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Conserved domains on  [gi|498068348|ref|WP_010382504|]
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MULTISPECIES: peptidylprolyl isomerase [Pseudoalteromonas]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 1001668)

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:0003755
PubMed:  12871165|7925971

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;
4-92 4.90e-35

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PRK15441:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 93  Bit Score: 114.74  E-value: 4.90e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348  4 ACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCPSKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVHGPVKTKFGY 83
Cdd:PRK15441  5 AAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGY 84


                ....*....
gi 498068348 84 HLIKTVYRS 92
Cdd:PRK15441 85 HIIKVLYRN 93
 
Name Accession Description Interval E-value
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 4-92 4.90e-35

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 114.74  E-value: 4.90e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348  4 ACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCPSKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVHGPVKTKFGY 83
Cdd:PRK15441  5 AAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGY 84


                ....*....
gi 498068348 84 HLIKTVYRS 92
Cdd:PRK15441 85 HIIKVLYRN 93
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 2-87 2.31e-33

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 111.98  E-value: 2.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILV---------KTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLGEFNKGDMVKAFDDVVFKKPLY 71
Cdd:COG0760    7 EEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKPG 86

                         90
                 ....*....|....*.
gi 498068348  72 EVHGPVKTKFGYHLIK 87
Cdd:COG0760   87 EISGPVKTQFGYHIIK 102
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 8-87 1.06e-22

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: 83.50  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   8 HILVKT-----------EKECLAIKAKLAKGGD-FNKLAKQHSL-CPSKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVH 74
Cdd:pfam00639  1 HILIKTpeaserdraeaKAKAEEILEQLKSGEDsFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                         90
                 ....*....|...
gi 498068348  75 GPVKTKFGYHLIK 87
Cdd:pfam00639 81 GPVETRFGFHIIK 93
 
Name Accession Description Interval E-value
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 4-92 4.90e-35

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 114.74  E-value: 4.90e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348  4 ACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCPSKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVHGPVKTKFGY 83
Cdd:PRK15441  5 AAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGY 84


                ....*....
gi 498068348 84 HLIKTVYRS 92
Cdd:PRK15441 85 HIIKVLYRN 93
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 2-87 2.31e-33

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 111.98  E-value: 2.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILV---------KTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLGEFNKGDMVKAFDDVVFKKPLY 71
Cdd:COG0760    7 EEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFALKPG 86

                         90
                 ....*....|....*.
gi 498068348  72 EVHGPVKTKFGYHLIK 87
Cdd:COG0760   87 EISGPVKTQFGYHIIK 102
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 8-87 1.06e-22

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: 83.50  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   8 HILVKT-----------EKECLAIKAKLAKGGD-FNKLAKQHSL-CPSKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVH 74
Cdd:pfam00639  1 HILIKTpeaserdraeaKAKAEEILEQLKSGEDsFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                         90
                 ....*....|...
gi 498068348  75 GPVKTKFGYHLIK 87
Cdd:pfam00639 81 GPVETRFGFHIIK 93
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 6-88 1.16e-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: 1.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348    6 AYHILV-------KTEKECLA----IKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEV 73
Cdd:pfam13616  18 ASHILIsysqavsRTEEEAKAkadsLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSLKVGEI 97

                          90
                  ....*....|....*
gi 498068348   74 HGPVKTKFGYHLIKT 88
Cdd:pfam13616  98 SGVVKTQFGFHIIKV 112
prsA PRK03095
peptidylprolyl isomerase PrsA;
2-87 5.23e-21

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 83.89  E-value: 5.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVHGPVKTK 80
Cdd:PRK03095 131 PEIKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTgSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQ 210


                 ....*..
gi 498068348  81 FGYHLIK 87
Cdd:PRK03095 211 FGYHIIK 217
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 2-87 2.85e-20

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 81.94  E-value: 2.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVHGPVKTK 80
Cdd:PRK02998 133 PEMKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTgSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTT 212


                 ....*..
gi 498068348  81 FGYHLIK 87
Cdd:PRK02998 213 YGYHIIK 219
prsA PRK03002
peptidylprolyl isomerase PrsA;
2-87 1.29e-17

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 74.59  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLGEFNKGDMVKAFDDVVFKKPLYEVHGPVKTK 80
Cdd:PRK03002 135 PEIKASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLlSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSP 214


                 ....*..
gi 498068348  81 FGYHLIK 87
Cdd:PRK03002 215 NGYHIIK 221
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-87 3.13e-17

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 73.98  E-value: 3.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLG--EFNKGDMVKAFDDVVFKKPLYEVHGPVK 78
Cdd:PRK00059 195 NTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPgSKDKGGDLGdvPYSDSGYDKEFMDGAKALKEGEISAPVK 274


                 ....*....
gi 498068348  79 TKFGYHLIK 87
Cdd:PRK00059 275 TQFGYHIIK 283
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 1-87 8.86e-17

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 68.90  E-value: 8.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   1 MPKACAYHILVK----------------------TEKECLAIKAKLAKG-GDFNKLAKQHSLCPSKKRGGDLGEFNKGDM 57
Cdd:PTZ00356   3 GDTVRAAHLLIKhtgsrnpvsrrtgkpvtrskeeAIKELAKWREQIVSGeKTFEEIARQRSDCGSAAKGGDLGFFGRGQM 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 498068348  58 VKAFDDVVFKKPLYEVHGPVKTKFGYHLIK 87
Cdd:PTZ00356  83 QKPFEDAAFALKVGEISDIVHTDSGVHIIL 112
prsA PRK04405
peptidylprolyl isomerase; Provisional
 2-87 4.70e-10

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 54.02  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   2 PKACAYHILVKTEKECLAIKAKLAKGGDFNKLAKQHSL-CPSKKRGGDLGEFNKGD--MVKAFDDVVFKKPLYEV-HGPV 77
Cdd:PRK04405 143 PKVTVQHILVSKKSTAETVIKKLKDGKDFAKLAKKYSTdTATKNKGGKLSAFDSTDttLDSTFKTAAFKLKNGEYtTTPV 222

                         90
                 ....*....|
gi 498068348  78 KTKFGYHLIK 87
Cdd:PRK04405 223 KTTYGYEVIK 232
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 9-50 4.52e-08

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 48.47  E-value: 4.52e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 498068348   9 ILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCP-SKKRGGDLG 50
Cdd:PRK10788 276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLG 318
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 6-87 6.82e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 45.12  E-value: 6.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348   6 AYHILVKT---------EKECLAIKAKLAKGG-DFNKLAKQHSLCP-SKKRGGDLGeFNKGDMVK-AFDDVVFKKPLYEV 73
Cdd:PRK10770 269 ARHILLKPspimtdeqaRAKLEQIAADIKSGKtTFAAAAKEFSQDPgSANQGGDLG-WATPDIFDpAFRDALMRLNKGQI 347

                         90
                 ....*....|....
gi 498068348  74 HGPVKTKFGYHLIK 87
Cdd:PRK10770 348 SAPVHSSFGWHLIE 361
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
8-87 5.58e-04

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 36.27  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498068348    8 HILVKTEKECLAIKAKLAKGGDFNKLAKQHSLCPSKKRGGDLGEfNKGDMVKAFDDVVFKKPLYEVHGPVKTKFGYHLIK 87
Cdd:pfam13145  26 EILVFKDQVAADAALALLKAGALEDFAALAKGEGIKAATLDIVE-SAELLPEELAKAAFALKPGEVSGPIKTGNGYYVVR 104
 
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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