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Conserved domains on  [gi|1929627173|gb|QPA17852|]
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peptidylprolyl isomerase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 11485412)

FKBP-type peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 1.14e-150

peptidyl-prolyl cis-trans isomerase; Provisional


:

Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 416.12  E-value: 1.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173   1 MTTPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRQRFQAM 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173  81 AAEGVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1929627173 161 ALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL 206
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 1.14e-150

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 416.12  E-value: 1.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173   1 MTTPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRQRFQAM 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173  81 AAEGVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1929627173 161 ALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL 206
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-205 6.21e-55

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 169.98  E-value: 6.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173 104 LQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPQELAY 181
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1929627173 182 GERGAGASIPPFSTLVFEVELLEI 205
Cdd:COG0545    81 GERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-203 5.81e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 131.55  E-value: 5.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173 117 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--NGVIPGWIEALTLMPVGSKWELTIPQELAYGERG-AGASIPPF 193
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 1929627173 194 STLVFEVELL 203
Cdd:pfam00254  85 ATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 1.14e-150

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 416.12  E-value: 1.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173   1 MTTPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRQRFQAM 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173  81 AAEGVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1929627173 161 ALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL 206
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-205 6.21e-55

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 169.98  E-value: 6.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173 104 LQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPQELAY 181
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1929627173 182 GERGAGASIPPFSTLVFEVELLEI 205
Cdd:COG0545    81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
6-205 3.80e-47

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 155.69  E-value: 3.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173   6 FDTIEAQASYGIGLQVGQQLSESGLE------GLLPEALVAGIADALEGKHPAVPVDVvHRALREIHERADAVRRQRFQA 79
Cdd:PRK10902   41 FKNDDQQSAYALGASLGRYMENSLKEqeklgiKLDKDQLIAGVQDAFADKSKLSDQEI-EQTLQAFEARVKSAAQAKMEK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173  80 MAAE----GVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVI 155
Cdd:PRK10902  120 DAADneakGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVI 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1929627173 156 PGWIEALTLMPVGSKWELTIPQELAYGERGAgASIPPFSTLVFEVELLEI 205
Cdd:PRK10902  200 PGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-203 5.81e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 131.55  E-value: 5.81e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173 117 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--NGVIPGWIEALTLMPVGSKWELTIPQELAYGERG-AGASIPPF 193
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 1929627173 194 STLVFEVELL 203
Cdd:pfam00254  85 ATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
10-108 1.15e-27

Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the amino terminus of pfam00254. This entry represents the N-terminal domain found in FKBP-type peptidylprolyl isomerases (PPIase). The N-terminal domain forms the dimer interface by the mutual exchange of two beta-strands between monomers.


Pssm-ID: 460169  Cd Length: 97  Bit Score: 100.26  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929627173  10 EAQASYGIGLQVGQQLSESGLEgLLPEALVAGIADALEGKHPAVPvDVVHRALREIHERADAVRRQRFQAMAAEGVKYLE 89
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGIE-LDLDAFLAGLKDALAGKPLLTD-EEAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*....
gi 1929627173  90 ENAKKEGVNSTESGLQFRV 108
Cdd:pfam01346  79 ENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
121-184 7.17e-13

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 63.20  E-value: 7.17e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929627173 121 DRVRVHYTGKLIDGTVFDSSVaRGEPAEFPV--NGVIPGWIEALTLMPVGSKWELTIPQELAYGER 184
Cdd:COG1047     5 DVVTLHYTLKLEDGEVFDSTF-EGEPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
123-184 2.89e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 39.69  E-value: 2.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929627173 123 VRVHYTGKLIDGTVFDSSVARGEPAEFPV-NGVIPGWIEA-LTLMPVGSKWELTIPQELAYGER 184
Cdd:PRK15095   11 VLVHFTLKLDDGSTAESTRNNGKPALFRLgDGSLSEGLEQqLLGLKVGDKKTFSLEPEAAFGVP 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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