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Conserved domains on  [gi|71993519|ref|NP_001021722|]
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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 ...
6-107 1.31e-46

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 144.94  E-value: 1.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519   6 QILVEGDNvTKPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGP 85
Cdd:COG0545   4 KVLKEGTG-AKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                        90       100
                ....*....|....*....|..
gi 71993519  86 RGVPPQIPANATLVFEVELLGV 107
Cdd:COG0545  83 RGAGGVIPPNSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
6-107 1.31e-46

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 144.94  E-value: 1.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519   6 QILVEGDNvTKPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGP 85
Cdd:COG0545   4 KVLKEGTG-AKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                        90       100
                ....*....|....*....|..
gi 71993519  86 RGVPPQIPANATLVFEVELLGV 107
Cdd:COG0545  83 RGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
15-105 2.27e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 138.87  E-value: 2.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519    15 TKPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGPRGV-PPQIP 93
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIP 82
                          90
                  ....*....|..
gi 71993519    94 ANATLVFEVELL 105
Cdd:pfam00254  83 PNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
16-108 3.24e-23

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 89.82  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519   16 KPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIgKGeVIKGWDQGVAQMSVGEKSKLTISADLGYGPRGVpPQIPAN 95
Cdd:PRK10902 160 APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL-DG-VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPAN 236
                         90
                 ....*....|...
gi 71993519   96 ATLVFEVELLGVN 108
Cdd:PRK10902 237 STLVFDVELLDVK 249
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
6-107 1.31e-46

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 144.94  E-value: 1.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519   6 QILVEGDNvTKPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGP 85
Cdd:COG0545   4 KVLKEGTG-AKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGE 82
                        90       100
                ....*....|....*....|..
gi 71993519  86 RGVPPQIPANATLVFEVELLGV 107
Cdd:COG0545  83 RGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
15-105 2.27e-44

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 138.87  E-value: 2.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519    15 TKPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGPRGV-PPQIP 93
Cdd:pfam00254   3 EKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIP 82
                          90
                  ....*....|..
gi 71993519    94 ANATLVFEVELL 105
Cdd:pfam00254  83 PNATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
16-108 3.24e-23

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 89.82  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519   16 KPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIgKGeVIKGWDQGVAQMSVGEKSKLTISADLGYGPRGVpPQIPAN 95
Cdd:PRK10902 160 APKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRL-DG-VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPAN 236
                         90
                 ....*....|...
gi 71993519   96 ATLVFEVELLGVN 108
Cdd:PRK10902 237 STLVFDVELLDVK 249
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
2-105 1.16e-18

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 76.76  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519    2 GVDRQILVEGDNVTkPKNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKgeVIKGWDQGVAQMSVGEKSKLTISADL 81
Cdd:PRK11570 103 GLQFRVLTQGEGAI-PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHEL 179
                         90       100
                 ....*....|....*....|....
gi 71993519   82 GYGPRGVPPQIPANATLVFEVELL 105
Cdd:PRK11570 180 AYGERGAGASIPPFSTLVFEVELL 203
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
18-104 1.02e-16

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 70.13  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993519  18 KNGQTVTCHYVLTLENGKKIDSSRDRGtPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGPRgvppqipaNAT 97
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEGE-PLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER--------DPE 72

                ....*..
gi 71993519  98 LVFEVEL 104
Cdd:COG1047  73 LVQTVPR 79
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
18-86 8.20e-08

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 47.39  E-value: 8.20e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71993519   18 KNGQTVTCHYVLTLENGKKIDSSRDRGTPFKFKIGKGEVIKGWDQGVAQMSVGEKSKLTISADLGYGPR 86
Cdd:PRK15095   6 QSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 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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