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Conserved domains on  [gi|2189165803|ref|NP_001388141|]
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peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 isoform 2 [Rattus norvegicus]

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, ...
 49-142 8.50e-31

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 107.74  E-value: 8.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHIL---------CEKHGKIMEAMEKLKSGMRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---V 114
Cdd:COG0760     9 VRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFALKpgeI 88

                          90       100
                  ....*....|....*....|....*...
gi 2189165803 115 SGmdkpvftdpPVKTKFGYHIIMVEGRK 142
Cdd:COG0760    89 SG---------PVKTQFGYHIIKVEDRR 107
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 49-142 8.50e-31

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 107.74  E-value: 8.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHIL---------CEKHGKIMEAMEKLKSGMRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---V 114
Cdd:COG0760     9 VRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFALKpgeI 88

                          90       100
                  ....*....|....*....|....*...
gi 2189165803 115 SGmdkpvftdpPVKTKFGYHIIMVEGRK 142
Cdd:COG0760    89 SG---------PVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 41-142 1.31e-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: 85.88  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  41 GPKGGGNAVKVRHIL-----------CEKHGKIMEAMEKLKSGMRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQE 107
Cdd:pfam13616   8 DKKSAPDSVKASHILisysqavsrteEEAKAKADSLLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVKEFED 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2189165803 108 AAFALPVSGMDKpvftdpPVKTKFGYHIIMVEGRK 142
Cdd:pfam13616  88 AVFSLKVGEISG------VVKTQFGFHIIKVTDKK 116
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 49-142 6.36e-16

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 71.93  E-value: 6.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHILCEKHGKIMEAMEKLKSGMRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKpvftdpP 126
Cdd:PRK02998  135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                          90
                  ....*....|....*.
gi 2189165803 127 VKTKFGYHIIMVEGRK 142
Cdd:PRK02998  209 VKTTYGYHIIKVTDKK 224
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 49-142 8.50e-31

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 107.74  E-value: 8.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHIL---------CEKHGKIMEAMEKLKSGMRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---V 114
Cdd:COG0760     9 VRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFALKpgeI 88

                          90       100
                  ....*....|....*....|....*...
gi 2189165803 115 SGmdkpvftdpPVKTKFGYHIIMVEGRK 142
Cdd:COG0760    89 SG---------PVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 41-142 1.31e-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: 85.88  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  41 GPKGGGNAVKVRHIL-----------CEKHGKIMEAMEKLKSGMRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQE 107
Cdd:pfam13616   8 DKKSAPDSVKASHILisysqavsrteEEAKAKADSLLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVKEFED 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2189165803 108 AAFALPVSGMDKpvftdpPVKTKFGYHIIMVEGRK 142
Cdd:pfam13616  88 AVFSLKVGEISG------VVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 61-140 1.76e-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: 77.34  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  61 KIMEAMEKLKSGMR-FSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---VSGmdkpvftdpPVKTKFGYH 134
Cdd:pfam00639  20 KAEEILEQLKSGEDsFAELARKYSDDCpsAANGGDLGWFTRGQLPPEFEKAAFALKpgeISG---------PVETRFGFH 90


                  ....*.
gi 2189165803 135 IIMVEG 140
Cdd:pfam00639  91 IIKLTD 96
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 49-142 6.36e-16

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 71.93  E-value: 6.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHILCEKHGKIMEAMEKLKSGMRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKpvftdpP 126
Cdd:PRK02998  135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                          90
                  ....*....|....*.
gi 2189165803 127 VKTKFGYHIIMVEGRK 142
Cdd:PRK02998  209 VKTTYGYHIIKVTDKK 224
prsA PRK03095
peptidylprolyl isomerase PrsA;
49-138 1.70e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 71.18  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHILCEKHGKIMEAMEKLKSGMRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALpvsgmdKPVFTDPP 126
Cdd:PRK03095  133 IKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGskEKGGDLGFFGAGKMVKEFEDAAYKL------KKDEVSEP 206

                          90
                  ....*....|..
gi 2189165803 127 VKTKFGYHIIMV 138
Cdd:PRK03095  207 VKSQFGYHIIKV 218
prsA PRK03002
peptidylprolyl isomerase PrsA;
49-142 4.53e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 66.88  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHILCEKHGKIMEAMEKLKSGMRFSEVATQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKpvftdpP 126
Cdd:PRK03002  137 IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLskEKGGDLGYFNSGRMAPEFETAAYKLKVGQISN------P 210

                          90
                  ....*....|....*.
gi 2189165803 127 VKTKFGYHIIMVEGRK 142
Cdd:PRK03002  211 VKSPNGYHIIKLTDKK 226
prsA PRK00059
peptidylprolyl isomerase; Provisional
 46-142 8.28e-13

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 63.96  E-value: 8.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  46 GNAVKVRHILCEKHGKIMEAMEKLKSGMRFSEVATQYSEDKA--RQGGDLGWM--TRGSMVGPFQEAAFALPVSGMDKpv 121
Cdd:PRK00059  194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGskDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISA-- 271

                          90       100
                  ....*....|....*....|.
gi 2189165803 122 ftdpPVKTKFGYHIIMVEGRK 142
Cdd:PRK00059  272 ----PVKTQFGYHIIKAIKKK 288
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 70-136 1.49e-12

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 60.04  E-value: 1.49e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2189165803  70 KSGMRFSEVATQYSE-DKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPpvktkfGYHII 136
Cdd:PTZ00356   50 SGEKTFEEIARQRSDcGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDS------GVHII 111
prsA PRK04405
peptidylprolyl isomerase; Provisional
 38-136 1.35e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 57.49  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  38 KSQGPKgggnaVKVRHILCEKHGKIMEAMEKLKSGMRFSEVATQYSEDKA--RQGGDLGW--MTRGSMVGPFQEAAFALp 113
Cdd:PRK04405  139 KSYQPK-----VTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTAtkNKGGKLSAfdSTDTTLDSTFKTAAFKL- 212

                          90       100
                  ....*....|....*....|...
gi 2189165803 114 vsgmDKPVFTDPPVKTKFGYHII 136
Cdd:PRK04405  213 ----KNGEYTTTPVKTTYGYEVI 231
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 53-142 1.55e-10

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 54.26  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  53 HILCEKHGKIMEAMEKLKSGMRFSEVATQYSE-DKARQGGDLGWMTRGSMVGPFQEAAFALPVsgmdkpVFTDPPVKTKF 131
Cdd:PRK15441    9 HILVKEEKLALDLLEQIKNGADFGKLAKKHSIcPSGKRGGDLGEFRQGQMVPAFDKVVFSCPV------LEPTGPLHTQF 82

                          90
                  ....*....|.
gi 2189165803 132 GYHIIMVEGRK 142
Cdd:PRK15441   83 GYHIIKVLYRN 93
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 49-136 2.70e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 51.28  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2189165803  49 VKVRHILC---------EKHGKIMEAMEKLKSG-MRFSEVATQYSED--KARQGGDLGWMTrGSMVGP-FQEAAFALPVS 115
Cdd:PRK10770  267 VHARHILLkpspimtdeQARAKLEQIAADIKSGkTTFAAAAKEFSQDpgSANQGGDLGWAT-PDIFDPaFRDALMRLNKG 345

                          90       100
                  ....*....|....*....|.
gi 2189165803 116 GMDKpvftdpPVKTKFGYHII 136
Cdd:PRK10770  346 QISA------PVHSSFGWHLI 360
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 64-108 1.56e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 43.07  E-value: 1.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2189165803  64 EAMEKLKSGMRFSEVATQYSEDK--ARQGGDLGWMTRGSMVGPFQEA 108
Cdd:PRK10788  286 AVLDELKKGADFATLAKEKSTDIisARNGGDLGWLEPATTPDELKNA 332
 
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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