NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148225514|ref|NP_001084775|]
View 

peptidylprolyl cis/trans isomerase, NIMA-interacting 4 L homeolog [Xenopus laevis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 29-127 5.75e-30

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 105.04  E-value: 5.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  29 KGGNAVKVRHIL---------CEKHGKVMEAMEKLKSGVRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDAAFAL 97
Cdd:COG0760    4 DSPEEVRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFAL 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 148225514  98 S---VStmdkpvytdPPVKTKFGYHIIMVEGRK 127
Cdd:COG0760   84 KpgeIS---------GPVKTQFGYHIIKVEDRR 107
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 29-127 5.75e-30

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 105.04  E-value: 5.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  29 KGGNAVKVRHIL---------CEKHGKVMEAMEKLKSGVRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDAAFAL 97
Cdd:COG0760    4 DSPEEVRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFAL 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 148225514  98 S---VStmdkpvytdPPVKTKFGYHIIMVEGRK 127
Cdd:COG0760   84 KpgeIS---------GPVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 29-127 3.11e-22

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: 84.34  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514   29 KGGNAVKVRHILCEKHGKVMEA-----------MEKLKSGVRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDAAF 95
Cdd:pfam13616  11 SAPDSVKASHILISYSQAVSRTeeeakakadslLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVKEFEDAVF 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 148225514   96 ALSVSTMDKPVYTDppvktkFGYHIIMVEGRK 127
Cdd:pfam13616  91 SLKVGEISGVVKTQ------FGFHIIKVTDKK 116
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 34-127 6.90e-16

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 71.54  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  34 VKVRHILCEKHGKVMEAMEKLKSGVRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQDAAFALSVSTMDKpvytdpP 111
Cdd:PRK02998 135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                         90
                 ....*....|....*.
gi 148225514 112 VKTKFGYHIIMVEGRK 127
Cdd:PRK02998 209 VKTTYGYHIIKVTDKK 224
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 29-127 5.75e-30

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 105.04  E-value: 5.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  29 KGGNAVKVRHIL---------CEKHGKVMEAMEKLKSGVRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDAAFAL 97
Cdd:COG0760    4 DSPEEVRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFAL 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 148225514  98 S---VStmdkpvytdPPVKTKFGYHIIMVEGRK 127
Cdd:COG0760   84 KpgeIS---------GPVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 29-127 3.11e-22

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: 84.34  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514   29 KGGNAVKVRHILCEKHGKVMEA-----------MEKLKSGVRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDAAF 95
Cdd:pfam13616  11 SAPDSVKASHILISYSQAVSRTeeeakakadslLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVKEFEDAVF 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 148225514   96 ALSVSTMDKPVYTDppvktkFGYHIIMVEGRK 127
Cdd:pfam13616  91 SLKVGEISGVVKTQ------FGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 46-125 5.08e-19

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: 75.41  E-value: 5.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514   46 KVMEAMEKLKSGVR-FSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDAAFAL---SVStmdkpvytdPPVKTKFGYH 119
Cdd:pfam00639  20 KAEEILEQLKSGEDsFAELARKYSDDCpsAANGGDLGWFTRGQLPPEFEKAAFALkpgEIS---------GPVETRFGFH 90


                  ....*.
gi 148225514  120 IIMVEG 125
Cdd:pfam00639  91 IIKLTD 96
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 34-127 6.90e-16

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 71.54  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  34 VKVRHILCEKHGKVMEAMEKLKSGVRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQDAAFALSVSTMDKpvytdpP 111
Cdd:PRK02998 135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                         90
                 ....*....|....*.
gi 148225514 112 VKTKFGYHIIMVEGRK 127
Cdd:PRK02998 209 VKTTYGYHIIKVTDKK 224
prsA PRK03095
peptidylprolyl isomerase PrsA;
34-123 1.92e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 70.41  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  34 VKVRHILCEKHGKVMEAMEKLKSGVRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQDAAFALsvstmdKPVYTDPP 111
Cdd:PRK03095 133 IKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGskEKGGDLGFFGAGKMVKEFEDAAYKL------KKDEVSEP 206

                         90
                 ....*....|..
gi 148225514 112 VKTKFGYHIIMV 123
Cdd:PRK03095 207 VKSQFGYHIIKV 218
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 55-121 2.27e-14

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 64.28  E-value: 2.27e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148225514  55 KSGVRFSEVATQYSE-DKARQGGDLGWMTRGSMVGPFQDAAFALSVSTMDKPVYTDPpvktkfGYHII 121
Cdd:PTZ00356  50 SGEKTFEEIARQRSDcGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDS------GVHII 111
prsA PRK03002
peptidylprolyl isomerase PrsA;
34-127 6.01e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 66.11  E-value: 6.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  34 VKVRHILCEKHGKVMEAMEKLKSGVRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQDAAFALSVSTMDKpvytdpP 111
Cdd:PRK03002 137 IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLskEKGGDLGYFNSGRMAPEFETAAYKLKVGQISN------P 210

                         90
                 ....*....|....*.
gi 148225514 112 VKTKFGYHIIMVEGRK 127
Cdd:PRK03002 211 VKSPNGYHIIKLTDKK 226
prsA PRK00059
peptidylprolyl isomerase; Provisional
 22-127 1.31e-12

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 62.81  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  22 DKKAQTPKGgnaVKVRHILCEKHGKVMEAMEKLKSGVRFSEVATQYSEDKA--RQGGDLGWM--TRGSMVGPFQDAAFAL 97
Cdd:PRK00059 188 SKFTEKPNT---MHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGskDKGGDLGDVpySDSGYDKEFMDGAKAL 264

                         90       100       110
                 ....*....|....*....|....*....|
gi 148225514  98 SVSTMDKpvytdpPVKTKFGYHIIMVEGRK 127
Cdd:PRK00059 265 KEGEISA------PVKTQFGYHIIKAIKKK 288
prsA PRK04405
peptidylprolyl isomerase; Provisional
 24-121 1.61e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 56.72  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  24 KAQTPKggnaVKVRHILCEKHGKVMEAMEKLKSGVRFSEVATQYSEDKA--RQGGDLGW--MTRGSMVGPFQDAAFALSV 99
Cdd:PRK04405 139 KSYQPK----VTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTAtkNKGGKLSAfdSTDTTLDSTFKTAAFKLKN 214

                         90       100
                 ....*....|....*....|..
gi 148225514 100 STmdkpvYTDPPVKTKFGYHII 121
Cdd:PRK04405 215 GE-----YTTTPVKTTYGYEVI 231
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 29-121 2.39e-10

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 56.29  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  29 KGGNA------VKVRHILC---------EKHGKVMEAMEKLKSG-VRFSEVATQYSED--KARQGGDLGWMTrGSMVGP- 89
Cdd:PRK10770 256 RGESQnisvteVHARHILLkpspimtdeQARAKLEQIAADIKSGkTTFAAAAKEFSQDpgSANQGGDLGWAT-PDIFDPa 334

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148225514  90 FQDAAFALSVSTMDKPVYTDppvktkFGYHII 121
Cdd:PRK10770 335 FRDALMRLNKGQISAPVHSS------FGWHLI 360
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 38-127 1.48e-09

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 51.18  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148225514  38 HILCEKHGKVMEAMEKLKSGVRFSEVATQYSE-DKARQGGDLGWMTRGSMVGPFQDAAFALSVstmdkpVYTDPPVKTKF 116
Cdd:PRK15441   9 HILVKEEKLALDLLEQIKNGADFGKLAKKHSIcPSGKRGGDLGEFRQGQMVPAFDKVVFSCPV------LEPTGPLHTQF 82

                         90
                 ....*....|.
gi 148225514 117 GYHIIMVEGRK 127
Cdd:PRK15441  83 GYHIIKVLYRN 93
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 49-93 7.09e-06

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 43.84  E-value: 7.09e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 148225514  49 EAMEKLKSGVRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQDA 93
Cdd:PRK10788 286 AVLDELKKGADFATLAKEKSTDIisARNGGDLGWLEPATTPDELKNA 332
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 51-123 4.42e-03

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 35.49  E-value: 4.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148225514  51 MEKLKSGVRFSEVATQYSED-KARQGGDLGWmtrgsmvGPFQD--AAFALSVSTMDKPVYTDpPVKTKFGYHIIMV 123
Cdd:PRK10770 185 VDQARNGADFGKLAIAYSADqQALKGGQMGW-------GRIQElpGLFAQALSTAKKGDIVG-PIRSGVGFHILKV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH