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Conserved domains on  [gi|1845973183|ref|NP_001370079|]
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Peptidyl-prolyl cis-trans isomerase [Caenorhabditis elegans]

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, ...
 29-126 1.98e-29

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 103.50  E-value: 1.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  29 GGTAVKVRHIL---------CEKQGKALEAIEKLKSGMKFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDAAFALs 97
Cdd:COG0760     5 SPEEVRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFAL- 83

                          90       100
                  ....*....|....*....|....*....
gi 1845973183  98 nsscDKPIYTDpPVKTKFGYHVIMVEGKK 126
Cdd:COG0760    84 ----KPGEISG-PVKTQFGYHIIKVEDRR 107
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 29-126 1.98e-29

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 103.50  E-value: 1.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  29 GGTAVKVRHIL---------CEKQGKALEAIEKLKSGMKFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDAAFALs 97
Cdd:COG0760     5 SPEEVRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFAL- 83

                          90       100
                  ....*....|....*....|....*....
gi 1845973183  98 nsscDKPIYTDpPVKTKFGYHVIMVEGKK 126
Cdd:COG0760    84 ----KPGEISG-PVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 27-126 9.66e-20

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: 77.79  E-value: 9.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  27 KGGGTAVKVRHIL-----------CEKQGKALEAIEKLKSGMKFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDAA 93
Cdd:pfam13616  10 KSAPDSVKASHILisysqavsrteEEAKAKADSLLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVKEFEDAV 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845973183  94 FALSNSSCDKpiytdpPVKTKFGYHVIMVEGKK 126
Cdd:pfam13616  90 FSLKVGEISG------VVKTQFGFHIIKVTDKK 116
prsA PRK03095
peptidylprolyl isomerase PrsA;
33-122 2.63e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 67.33  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  33 VKVRHILCEKQGKALEAIEKLKSGMKFNEVAAQYSEDKA--RSGGDLGWMTRGSMVGPFQDAAFALSNSSCDKpiytdpP 110
Cdd:PRK03095  133 IKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGskEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSE------P 206

                          90
                  ....*....|..
gi 1845973183 111 VKTKFGYHVIMV 122
Cdd:PRK03095  207 VKSQFGYHIIKV 218
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 29-126 1.98e-29

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 103.50  E-value: 1.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  29 GGTAVKVRHIL---------CEKQGKALEAIEKLKSGMKFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDAAFALs 97
Cdd:COG0760     5 SPEEVRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFAL- 83

                          90       100
                  ....*....|....*....|....*....
gi 1845973183  98 nsscDKPIYTDpPVKTKFGYHVIMVEGKK 126
Cdd:COG0760    84 ----KPGEISG-PVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 27-126 9.66e-20

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: 77.79  E-value: 9.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  27 KGGGTAVKVRHIL-----------CEKQGKALEAIEKLKSGMKFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDAA 93
Cdd:pfam13616  10 KSAPDSVKASHILisysqavsrteEEAKAKADSLLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVKEFEDAV 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845973183  94 FALSNSSCDKpiytdpPVKTKFGYHVIMVEGKK 126
Cdd:pfam13616  90 FSLKVGEISG------VVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 45-124 1.53e-16

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: 69.25  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  45 KALEAIEKLKSGM-KFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDAAFALsnsscdKPIYTDPPVKTKFGYHVIM 121
Cdd:pfam00639  20 KAEEILEQLKSGEdSFAELARKYSDDCpsAANGGDLGWFTRGQLPPEFEKAAFAL------KPGEISGPVETRFGFHIIK 93


                  ...
gi 1845973183 122 VEG 124
Cdd:pfam00639  94 LTD 96
prsA PRK03095
peptidylprolyl isomerase PrsA;
33-122 2.63e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 67.33  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  33 VKVRHILCEKQGKALEAIEKLKSGMKFNEVAAQYSEDKA--RSGGDLGWMTRGSMVGPFQDAAFALSNSSCDKpiytdpP 110
Cdd:PRK03095  133 IKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGskEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSE------P 206

                          90
                  ....*....|..
gi 1845973183 111 VKTKFGYHVIMV 122
Cdd:PRK03095  207 VKSQFGYHIIKV 218
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 33-126 1.57e-13

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 64.99  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  33 VKVRHILCEKQGKALEAIEKLKSGMKFNEVAAQYSEDKA--RSGGDLGWMTRGSMVGPFQDAAFALSNSSCDKpiytdpP 110
Cdd:PRK02998  135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                          90
                  ....*....|....*.
gi 1845973183 111 VKTKFGYHVIMVEGKK 126
Cdd:PRK02998  209 VKTTYGYHIIKVTDKK 224
prsA PRK04405
peptidylprolyl isomerase; Provisional
 23-120 3.47e-13

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 64.03  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  23 KKEAKGGGTAVKVRHILCEKQGKALEAIEKLKSGMKFNEVAAQYSEDKARS--GGDLGW--MTRGSMVGPFQDAAFALSN 98
Cdd:PRK04405  135 KKAWKSYQPKVTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKnkGGKLSAfdSTDTTLDSTFKTAAFKLKN 214

                          90       100
                  ....*....|....*....|..
gi 1845973183  99 SScdkpiYTDPPVKTKFGYHVI 120
Cdd:PRK04405  215 GE-----YTTTPVKTTYGYEVI 231
prsA PRK03002
peptidylprolyl isomerase PrsA;
33-126 1.33e-12

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 62.26  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  33 VKVRHILCEKQGKALEAIEKLKSGMKFNEVAAQYSEDKA--RSGGDLGWMTRGSMVGPFQDAAFALsnsscdKPIYTDPP 110
Cdd:PRK03002  137 IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLskEKGGDLGYFNSGRMAPEFETAAYKL------KVGQISNP 210

                          90
                  ....*....|....*.
gi 1845973183 111 VKTKFGYHVIMVEGKK 126
Cdd:PRK03002  211 VKSPNGYHIIKLTDKK 226
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 29-120 6.57e-12

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 57.73  E-value: 6.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  29 GGTAVKVRHILCE----------KQGKAL-----EAIEKLK--------SGMKFNEVAAQYSE-DKARSGGDLGWMTRGS 84
Cdd:PTZ00356    2 EGDTVRAAHLLIKhtgsrnpvsrRTGKPVtrskeEAIKELAkwreqivsGEKTFEEIARQRSDcGSAAKGGDLGFFGRGQ 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845973183  85 MVGPFQDAAFALsnsscdKPIYTDPPVKTKFGYHVI 120
Cdd:PTZ00356   82 MQKPFEDAAFAL------KVGEISDIVHTDSGVHII 111
prsA PRK00059
peptidylprolyl isomerase; Provisional
 30-126 4.23e-11

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 58.57  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  30 GTAVKVRHILCEKQGKALEAIEKLKSGMKFNEVAAQYSEDKA--RSGGDLGWM--TRGSMVGPFQDAAFALSNSSCDKpi 105
Cdd:PRK00059  194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGskDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISA-- 271

                          90       100
                  ....*....|....*....|.
gi 1845973183 106 ytdpPVKTKFGYHVIMVEGKK 126
Cdd:PRK00059  272 ----PVKTQFGYHIIKAIKKK 288
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 37-122 2.14e-09

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 50.79  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  37 HILCEKQGKALEAIEKLKSGMKFNEVAAQYSE-DKARSGGDLGWMTRGSMVGPFQDAAFalsnsSCDKpIYTDPPVKTKF 115
Cdd:PRK15441    9 HILVKEEKLALDLLEQIKNGADFGKLAKKHSIcPSGKRGGDLGEFRQGQMVPAFDKVVF-----SCPV-LEPTGPLHTQF 82


                  ....*..
gi 1845973183 116 GYHVIMV 122
Cdd:PRK15441   83 GYHIIKV 89
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 31-120 2.16e-09

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 53.59  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  31 TAVKVRHILC-------EKQGKA-LEAI-EKLKSG-MKFNEVAAQYSED--KARSGGDLGWMTrGSMVGP-FQDAAFALS 97
Cdd:PRK10770  265 TEVHARHILLkpspimtDEQARAkLEQIaADIKSGkTTFAAAAKEFSQDpgSANQGGDLGWAT-PDIFDPaFRDALMRLN 343

                          90       100
                  ....*....|....*....|...
gi 1845973183  98 NSScdkpiyTDPPVKTKFGYHVI 120
Cdd:PRK10770  344 KGQ------ISAPVHSSFGWHLI 360
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 46-92 3.98e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 41.53  E-value: 3.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1845973183  46 ALEAIEKLKSGMKFNEVAAQYSEDK--ARSGGDLGWMTRGSMVGPFQDA 92
Cdd:PRK10788  284 AKAVLDELKKGADFATLAKEKSTDIisARNGGDLGWLEPATTPDELKNA 332
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 28-122 4.49e-03

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 35.49  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845973183  28 GGGTAVKVRHIL--------------CEKQGKALeaIEKLKSGMKFNEVAAQYSED-KARSGGDLGWMTRGSMVGPFqda 92
Cdd:PRK10770  151 DASTELNLSHILiplpenptqdqvdeAESQARSI--VDQARNGADFGKLAIAYSADqQALKGGQMGWGRIQELPGLF--- 225

                          90       100       110
                  ....*....|....*....|....*....|
gi 1845973183  93 AFALSNSSCDKPIytdPPVKTKFGYHVIMV 122
Cdd:PRK10770  226 AQALSTAKKGDIV---GPIRSGVGFHILKV 252
 
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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