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Conserved domains on  [gi|568916966|ref|XP_006499551|]
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peptidylprolyl cis/trans isomerase, NIMA-interacting 1 isoform X1 [Mus musculus]

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;
47-158 2.27e-49

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PTZ00356:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 115  Bit Score: 154.41  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  47 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRSKEEALELINGYIRKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 125
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568916966 126 MEKPFEDASFALRTGEMSGPVFTESGIHIILRT 158
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 6-36 6.51e-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: 56.74  E-value: 6.51e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568916966    6 LPPGWKKYMSrSSGREYYFNHITNASQWERP 36
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 47-158 2.27e-49

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 154.41  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  47 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRSKEEALELINGYIRKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 125
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568916966 126 MEKPFEDASFALRTGEMSGPVFTESGIHIILRT 158
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 47-159 4.69e-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: 4.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  47 EPARVRCSHLLVKHSQSrrpsswrqEKITRSKEEALELINgyirKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQ 125
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELLA----QLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568916966 126 MEKPFEDASFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 55-159 2.56e-26

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: 95.44  E-value: 2.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966   55 HLLVKHsqsrrpsswrQEKITRSKEEALELINGYIRKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMEKPFEDA 133
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 568916966  134 SFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 6-36 6.51e-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: 56.74  E-value: 6.51e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568916966    6 LPPGWKKYMSrSSGREYYFNHITNASQWERP 36
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 7-38 1.07e-10

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: 53.30  E-value: 1.07e-10
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568916966   7 PPGWKKYMSRSsGREYYFNHITNASQWERPSE 38
Cdd:cd00201    1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 6-38 1.82e-10

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: 52.99  E-value: 1.82e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568916966     6 LPPGWKKYMSRSsGREYYFNHITNASQWERPSE 38
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 47-158 2.27e-49

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 154.41  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  47 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRSKEEALELINGYIRKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 125
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568916966 126 MEKPFEDASFALRTGEMSGPVFTESGIHIILRT 158
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 47-159 4.69e-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: 4.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  47 EPARVRCSHLLVKHSQSrrpsswrqEKITRSKEEALELINgyirKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQ 125
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELLA----QLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568916966 126 MEKPFEDASFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 55-159 2.56e-26

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: 95.44  E-value: 2.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966   55 HLLVKHsqsrrpsswrQEKITRSKEEALELINGYIRKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMEKPFEDA 133
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 568916966  134 SFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 48-155 7.16e-25

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: 92.43  E-value: 7.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966   48 PARVRCSHLLVKHSQsrrpsswrqeKITRSKEEALELINGYIRKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQM 126
Cdd:pfam13616  13 PDSVKASHILISYSQ----------AVSRTEEEAKAKADSLLAALKNGA-DFAALAKTYSdDPASKNNGGDLGWFTKGQM 81

                          90       100
                  ....*....|....*....|....*....
gi 568916966  127 EKPFEDASFALRTGEMSGPVFTESGIHII 155
Cdd:pfam13616  82 VKEFEDAVFSLKVGEISGVVKTQFGFHII 110
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 78-155 4.92e-12

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 58.50  E-value: 4.92e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568916966  78 KEEALELinGYIRKIKSGEeDFESLASQFSDCSSAKARGDLGAFSRGQMEKPFEDASFALRTGEMSGPVFTESGIHII 155
Cdd:PRK15441  13 KEEKLAL--DLLEQIKNGA-DFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 6-36 6.51e-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: 56.74  E-value: 6.51e-12
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568916966    6 LPPGWKKYMSrSSGREYYFNHITNASQWERP 36
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
prsA PRK03095
peptidylprolyl isomerase PrsA;
50-159 7.20e-12

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 61.55  E-value: 7.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  50 RVRCSHLLVKHsqsrrpsswrQEKITRSKEEaleLINGyirkiksgeEDFESLASQFS-DCSSAKARGDLGAFSRGQMEK 128
Cdd:PRK03095 132 EIKASHILVKD----------EATAKKVKEE---LGQG---------KSFEELAKQYSeDTGSKEKGGDLGFFGAGKMVK 189

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568916966 129 PFEDASFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:PRK03095 190 EFEDAAYKLKKDEVSEPVKSQFGYHIIKVTD 220
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 50-159 7.81e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 61.53  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  50 RVRCSHLLVKhsqsrrpsswrQEKITRSKEEalelingyirKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQMEK 128
Cdd:PRK02998 134 EMKVSHILVK-----------DEKTAKEVKE----------KVNNGE-DFAALAKQYSeDTGSKEQGGEISGFAPGQTVK 191

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568916966 129 PFEDASFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:PRK02998 192 EFEEAAYKLDAGQVSEPVKTTYGYHIIKVTD 222
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 7-38 1.07e-10

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: 53.30  E-value: 1.07e-10
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568916966   7 PPGWKKYMSRSsGREYYFNHITNASQWERPSE 38
Cdd:cd00201    1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 6-38 1.82e-10

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: 52.99  E-value: 1.82e-10
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568916966     6 LPPGWKKYMSRSsGREYYFNHITNASQWERPSE 38
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
prsA PRK00059
peptidylprolyl isomerase; Provisional
 48-155 3.03e-09

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 54.33  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  48 PARVRCSHLLVKhsqsrrpsswrqekitrSKEEAlelingyiRKIKS---GEEDFESLASQFS-DCSSAKARGDLG--AF 121
Cdd:PRK00059 194 PNTMHLAHILVK-----------------TEDEA--------KKVKKrldKGEDFAKVAKEVSqDPGSKDKGGDLGdvPY 248

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568916966 122 SRGQMEKPFEDASFALRTGEMSGPVFTESGIHII 155
Cdd:PRK00059 249 SDSGYDKEFMDGAKALKEGEISAPVKTQFGYHII 282
prsA PRK03002
peptidylprolyl isomerase PrsA;
90-159 3.94e-09

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 53.79  E-value: 3.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568916966  90 RKIKSGEEdFESLASQFS-DCSSAKARGDLGAFSRGQMEKPFEDASFALRTGEMSGPVFTESGIHIILRTE 159
Cdd:PRK03002 155 KKLDAGAS-FEELAKQESqDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTD 224
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 51-155 5.26e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 50.89  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  51 VRCSHLLVKhsqsrrPSSWRQEKITRSKEEALElingyiRKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMEKP 129
Cdd:PRK10770 267 VHARHILLK------PSPIMTDEQARAKLEQIA------ADIKSGKTTFAAAAKEFSqDPGSANQGGDLGWATPDIFDPA 334

                         90       100
                 ....*....|....*....|....*.
gi 568916966 130 FEDASFALRTGEMSGPVFTESGIHII 155
Cdd:PRK10770 335 FRDALMRLNKGQISAPVHSSFGWHLI 360
prsA PRK04405
peptidylprolyl isomerase; Provisional
 57-155 1.22e-07

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 49.40  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568916966  57 LVKHSQSRRPSSWR--QEKIT-----RSKEEALELIngyIRKIKSGEeDFESLASQFS-DCSSAKARGDLGAF--SRGQM 126
Cdd:PRK04405 126 LKKVTNSQLKKAWKsyQPKVTvqhilVSKKSTAETV---IKKLKDGK-DFAKLAKKYStDTATKNKGGKLSAFdsTDTTL 201

                         90       100       110
                 ....*....|....*....|....*....|
gi 568916966 127 EKPFEDASFALRTGEM-SGPVFTESGIHII 155
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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