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Conserved domains on  [gi|157817696|ref|NP_001100171|]
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peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Rattus norvegicus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 13628690)

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|2.20.70.10
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  12871165|16807295|11812645
SCOP:  3000622

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rotamase_2 super family cl29122
PPIC-type PPIASE domain;
53-164 1.41e-51

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PTZ00356:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 115  Bit Score: 160.19  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  53 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 131
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157817696 132 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 164
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 7-37 1.38e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 58.67  E-value: 1.38e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 157817696    7 LPSGWEKRMSrSSGRVYYFNHITNASQWERP 37
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 53-164 1.41e-51

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 160.19  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  53 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 131
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157817696 132 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 164
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 53-165 7.38e-27

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 98.49  E-value: 7.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  53 EPARVRCSHLLVKHSQSrrpsswrqEKITRSKEEALELIngyiQKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQ 131
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELL----AQLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 157817696 132 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 61-165 8.78e-27

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: 96.60  E-value: 8.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696   61 HLLVKHsqsrrpsswrQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMQKPFEDA 139
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 157817696  140 SFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 7-37 1.38e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 58.67  E-value: 1.38e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 157817696    7 LPSGWEKRMSrSSGRVYYFNHITNASQWERP 37
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 8-37 1.02e-11

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.38  E-value: 1.02e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 157817696   8 PSGWEKRMSRSsGRVYYFNHITNASQWERP 37
Cdd:cd00201    1 PPGWEERWDPD-GRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 7-37 2.22e-11

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 55.30  E-value: 2.22e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 157817696     7 LPSGWEKRMSRSsGRVYYFNHITNASQWERP 37
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKP 31
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 53-164 1.41e-51

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 160.19  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  53 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 131
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157817696 132 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 164
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 53-165 7.38e-27

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 98.49  E-value: 7.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  53 EPARVRCSHLLVKHSQSrrpsswrqEKITRSKEEALELIngyiQKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQ 131
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELL----AQLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 157817696 132 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 61-165 8.78e-27

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: 96.60  E-value: 8.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696   61 HLLVKHsqsrrpsswrQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMQKPFEDA 139
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 157817696  140 SFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 54-161 2.06e-26

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: 96.28  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696   54 PARVRCSHLLVKHSQsrrpsswrqeKITRSKEEALELINGYIQKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQM 132
Cdd:pfam13616  13 PDSVKASHILISYSQ----------AVSRTEEEAKAKADSLLAALKNGA-DFAALAKTYSdDPASKNNGGDLGWFTKGQM 81

                          90       100
                  ....*....|....*....|....*....
gi 157817696  133 QKPFEDASFALRTGEMSGPVFTDSGIHII 161
Cdd:pfam13616  82 VKEFEDAVFSLKVGEISGVVKTQFGFHII 110
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 7-37 1.38e-12

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 58.67  E-value: 1.38e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 157817696    7 LPSGWEKRMSrSSGRVYYFNHITNASQWERP 37
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 84-161 6.04e-12

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 58.50  E-value: 6.04e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157817696  84 KEEALELinGYIQKIKSGEeDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHII 161
Cdd:PRK15441  13 KEEKLAL--DLLEQIKNGA-DFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 56-165 6.23e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 61.91  E-value: 6.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  56 RVRCSHLLVKhsqsrrpsswrQEKITRSKEEalelingyiqKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQMQK 134
Cdd:PRK02998 134 EMKVSHILVK-----------DEKTAKEVKE----------KVNNGE-DFAALAKQYSeDTGSKEQGGEISGFAPGQTVK 191

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157817696 135 PFEDASFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:PRK02998 192 EFEEAAYKLDAGQVSEPVKTTYGYHIIKVTD 222
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 8-37 1.02e-11

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.38  E-value: 1.02e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 157817696   8 PSGWEKRMSRSsGRVYYFNHITNASQWERP 37
Cdd:cd00201    1 PPGWEERWDPD-GRVYYYNHNTKETQWEDP 29
prsA PRK03095
peptidylprolyl isomerase PrsA;
56-165 1.43e-11

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 60.78  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  56 RVRCSHLLVKHsqsrrpsswrQEKITRSKEEaleLINGyiqkiksgeEDFESLASQFS-DCSSAKARGDLGAFSRGQMQK 134
Cdd:PRK03095 132 EIKASHILVKD----------EATAKKVKEE---LGQG---------KSFEELAKQYSeDTGSKEKGGDLGFFGAGKMVK 189

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157817696 135 PFEDASFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:PRK03095 190 EFEDAAYKLKKDEVSEPVKSQFGYHIIKVTD 220
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 7-37 2.22e-11

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 55.30  E-value: 2.22e-11
                           10        20        30
                   ....*....|....*....|....*....|.
gi 157817696     7 LPSGWEKRMSRSsGRVYYFNHITNASQWERP 37
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKP 31
prsA PRK00059
peptidylprolyl isomerase; Provisional
 54-161 3.74e-09

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 54.33  E-value: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  54 PARVRCSHLLVKhsqsrrpsswrqekitrSKEEAlelingyiQKIKS---GEEDFESLASQFS-DCSSAKARGDLG--AF 127
Cdd:PRK00059 194 PNTMHLAHILVK-----------------TEDEA--------KKVKKrldKGEDFAKVAKEVSqDPGSKDKGGDLGdvPY 248

                         90       100       110
                 ....*....|....*....|....*....|....
gi 157817696 128 SRGQMQKPFEDASFALRTGEMSGPVFTDSGIHII 161
Cdd:PRK00059 249 SDSGYDKEFMDGAKALKEGEISAPVKTQFGYHII 282
prsA PRK03002
peptidylprolyl isomerase PrsA;
105-165 4.10e-09

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 53.79  E-value: 4.10e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817696 105 FESLASQFS-DCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 165
Cdd:PRK03002 163 FEELAKQESqDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTD 224
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 57-161 1.69e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 49.35  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  57 VRCSHLLVKhsqsrrPSSWRQEKITRSKEEALElingyiQKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMQKP 135
Cdd:PRK10770 267 VHARHILLK------PSPIMTDEQARAKLEQIA------ADIKSGKTTFAAAAKEFSqDPGSANQGGDLGWATPDIFDPA 334

                         90       100
                 ....*....|....*....|....*.
gi 157817696 136 FEDASFALRTGEMSGPVFTDSGIHII 161
Cdd:PRK10770 335 FRDALMRLNKGQISAPVHSSFGWHLI 360
prsA PRK04405
peptidylprolyl isomerase; Provisional
 63-161 5.70e-07

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 47.86  E-value: 5.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817696  63 LVKHSQSRRPSSWR--QEKIT-----RSKEEALELIngyIQKIKSGEeDFESLASQFS-DCSSAKARGDLGAF--SRGQM 132
Cdd:PRK04405 126 LKKVTNSQLKKAWKsyQPKVTvqhilVSKKSTAETV---IKKLKDGK-DFAKLAKKYStDTATKNKGGKLSAFdsTDTTL 201

                         90       100       110
                 ....*....|....*....|....*....|
gi 157817696 133 QKPFEDASFALRTGEM-SGPVFTDSGIHII 161
Cdd:PRK04405 202 DSTFKTAAFKLKNGEYtTTPVKTTYGYEVI 231
 
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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