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Conserved domains on  [gi|806394255]
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Chain A, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

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;
69-180 1.73e-49

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PTZ00356:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 115  Bit Score: 155.57  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  69 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRTKEEALELINGYIQKIKSGEEDFESLASQFSD*SSAKARGDLGAFSRGQ 147
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 806394255 148 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 180
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 25-55 9.84e-13

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: 59.44  E-value: 9.84e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 806394255   25 LPPGWEKAMSrSSGRVYYFNHITNASQWERP 55
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 69-180 1.73e-49

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 155.57  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  69 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRTKEEALELINGYIQKIKSGEEDFESLASQFSD*SSAKARGDLGAFSRGQ 147
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 806394255 148 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 180
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 70-177 7.05e-27

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: 98.21  E-value: 7.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255   70 PARVRCSHLLVKHSQsrrpsswrqeKITRTKEEALELINGYIQKIKSGEeDFESLASQFS-D*SSAKARGDLGAFSRGQM 148
Cdd:pfam13616  13 PDSVKASHILISYSQ----------AVSRTEEEAKAKADSLLAALKNGA-DFAALAKTYSdDPASKNNGGDLGWFTKGQM 81

                          90       100
                  ....*....|....*....|....*....
gi 806394255  149 QKPFEDASFALRTGEMSGPVFTDSGIHII 177
Cdd:pfam13616  82 VKEFEDAVFSLKVGEISGVVKTQFGFHII 110
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 69-181 9.29e-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: 9.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  69 EPARVRCSHLLVKHSQSrrpsswrqEKITRTKEEALELIngyiQKIKSGEeDFESLASQFS-D*SSAKARGDLGAFSRGQ 147
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELL----AQLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 806394255 148 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 181
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 25-55 9.84e-13

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: 59.44  E-value: 9.84e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 806394255   25 LPPGWEKAMSrSSGRVYYFNHITNASQWERP 55
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 26-55 9.88e-12

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: 56.77  E-value: 9.88e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 806394255  26 PPGWEKAMSRSsGRVYYFNHITNASQWERP 55
Cdd:cd00201    1 PPGWEERWDPD-GRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 25-57 2.07e-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: 55.68  E-value: 2.07e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 806394255    25 LPPGWEKAMSRSsGRVYYFNHITNASQWERPSG 57
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 69-180 1.73e-49

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 155.57  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  69 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRTKEEALELINGYIQKIKSGEEDFESLASQFSD*SSAKARGDLGAFSRGQ 147
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 806394255 148 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 180
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 70-177 7.05e-27

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: 98.21  E-value: 7.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255   70 PARVRCSHLLVKHSQsrrpsswrqeKITRTKEEALELINGYIQKIKSGEeDFESLASQFS-D*SSAKARGDLGAFSRGQM 148
Cdd:pfam13616  13 PDSVKASHILISYSQ----------AVSRTEEEAKAKADSLLAALKNGA-DFAALAKTYSdDPASKNNGGDLGWFTKGQM 81

                          90       100
                  ....*....|....*....|....*....
gi 806394255  149 QKPFEDASFALRTGEMSGPVFTDSGIHII 177
Cdd:pfam13616  82 VKEFEDAVFSLKVGEISGVVKTQFGFHII 110
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 69-181 9.29e-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: 9.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  69 EPARVRCSHLLVKHSQSrrpsswrqEKITRTKEEALELIngyiQKIKSGEeDFESLASQFS-D*SSAKARGDLGAFSRGQ 147
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELL----AQLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 806394255 148 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 181
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 77-181 1.66e-25

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: 93.90  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255   77 HLLVKHsqsrrpsswrQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFS-D*SSAKARGDLGAFSRGQMQKPFEDA 155
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 806394255  156 SFALRTGEMSGPVFTDSGIHIILRTE 181
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
prsA PRK03095
peptidylprolyl isomerase PrsA;
72-181 6.44e-13

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 65.02  E-value: 6.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  72 RVRCSHLLVKHsqsrrpsswrQEKITRTKEEaleLINGyiqkiKSgeedFESLASQFSD*SSAKARG-DLGAFSRGQMQK 150
Cdd:PRK03095 132 EIKASHILVKD----------EATAKKVKEE---LGQG-----KS----FEELAKQYSEDTGSKEKGgDLGFFGAGKMVK 189

                         90       100       110
                 ....*....|....*....|....*....|.
gi 806394255 151 PFEDASFALRTGEMSGPVFTDSGIHIILRTE 181
Cdd:PRK03095 190 EFEDAAYKLKKDEVSEPVKSQFGYHIIKVTD 220
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 25-55 9.84e-13

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: 59.44  E-value: 9.84e-13
                          10        20        30
                  ....*....|....*....|....*....|.
gi 806394255   25 LPPGWEKAMSrSSGRVYYFNHITNASQWERP 55
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 72-181 1.38e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 64.22  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  72 RVRCSHLLVKhsqsrrpsswrQEKITRTKEEalelingyiqKIKSGEeDFESLASQFSD*SSAKARG-DLGAFSRGQMQK 150
Cdd:PRK02998 134 EMKVSHILVK-----------DEKTAKEVKE----------KVNNGE-DFAALAKQYSEDTGSKEQGgEISGFAPGQTVK 191

                         90       100       110
                 ....*....|....*....|....*....|.
gi 806394255 151 PFEDASFALRTGEMSGPVFTDSGIHIILRTE 181
Cdd:PRK02998 192 EFEEAAYKLDAGQVSEPVKTTYGYHIIKVTD 222
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 26-55 9.88e-12

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: 56.77  E-value: 9.88e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 806394255  26 PPGWEKAMSRSsGRVYYFNHITNASQWERP 55
Cdd:cd00201    1 PPGWEERWDPD-GRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 25-57 2.07e-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: 55.68  E-value: 2.07e-11
                           10        20        30
                   ....*....|....*....|....*....|...
gi 806394255    25 LPPGWEKAMSRSsGRVYYFNHITNASQWERPSG 57
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
prsA PRK00059
peptidylprolyl isomerase; Provisional
 70-177 3.24e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 57.80  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  70 PARVRCSHLLVKhsqsrrpsswrqekitrTKEEAlelingyiQKIKS---GEEDFESLASQFS-D*SSAKARGDLG--AF 143
Cdd:PRK00059 194 PNTMHLAHILVK-----------------TEDEA--------KKVKKrldKGEDFAKVAKEVSqDPGSKDKGGDLGdvPY 248

                         90       100       110
                 ....*....|....*....|....*....|....
gi 806394255 144 SRGQMQKPFEDASFALRTGEMSGPVFTDSGIHII 177
Cdd:PRK00059 249 SDSGYDKEFMDGAKALKEGEISAPVKTQFGYHII 282
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 100-177 5.40e-10

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 53.87  E-value: 5.40e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806394255 100 KEEALELinGYIQKIKSGEeDFESLASQFSD*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHII 177
Cdd:PRK15441  13 KEEKLAL--DLLEQIKNGA-DFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87
prsA PRK03002
peptidylprolyl isomerase PrsA;
121-181 2.13e-09

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 55.33  E-value: 2.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 806394255 121 FESLASQFS-D*SSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 181
Cdd:PRK03002 163 FEELAKQESqDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTD 224
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 73-177 1.41e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 50.12  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  73 VRCSHLLVKhsqsrrPSSWRQEKITRTKEEALElingyiQKIKSGEEDFESLASQFS-D*SSAKARGDLGAFSRGQMQKP 151
Cdd:PRK10770 267 VHARHILLK------PSPIMTDEQARAKLEQIA------ADIKSGKTTFAAAAKEFSqDPGSANQGGDLGWATPDIFDPA 334

                         90       100
                 ....*....|....*....|....*.
gi 806394255 152 FEDASFALRTGEMSGPVFTDSGIHII 177
Cdd:PRK10770 335 FRDALMRLNKGQISAPVHSSFGWHLI 360
prsA PRK04405
peptidylprolyl isomerase; Provisional
 79-177 8.23e-07

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 47.86  E-value: 8.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806394255  79 LVKHSQSRRPSSWR--QEKIT-----RTKEEALELIngyIQKIKSGEeDFESLASQFS-D*SSAKARGDLGAF--SRGQM 148
Cdd:PRK04405 126 LKKVTNSQLKKAWKsyQPKVTvqhilVSKKSTAETV---IKKLKDGK-DFAKLAKKYStDTATKNKGGKLSAFdsTDTTL 201

                         90       100       110
                 ....*....|....*....|....*....|
gi 806394255 149 QKPFEDASFALRTGEM-SGPVFTDSGIHII 177
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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