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Conserved domains on  [gi|768002764|ref|XP_011526370|]
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peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 isoform X1 [Homo sapiens]

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;
56-167 2.82e-52

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PTZ00356:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 115  Bit Score: 162.12  E-value: 2.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  56 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 134
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 768002764 135 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 167
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 25-42 1.56e-07

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: 45.19  E-value: 1.56e-07
                          10
                  ....*....|....*...
gi 768002764   25 GRVYYFNHITNASQWERP 42
Cdd:pfam00397  13 GRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 56-167 2.82e-52

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 162.12  E-value: 2.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  56 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 134
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 768002764 135 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 167
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 56-168 2.90e-28

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 2.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  56 EPARVRCSHLLVKHSQSrrpsswrqEKITRTKEEALELIngyiQKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQ 134
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELL----AQLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 768002764 135 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 64-168 1.59e-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: 98.91  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764   64 HLLVKHsqsrrpsswrQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMQKPFEDA 142
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 768002764  143 SFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 25-42 1.56e-07

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: 45.19  E-value: 1.56e-07
                          10
                  ....*....|....*...
gi 768002764   25 GRVYYFNHITNASQWERP 42
Cdd:pfam00397  13 GRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 25-42 7.93e-07

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: 43.29  E-value: 7.93e-07
                         10
                 ....*....|....*...
gi 768002764  25 GRVYYFNHITNASQWERP 42
Cdd:cd00201   12 GRVYYYNHNTKETQWEDP 29
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 25-44 6.31e-06

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: 41.05  E-value: 6.31e-06
                           10        20
                   ....*....|....*....|
gi 768002764    25 GRVYYFNHITNASQWERPSG 44
Cdd:smart00456  14 GRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 56-167 2.82e-52

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 162.12  E-value: 2.82e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  56 EPARVRCSHLLVKHSQSRRPSSWRQEK-ITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQ 134
Cdd:PTZ00356   2 EGDTVRAAHLLIKHTGSRNPVSRRTGKpVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 768002764 135 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRT 167
Cdd:PTZ00356  82 MQKPFEDAAFALKVGEISDIVHTDSGVHIILRL 114
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 56-168 2.90e-28

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.96  E-value: 2.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  56 EPARVRCSHLLVKHSQSrrpsswrqEKITRTKEEALELIngyiQKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQ 134
Cdd:COG0760    5 SPEEVRASHILVKVPPS--------EDRAKAEAKAEELL----AQLKAGA-DFAELAKEYSqDPGSAANGGDLGWFSRGQ 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 768002764 135 MQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:COG0760   72 LVPEFEEAAFALKPGEISGPVKTQFGYHIIKVED 105
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 64-168 1.59e-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: 98.91  E-value: 1.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764   64 HLLVKHsqsrrpsswrQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMQKPFEDA 142
Cdd:pfam00639   1 HILIKT----------PEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 768002764  143 SFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 57-164 8.18e-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: 97.44  E-value: 8.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764   57 PARVRCSHLLVKHSQsrrpsswrqeKITRTKEEALELINGYIQKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQM 135
Cdd:pfam13616  13 PDSVKASHILISYSQ----------AVSRTEEEAKAKADSLLAALKNGA-DFAALAKTYSdDPASKNNGGDLGWFTKGQM 81

                          90       100
                  ....*....|....*....|....*....
gi 768002764  136 QKPFEDASFALRTGEMSGPVFTDSGIHII 164
Cdd:pfam13616  82 VKEFEDAVFSLKVGEISGVVKTQFGFHII 110
prsA PRK03095
peptidylprolyl isomerase PrsA;
59-168 6.13e-13

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 64.63  E-value: 6.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  59 RVRCSHLLVKHsqsrrpsswrQEKITRTKEEaleLINGyiqkiKSgeedFESLASQFS-DCSSAKARGDLGAFSRGQMQK 137
Cdd:PRK03095 132 EIKASHILVKD----------EATAKKVKEE---LGQG-----KS----FEELAKQYSeDTGSKEKGGDLGFFGAGKMVK 189

                         90       100       110
                 ....*....|....*....|....*....|.
gi 768002764 138 PFEDASFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:PRK03095 190 EFEDAAYKLKKDEVSEPVKSQFGYHIIKVTD 220
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 59-168 1.33e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 63.84  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  59 RVRCSHLLVKhsqsrrpsswrQEKITRTKEEalelingyiqKIKSGEeDFESLASQFS-DCSSAKARGDLGAFSRGQMQK 137
Cdd:PRK02998 134 EMKVSHILVK-----------DEKTAKEVKE----------KVNNGE-DFAALAKQYSeDTGSKEQGGEISGFAPGQTVK 191

                         90       100       110
                 ....*....|....*....|....*....|.
gi 768002764 138 PFEDASFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:PRK02998 192 EFEEAAYKLDAGQVSEPVKTTYGYHIIKVTD 222
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 87-164 6.46e-12

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 58.50  E-value: 6.46e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768002764  87 KEEALELinGYIQKIKSGEeDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHII 164
Cdd:PRK15441  13 KEEKLAL--DLLEQIKNGA-DFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87
prsA PRK00059
peptidylprolyl isomerase; Provisional
 57-164 4.02e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 57.03  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  57 PARVRCSHLLVKhsqsrrpsswrqekitrTKEEAlelingyiQKIKS---GEEDFESLASQFS-DCSSAKARGDLG--AF 130
Cdd:PRK00059 194 PNTMHLAHILVK-----------------TEDEA--------KKVKKrldKGEDFAKVAKEVSqDPGSKDKGGDLGdvPY 248

                         90       100       110
                 ....*....|....*....|....*....|....
gi 768002764 131 SRGQMQKPFEDASFALRTGEMSGPVFTDSGIHII 164
Cdd:PRK00059 249 SDSGYDKEFMDGAKALKEGEISAPVKTQFGYHII 282
prsA PRK03002
peptidylprolyl isomerase PrsA;
108-168 2.24e-09

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 54.94  E-value: 2.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768002764 108 FESLASQFS-DCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE 168
Cdd:PRK03002 163 FEELAKQESqDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTD 224
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 25-42 1.56e-07

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: 45.19  E-value: 1.56e-07
                          10
                  ....*....|....*...
gi 768002764   25 GRVYYFNHITNASQWERP 42
Cdd:pfam00397  13 GRVYYYNHETGETQWEKP 30
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 60-164 2.06e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 49.35  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  60 VRCSHLLVKhsqsrrPSSWRQEKITRTKEEALElingyiQKIKSGEEDFESLASQFS-DCSSAKARGDLGAFSRGQMQKP 138
Cdd:PRK10770 267 VHARHILLK------PSPIMTDEQARAKLEQIA------ADIKSGKTTFAAAAKEFSqDPGSANQGGDLGWATPDIFDPA 334

                         90       100
                 ....*....|....*....|....*.
gi 768002764 139 FEDASFALRTGEMSGPVFTDSGIHII 164
Cdd:PRK10770 335 FRDALMRLNKGQISAPVHSSFGWHLI 360
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 25-42 7.93e-07

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: 43.29  E-value: 7.93e-07
                         10
                 ....*....|....*...
gi 768002764  25 GRVYYFNHITNASQWERP 42
Cdd:cd00201   12 GRVYYYNHNTKETQWEDP 29
prsA PRK04405
peptidylprolyl isomerase; Provisional
 66-164 8.63e-07

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 47.47  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768002764  66 LVKHSQSRRPSSWR--QEKIT-----RTKEEALELIngyIQKIKSGEeDFESLASQFS-DCSSAKARGDLGAF--SRGQM 135
Cdd:PRK04405 126 LKKVTNSQLKKAWKsyQPKVTvqhilVSKKSTAETV---IKKLKDGK-DFAKLAKKYStDTATKNKGGKLSAFdsTDTTL 201

                         90       100       110
                 ....*....|....*....|....*....|
gi 768002764 136 QKPFEDASFALRTGEM-SGPVFTDSGIHII 164
Cdd:PRK04405 202 DSTFKTAAFKLKNGEYtTTPVKTTYGYEVI 231
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 25-44 6.31e-06

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: 41.05  E-value: 6.31e-06
                           10        20
                   ....*....|....*....|
gi 768002764    25 GRVYYFNHITNASQWERPSG 44
Cdd:smart00456  14 GRPYYYNHETKETQWEKPRE 33
 
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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