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Conserved domains on  [gi|497896781|ref|WP_010210937|]
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MULTISPECIES: peptidylprolyl isomerase [Pseudomonas]

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 9.81e-38

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 123.15  E-value: 9.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   3 KATARHILVS---------TEDKCNELKAQIEGGADFAEIAKANSSCPSSR-DGGNLGSFGPGQMVKEFDTVVFSAPVNT 72
Cdd:COG0760    8 EVRASHILVKvppsedrakAEAKAEELLAQLKAGADFAELAKEYSQDPGSAaNGGDLGWFSRGQLVPEFEEAAFALKPGE 87

                         90       100
                 ....*....|....*....|.
gi 497896781  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 9.81e-38

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 123.15  E-value: 9.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   3 KATARHILVS---------TEDKCNELKAQIEGGADFAEIAKANSSCPSSR-DGGNLGSFGPGQMVKEFDTVVFSAPVNT 72
Cdd:COG0760    8 EVRASHILVKvppsedrakAEAKAEELLAQLKAGADFAELAKEYSQDPGSAaNGGDLGWFSRGQLVPEFEEAAFALKPGE 87

                         90       100
                 ....*....|....*....|.
gi 497896781  73 VQGPVKTQFGYHLLEVTSRQD 93
Cdd:COG0760   88 ISGPVKTQFGYHIIKVEDRRP 108
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-92 2.52e-31

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 105.49  E-value: 2.52e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781  1 MAK-ATARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSRDGGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKT 79
Cdd:PRK15441  1 MAKtAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHT 80

                        90
                ....*....|...
gi 497896781 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 ...
 2-92 3.81e-30

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: 103.22  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781    2 AKATARHILVSTED-----------KCNELKAQIEGGADFAEIAKANSSCPSSRD-GGNLGSFGPGQMVKEFDTVVFSAP 69
Cdd:pfam13616  14 DSVKASHILISYSQavsrteeeakaKADSLLAALKNGADFAALAKTYSDDPASKNnGGDLGWFTKGQMVKEFEDAVFSLK 93

                          90       100
                  ....*....|....*....|...
gi 497896781   70 VNTVQGPVKTQFGYHLLEVTSRQ 92
Cdd:pfam13616  94 VGEISGVVKTQFGFHIIKVTDKK 116
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 3-93 9.81e-38

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 123.15  E-value: 9.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   3 KATARHILVS---------TEDKCNELKAQIEGGADFAEIAKANSSCPSSR-DGGNLGSFGPGQMVKEFDTVVFSAPVNT 72
Cdd:COG0760    8 EVRASHILVKvppsedrakAEAKAEELLAQLKAGADFAELAKEYSQDPGSAaNGGDLGWFSRGQLVPEFEEAAFALKPGE 87

                         90       100
                 ....*....|....*....|.
gi 497896781  73 VQGPVKTQFGYHLLEVTSRQD 93
Cdd:COG0760   88 ISGPVKTQFGYHIIKVEDRRP 108
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-92 2.52e-31

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 105.49  E-value: 2.52e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781  1 MAK-ATARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSRDGGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKT 79
Cdd:PRK15441  1 MAKtAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHT 80

                        90
                ....*....|...
gi 497896781 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 ...
 2-92 3.81e-30

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: 103.22  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781    2 AKATARHILVSTED-----------KCNELKAQIEGGADFAEIAKANSSCPSSRD-GGNLGSFGPGQMVKEFDTVVFSAP 69
Cdd:pfam13616  14 DSVKASHILISYSQavsrteeeakaKADSLLAALKNGADFAALAKTYSDDPASKNnGGDLGWFTKGQMVKEFEDAVFSLK 93

                          90       100
                  ....*....|....*....|...
gi 497896781   70 VNTVQGPVKTQFGYHLLEVTSRQ 92
Cdd:pfam13616  94 VGEISGVVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 8-90 1.96e-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: 90.44  E-value: 1.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   8 HILVST-----------EDKCNELKAQIEGGAD-FAEIAKANSS-CPSSRDGGNLGSFGPGQMVKEFDTVVFSAPVNTVQ 74
Cdd:pfam00639  1 HILIKTpeaserdraeaKAKAEEILEQLKSGEDsFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                         90
                 ....*....|....*.
gi 497896781  75 GPVKTQFGYHLLEVTS 90
Cdd:pfam00639 81 GPVETRFGFHIIKLTD 96
prsA PRK03002
peptidylprolyl isomerase PrsA;
6-93 2.94e-22

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 86.91  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   6 ARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSRD-GGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKTQFGYH 84
Cdd:PRK03002 139 ASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKEkGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYH 218


                 ....*....
gi 497896781  85 LLEVTSRQD 93
Cdd:PRK03002 219 IIKLTDKKD 227
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 3-93 7.24e-22

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 86.18  E-value: 7.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   3 KATARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSRD-GGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKTQF 81
Cdd:PRK02998 134 EMKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEqGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTY 213

                         90
                 ....*....|..
gi 497896781  82 GYHLLEVTSRQD 93
Cdd:PRK02998 214 GYHIIKVTDKKE 225
prsA PRK03095
peptidylprolyl isomerase PrsA;
6-93 1.34e-21

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 85.43  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   6 ARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSRD-GGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKTQFGYH 84
Cdd:PRK03095 135 ASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEkGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYH 214


                 ....*....
gi 497896781  85 LLEVTSRQD 93
Cdd:PRK03095 215 IIKVTDIKE 223
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-93 1.68e-20

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 83.22  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   2 AKATARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSRD-GGNLG--SFGPGQMVKEFDTVVFSAPVNTVQGPVK 78
Cdd:PRK00059 195 NTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKDkGGDLGdvPYSDSGYDKEFMDGAKALKEGEISAPVK 274

                         90
                 ....*....|....*
gi 497896781  79 TQFGYHLLEVTSRQD 93
Cdd:PRK00059 275 TQFGYHIIKAIKKKE 289
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 5-86 9.60e-17

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 68.90  E-value: 9.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   5 TARHILVSTEDKCNELK---AQIEGGA-DFAEIAKANSSCPSSRDGGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKTQ 80
Cdd:PTZ00356  26 TGKPVTRSKEEAIKELAkwrEQIVSGEkTFEEIARQRSDCGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTD 105


                 ....*.
gi 497896781  81 FGYHLL 86
Cdd:PTZ00356 106 SGVHII 111
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
7-93 1.12e-07

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 45.90  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781    7 RHILVSTEDKCNELKAQIEGGA--DFAEIAKANSSCPSSRDGGNLGSFGPgqmvKEFDTVVFSAPVNTVQGPVKTQFGYH 84
Cdd:pfam13145  26 EILVFKDQVAADAALALLKAGAleDFAALAKGEGIKAATLDIVESAELLP----EELAKAAFALKPGEVSGPIKTGNGYY 101


                  ....*....
gi 497896781   85 LLEVTSRQD 93
Cdd:pfam13145 102 VVRVTEIKP 110
prsA PRK04405
peptidylprolyl isomerase; Provisional
 3-88 1.26e-07

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 47.09  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   3 KATARHILVSTEDKCNELKAQIEGGADFAEIAKANSSCPSSR-DGGNLGSFGP--GQMVKEFDTVVFSAPVNTV-QGPVK 78
Cdd:PRK04405 144 KVTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKnKGGKLSAFDStdTTLDSTFKTAAFKLKNGEYtTTPVK 223

                         90
                 ....*....|
gi 497896781  79 TQFGYHLLEV 88
Cdd:PRK04405 224 TTYGYEVIKM 233
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 14-88 8.50e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 45.12  E-value: 8.50e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497896781  14 EDKCNELKAQIEGGADFAEIAKANSSCPSSRDGGNLGSFGPGQMVKEFDTVVFSAPVNTVQGPVKTQFGYHLLEV 88
Cdd:PRK10770 178 ESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMGWGRIQELPGLFAQALSTAKKGDIVGPIRSGVGFHILKV 252
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 6-92 5.02e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 42.81  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497896781   6 ARHIL-----VSTED----KCNELKAQIEGG-ADFAEIAKANSSCP-SSRDGGNLGSFGPGQMVKEFDTVVFSAPVNTVQ 74
Cdd:PRK10770 269 ARHILlkpspIMTDEqaraKLEQIAADIKSGkTTFAAAAKEFSQDPgSANQGGDLGWATPDIFDPAFRDALMRLNKGQIS 348

                         90
                 ....*....|....*....
gi 497896781  75 GPVKTQFGYHLLE-VTSRQ 92
Cdd:PRK10770 349 APVHSSFGWHLIElLDTRQ 367
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 9-61 5.94e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 39.61  E-value: 5.94e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497896781   9 ILVSTEDKCNELKAQIEGGADFAEIAKANSSCP-SSRDGGNLGSFGPGQMVKEF 61
Cdd:PRK10788 276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPDEL 329
 
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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