGLDLGVQGMRVGGQRLLIVPPELAYGSKGVQEIPPNATIELDVELLAIKQSP 221
Cdd:PRK10902  198 VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDVKPAP 252
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
124-203 6.11e-07

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 47.40  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 124 GSRVAVHYVAKWR-GITFMTSRqglgvgGGTPYGFDVGQserGTVLKGLDLGVQGMRVGGQRLLIVPPELAYG---SKGV 199
Cdd:COG1047     4 GDVVTLHYTLKLEdGEVFDSTF------EGEPLEFLHGA---GQLIPGLEEALEGMEVGDKKTVTLPPEEAYGerdPELV 74

                  ....
gi 1229782803 200 QEIP 203
Cdd:COG1047    75 QTVP 78
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
102-217 6.58e-07

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 48.26  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229782803 102 TTLPNGLKYYDLKVGGGTKAVIGSRVAVHYVAKW-RGITFMTSrqglgVGGGTPYGFDVGqsergTVLKGLDLGVQGMRV 180
Cdd:PRK11570   98 NSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLiDGTVFDSS-----VARGEPAEFPVN-----GVIPGWIEALTLMPV 167
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1229782803 181 GGQRLLIVPPELAYGSKGV-QEIPPNATIELDVELLAI 217
Cdd:PRK11570  168 GSKWELTIPHELAYGERGAgASIPPFSTLVFEVELLEI 205
 
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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