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Conserved domains on  [gi|15599371|ref|NP_252865|]
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peptidyl-prolyl cis-trans isomerase C2 [Pseudomonas aeruginosa PAO1]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 11433571)

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

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  12871165
SCOP:  3000622

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 3-93 4.80e-36

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 118.91  E-value: 4.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371   3 RATARHILVS---------SEAKCNELKTAIEGGADFAEVAREHSSCP-SGRDGGNLGSFGPGQMVREFDQVVFSAPLNV 72
Cdd:COG0760   8 EVRASHILVKvppsedrakAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKPGE 87

                        90       100
                ....*....|....*....|.
gi 15599371  73 VQGPVKTQFGYHLLEVTSRQD 93
Cdd:COG0760  88 ISGPVKTQFGYHIIKVEDRRP 108
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 3-93 4.80e-36

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 118.91  E-value: 4.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371   3 RATARHILVS---------SEAKCNELKTAIEGGADFAEVAREHSSCP-SGRDGGNLGSFGPGQMVREFDQVVFSAPLNV 72
Cdd:COG0760   8 EVRASHILVKvppsedrakAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKPGE 87

                        90       100
                ....*....|....*....|.
gi 15599371  73 VQGPVKTQFGYHLLEVTSRQD 93
Cdd:COG0760  88 ISGPVKTQFGYHIIKVEDRRP 108
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-92 4.31e-32

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 107.42  E-value: 4.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371   1 MAR-ATARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGRDGGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVKT 79
Cdd:PRK15441  1 MAKtAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHT 80

                        90
                ....*....|...
gi 15599371  80 QFGYHLLEVTSRQ 92
Cdd:PRK15441 81 QFGYHIIKVLYRN 93
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 4-92 6.76e-29

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 99.75  E-value: 6.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371     4 ATARHILVSSE-----------AKCNELKTAIEGGADFAEVAREHSSCP-SGRDGGNLGSFGPGQMVREFDQVVFSAPLN 71
Cdd:pfam13616  16 VKASHILISYSqavsrteeeakAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSLKVG 95

                          90       100
                  ....*....|....*....|.
gi 15599371    72 VVQGPVKTQFGYHLLEVTSRQ 92
Cdd:pfam13616  96 EISGVVKTQFGFHIIKVTDKK 116
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 3-93 4.80e-36

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 118.91  E-value: 4.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371   3 RATARHILVS---------SEAKCNELKTAIEGGADFAEVAREHSSCP-SGRDGGNLGSFGPGQMVREFDQVVFSAPLNV 72
Cdd:COG0760   8 EVRASHILVKvppsedrakAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKPGE 87

                        90       100
                ....*....|....*....|.
gi 15599371  73 VQGPVKTQFGYHLLEVTSRQD 93
Cdd:COG0760  88 ISGPVKTQFGYHIIKVEDRRP 108
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-92 4.31e-32

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 107.42  E-value: 4.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371   1 MAR-ATARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGRDGGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVKT 79
Cdd:PRK15441  1 MAKtAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHT 80

                        90
                ....*....|...
gi 15599371  80 QFGYHLLEVTSRQ 92
Cdd:PRK15441 81 QFGYHIIKVLYRN 93
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 4-92 6.76e-29

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 99.75  E-value: 6.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371     4 ATARHILVSSE-----------AKCNELKTAIEGGADFAEVAREHSSCP-SGRDGGNLGSFGPGQMVREFDQVVFSAPLN 71
Cdd:pfam13616  16 VKASHILISYSqavsrteeeakAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSLKVG 95

                          90       100
                  ....*....|....*....|.
gi 15599371    72 VVQGPVKTQFGYHLLEVTSRQ 92
Cdd:pfam13616  96 EISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 8-90 3.07e-25

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 90.05  E-value: 3.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    8 HILVS----SEAKCNELKTAIE--------GGADFAEVAREHSS-CPSGRDGGNLGSFGPGQMVREFDQVVFSAPLNVVQ 74
Cdd:pfam00639  1 HILIKtpeaSERDRAEAKAKAEeileqlksGEDSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                         90
                 ....*....|....*.
gi 15599371   75 GPVKTQFGYHLLEVTS 90
Cdd:pfam00639 81 GPVETRFGFHIIKLTD 96
prsA PRK03095
peptidylprolyl isomerase PrsA;
6-93 6.58e-22

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 86.20  E-value: 6.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    6 ARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGRD-GGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVKTQFGYH 84
Cdd:PRK03095 135 ASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEkGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYH 214


                 ....*....
gi 15599371   85 LLEVTSRQD 93
Cdd:PRK03095 215 IIKVTDIKE 223
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 6-93 5.29e-21

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 83.87  E-value: 5.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    6 ARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGRD-GGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVKTQFGYH 84
Cdd:PRK02998 137 VSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEqGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYH 216


                 ....*....
gi 15599371   85 LLEVTSRQD 93
Cdd:PRK02998 217 IIKVTDKKE 225
prsA PRK03002
peptidylprolyl isomerase PrsA;
6-93 8.56e-20

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 80.75  E-value: 8.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    6 ARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGRD-GGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVKTQFGYH 84
Cdd:PRK03002 139 ASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKEkGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYH 218


                 ....*....
gi 15599371   85 LLEVTSRQD 93
Cdd:PRK03002 219 IIKLTDKKD 227
prsA PRK00059
peptidylprolyl isomerase; Provisional
 6-93 1.30e-16

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 72.44  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    6 ARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGRD-GGNLG--SFGPGQMVREFDQVVFSAPLNVVQGPVKTQFG 82
Cdd:PRK00059 199 LAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKDkGGDLGdvPYSDSGYDKEFMDGAKALKEGEISAPVKTQFG 278

                         90
                 ....*....|.
gi 15599371   83 YHLLEVTSRQD 93
Cdd:PRK00059 279 YHIIKAIKKKE 289
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 3-86 4.07e-14

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 62.35  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    3 RATARHILVSSEAKCNELK----TAIEGGADFAEVAREHSSCPSGRDGGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVK 78
Cdd:PTZ00356  24 RRTGKPVTRSKEEAIKELAkwreQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVH 103


                 ....*...
gi 15599371   79 TQFGYHLL 86
Cdd:PTZ00356 104 TDSGVHII 111
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 13-88 7.35e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 42.42  E-value: 7.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599371   13 SEAKCNELKTAIEGGADFAEVAREHSSCPSGRDGGNLGSFGPGQMVREFDQVVFSAPLNVVQGPVKTQFGYHLLEV 88
Cdd:PRK10770 177 AESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGPIRSGVGFHILKV 252
prsA PRK04405
peptidylprolyl isomerase; Provisional
 5-88 7.88e-06

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 42.08  E-value: 7.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    5 TARHILVSSEAKCNELKTAIEGGADFAEVAREHSSCPSGR-DGGNLGSFGPGQmvREFDQVVFSAPLNVVQG-----PVK 78
Cdd:PRK04405 146 TVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKnKGGKLSAFDSTD--TTLDSTFKTAAFKLKNGeytttPVK 223

                         90
                 ....*....|
gi 15599371   79 TQFGYHLLEV 88
Cdd:PRK04405 224 TTYGYEVIKM 233
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 9-83 3.98e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 40.38  E-value: 3.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599371    9 ILVSSEAKCNELKTAIEGGADFAEVAREHSSCP-SGRDGGNLGSFGPGQMVREFDQvvfsAPLN---VVQGPVKTQFGY 83
Cdd:PRK10788 276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPDELKN----AGLKekgQLSGVIKSSVGF 350
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 6-92 6.18e-05

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 39.72  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371    6 ARHILVSS---------EAKCNELKTAIEGG-ADFAEVAREHSSCP-SGRDGGNLGSFGPGQmvreFDQVVFSAPLNVVQ 74
Cdd:PRK10770 269 ARHILLKPspimtdeqaRAKLEQIAADIKSGkTTFAAAAKEFSQDPgSANQGGDLGWATPDI----FDPAFRDALMRLNK 344

                         90       100
                 ....*....|....*....|...
gi 15599371   75 G----PVKTQFGYHLLE-VTSRQ 92
Cdd:PRK10770 345 GqisaPVHSSFGWHLIElLDTRQ 367
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
2-93 1.88e-04

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 37.42  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599371     2 ARATARHILVSSEAKCNELKTAIEGGA--DFAEVAREhsscpSGRDGGNLGSFGPGQMV-REFDQVVFSAPLNVVQGPVK 78
Cdd:pfam13145  21 EGRLLEILVFKDQVAADAALALLKAGAleDFAALAKG-----EGIKAATLDIVESAELLpEELAKAAFALKPGEVSGPIK 95

                          90
                  ....*....|....*
gi 15599371    79 TQFGYHLLEVTSRQD 93
Cdd:pfam13145  96 TGNGYYVVRVTEIKP 110
 
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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