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Conserved domains on  [gi|392900682|ref|NP_001255532|]
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peptidylprolyl isomerase [Caenorhabditis elegans]

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 ...
 1-83 2.68e-46

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 143.40  E-value: 2.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERGAPPKIPGNSVLKFDVEL 80
Cdd:COG0545   22 VHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVEL 101


                 ...
gi 392900682  81 MKI 83
Cdd:COG0545  102 LDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 1-83 2.68e-46

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 143.40  E-value: 2.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERGAPPKIPGNSVLKFDVEL 80
Cdd:COG0545   22 VHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVEL 101


                 ...
gi 392900682  81 MKI 83
Cdd:COG0545  102 LDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-80 2.15e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 138.10  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERG-APPKIPGNSVLKFDVE 79
Cdd:pfam00254 13 VHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPNATLVFEVE 92


                 .
gi 392900682  80 L 80
Cdd:pfam00254 93 L 93
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 3-83 1.62e-25

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 95.22  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   3 YTGTLLDGTEFDSSRTRNEEFTFTLgqGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERGApPKIPGNSVLKFDVELMK 82
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLD 247


                 .
gi 392900682  83 I 83
Cdd:PRK10902 248 V 248
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 1-83 2.68e-46

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 143.40  E-value: 2.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERGAPPKIPGNSVLKFDVEL 80
Cdd:COG0545   22 VHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVEL 101


                 ...
gi 392900682  81 MKI 83
Cdd:COG0545  102 LDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-80 2.15e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 138.10  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERG-APPKIPGNSVLKFDVE 79
Cdd:pfam00254 13 VHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPNATLVFEVE 92


                 .
gi 392900682  80 L 80
Cdd:pfam00254 93 L 93
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 3-83 1.62e-25

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 95.22  E-value: 1.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   3 YTGTLLDGTEFDSSRTRNEEFTFTLgqGNVIKGWDQGLLNMCVGERRILTIPPHLGYGERGApPKIPGNSVLKFDVELMK 82
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLD 247


                 .
gi 392900682  83 I 83
Cdd:PRK10902 248 V 248
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 1-83 1.89e-22

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 86.00  E-value: 1.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGqgNVIKGWDQGLLNMCVGERRILTIPPHLGYGERGAPPKIPGNSVLKFDVEL 80
Cdd:PRK11570 125 VHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVEL 202


                 ...
gi 392900682  81 MKI 83
Cdd:PRK11570 203 LEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 1-62 4.04e-17

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 70.52  E-value: 4.04e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392900682   1 MHYTGTLLDGTEFDSSRTRnEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGER 62
Cdd:COG1047    9 LHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 1-62 5.29e-07

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 44.70  E-value: 5.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392900682   1 MHYTGTLLDGTEFDSSRTRNEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTIPPHLGYGER 62
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 3-53 7.48e-04

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 36.65  E-value: 7.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392900682   3 YTGTLlDGTEFDSSRTrnEEFTFTLGQGNVIKGWDQGLLNMCVGERRILTI 53
Cdd:COG0544  168 FEGTI-DGEEFEGGKA--EDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEV 215
 
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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