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Conserved domains on  [gi|1536901840|ref|NP_006214|]
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peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 isoform 1 [Homo sapiens]

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, ...
 38-131 1.58e-30

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


:

Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 106.58  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHIL---------CEKHGKIMEAMEKLKSGMRFNEVAAQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---V 103
Cdd:COG0760     9 VRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFALKpgeI 88

                          90       100
                  ....*....|....*....|....*...
gi 1536901840 104 SGmdkpvftdpPVKTKFGYHIIMVEGRK 131
Cdd:COG0760    89 SG---------PVKTQFGYHIIKVEDRR 107
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 38-131 1.58e-30

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 106.58  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHIL---------CEKHGKIMEAMEKLKSGMRFNEVAAQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---V 103
Cdd:COG0760     9 VRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFALKpgeI 88

                          90       100
                  ....*....|....*....|....*...
gi 1536901840 104 SGmdkpvftdpPVKTKFGYHIIMVEGRK 131
Cdd:COG0760    89 SG---------PVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 26-131 4.77e-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: 83.96  E-value: 4.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  26 KKAQGPKGGGNAVKVRHIL-----------CEKHGKIMEAMEKLKSGMRFNEVAAQYSEDK--ARQGGDLGWMTRGSMVG 92
Cdd:pfam13616   4 SKLVDKKSAPDSVKASHILisysqavsrteEEAKAKADSLLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVK 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1536901840  93 PFQEAAFALPVSGMDKpvftdpPVKTKFGYHIIMVEGRK 131
Cdd:pfam13616  84 EFEDAVFSLKVGEISG------VVKTQFGFHIIKVTDKK 116
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 38-131 2.46e-15

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 70.00  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKpvftdpP 115
Cdd:PRK02998  135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                          90
                  ....*....|....*.
gi 1536901840 116 VKTKFGYHIIMVEGRK 131
Cdd:PRK02998  209 VKTTYGYHIIKVTDKK 224
 
Name Accession Description Interval E-value
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 38-131 1.58e-30

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 106.58  E-value: 1.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHIL---------CEKHGKIMEAMEKLKSGMRFNEVAAQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---V 103
Cdd:COG0760     9 VRASHILvkvppsedrAKAEAKAEELLAQLKAGADFAELAKEYSQDPgsAANGGDLGWFSRGQLVPEFEEAAFALKpgeI 88

                          90       100
                  ....*....|....*....|....*...
gi 1536901840 104 SGmdkpvftdpPVKTKFGYHIIMVEGRK 131
Cdd:COG0760    89 SG---------PVKTQFGYHIIKVEDRR 107
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 26-131 4.77e-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: 83.96  E-value: 4.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  26 KKAQGPKGGGNAVKVRHIL-----------CEKHGKIMEAMEKLKSGMRFNEVAAQYSEDK--ARQGGDLGWMTRGSMVG 92
Cdd:pfam13616   4 SKLVDKKSAPDSVKASHILisysqavsrteEEAKAKADSLLAALKNGADFAALAKTYSDDPasKNNGGDLGWFTKGQMVK 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1536901840  93 PFQEAAFALPVSGMDKpvftdpPVKTKFGYHIIMVEGRK 131
Cdd:pfam13616  84 EFEDAVFSLKVGEISG------VVKTQFGFHIIKVTDKK 116
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 50-129 5.03e-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: 75.80  E-value: 5.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  50 KIMEAMEKLKSGMR-FNEVAAQYSEDK--ARQGGDLGWMTRGSMVGPFQEAAFALP---VSGmdkpvftdpPVKTKFGYH 123
Cdd:pfam00639  20 KAEEILEQLKSGEDsFAELARKYSDDCpsAANGGDLGWFTRGQLPPEFEKAAFALKpgeISG---------PVETRFGFH 90


                  ....*.
gi 1536901840 124 IIMVEG 129
Cdd:pfam00639  91 IIKLTD 96
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 38-131 2.46e-15

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 70.00  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKpvftdpP 115
Cdd:PRK02998  135 MKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGskEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSE------P 208

                          90
                  ....*....|....*.
gi 1536901840 116 VKTKFGYHIIMVEGRK 131
Cdd:PRK02998  209 VKTTYGYHIIKVTDKK 224
prsA PRK03095
peptidylprolyl isomerase PrsA;
38-127 4.26e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 69.64  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALpvsgmdKPVFTDPP 115
Cdd:PRK03095  133 IKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGskEKGGDLGFFGAGKMVKEFEDAAYKL------KKDEVSEP 206

                          90
                  ....*....|..
gi 1536901840 116 VKTKFGYHIIMV 127
Cdd:PRK03095  207 VKSQFGYHIIKV 218
prsA PRK03002
peptidylprolyl isomerase PrsA;
38-131 8.08e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 66.11  E-value: 8.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKA--RQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKpvftdpP 115
Cdd:PRK03002  137 IKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLskEKGGDLGYFNSGRMAPEFETAAYKLKVGQISN------P 210

                          90
                  ....*....|....*.
gi 1536901840 116 VKTKFGYHIIMVEGRK 131
Cdd:PRK03002  211 VKSPNGYHIIKLTDKK 226
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 59-125 7.93e-13

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 60.42  E-value: 7.93e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1536901840  59 KSGMRFNEVAAQYSE-DKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPpvktkfGYHII 125
Cdd:PTZ00356   50 SGEKTFEEIARQRSDcGSAAKGGDLGFFGRGQMQKPFEDAAFALKVGEISDIVHTDS------GVHII 111
prsA PRK00059
peptidylprolyl isomerase; Provisional
 35-131 1.07e-11

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 60.49  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  35 GNAVKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKA--RQGGDLGWM--TRGSMVGPFQEAAFALPVSGMDKpv 110
Cdd:PRK00059  194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGskDKGGDLGDVpySDSGYDKEFMDGAKALKEGEISA-- 271

                          90       100
                  ....*....|....*....|.
gi 1536901840 111 ftdpPVKTKFGYHIIMVEGRK 131
Cdd:PRK00059  272 ----PVKTQFGYHIIKAIKKK 288
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 42-131 2.31e-10

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 53.49  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  42 HILCEKHGKIMEAMEKLKSGMRFNEVAAQYSE-DKARQGGDLGWMTRGSMVGPFQEAAFALPVsgmdkpVFTDPPVKTKF 120
Cdd:PRK15441    9 HILVKEEKLALDLLEQIKNGADFGKLAKKHSIcPSGKRGGDLGEFRQGQMVPAFDKVVFSCPV------LEPTGPLHTQF 82

                          90
                  ....*....|.
gi 1536901840 121 GYHIIMVEGRK 131
Cdd:PRK15441   83 GYHIIKVLYRN 93
prsA PRK04405
peptidylprolyl isomerase; Provisional
 38-125 9.37e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 54.79  E-value: 9.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKA--RQGGDLGW--MTRGSMVGPFQEAAFALpvsgmDKPVFTD 113
Cdd:PRK04405  145 VTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTAtkNKGGKLSAfdSTDTTLDSTFKTAAFKL-----KNGEYTT 219

                          90
                  ....*....|..
gi 1536901840 114 PPVKTKFGYHII 125
Cdd:PRK04405  220 TPVKTTYGYEVI 231
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 38-125 3.02e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 50.51  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1536901840  38 VKVRHILC---------EKHGKIMEAMEKLKSG-MRFNEVAAQYSED--KARQGGDLGWMTrGSMVGP-FQEAAFALPVS 104
Cdd:PRK10770  267 VHARHILLkpspimtdeQARAKLEQIAADIKSGkTTFAAAAKEFSQDpgSANQGGDLGWAT-PDIFDPaFRDALMRLNKG 345

                          90       100
                  ....*....|....*....|.
gi 1536901840 105 GMDKpvftdpPVKTKFGYHII 125
Cdd:PRK10770  346 QISA------PVHSSFGWHLI 360
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 53-97 3.83e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 41.92  E-value: 3.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1536901840  53 EAMEKLKSGMRFNEVAAQYSEDK--ARQGGDLGWMTRGSMVGPFQEA 97
Cdd:PRK10788  286 AVLDELKKGADFATLAKEKSTDIisARNGGDLGWLEPATTPDELKNA 332
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 55-127 6.46e-03

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 35.10  E-value: 6.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1536901840  55 MEKLKSGMRFNEVAAQYSED-KARQGGDLGWmtrgsmvGPFQE--AAFALPVSGMDKPVFTDpPVKTKFGYHIIMV 127
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.
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