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Conserved domains on  [gi|495739733|ref|WP_008464312|]
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MULTISPECIES: peptidylprolyl isomerase PpiC [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;
1-91 2.60e-39

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PRK15441:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 93  Bit Score: 125.52  E-value: 2.60e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733  1 MANTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGEFRRGQMVPQFDKVAFSGAILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 495739733 80 KFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
 
Name Accession Description Interval E-value
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-91 2.60e-39

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 125.52  E-value: 2.60e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733  1 MANTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGEFRRGQMVPQFDKVAFSGAILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 495739733 80 KFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 1-91 2.79e-32

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 109.28  E-value: 2.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   1 MANTAHALHILVKH---------KEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQFDKVAFS-- 68
Cdd:COG0760    5 SPEEVRASHILVKVppsedrakaEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFAlk 84

                         90       100
                 ....*....|....*....|....
gi 495739733  69 -GAILEPhlVKTKFGWHVIKVLYR 91
Cdd:COG0760   85 pGEISGP--VKTQFGYHIIKVEDR 106
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 9-88 2.75e-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: 92.75  E-value: 2.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   9 HILVKHKE-----------IAEDIIKQLGKGA-KFQTLAKKYSS-CPSGKKGGDLGEFRRGQMVPQFDKVAFS---GAIL 72
Cdd:pfam00639  1 HILIKTPEaserdraeakaKAEEILEQLKSGEdSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFAlkpGEIS 80

                         90
                 ....*....|....*.
gi 495739733  73 EPhlVKTKFGWHVIKV 88
Cdd:pfam00639 81 GP--VETRFGFHIIKL 94
 
Name Accession Description Interval E-value
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-91 2.60e-39

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 125.52  E-value: 2.60e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733  1 MANTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGEFRRGQMVPQFDKVAFSGAILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 495739733 80 KFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 1-91 2.79e-32

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 109.28  E-value: 2.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   1 MANTAHALHILVKH---------KEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQFDKVAFS-- 68
Cdd:COG0760    5 SPEEVRASHILVKVppsedrakaEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFAlk 84

                         90       100
                 ....*....|....*....|....
gi 495739733  69 -GAILEPhlVKTKFGWHVIKVLYR 91
Cdd:COG0760   85 pGEISGP--VKTQFGYHIIKVEDR 106
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 9-88 2.75e-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: 92.75  E-value: 2.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   9 HILVKHKE-----------IAEDIIKQLGKGA-KFQTLAKKYSS-CPSGKKGGDLGEFRRGQMVPQFDKVAFS---GAIL 72
Cdd:pfam00639  1 HILIKTPEaserdraeakaKAEEILEQLKSGEdSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFAlkpGEIS 80

                         90
                 ....*....|....*.
gi 495739733  73 EPhlVKTKFGWHVIKV 88
Cdd:pfam00639 81 GP--VETRFGFHIIKL 94
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 1-92 1.44e-23

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: 86.27  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733    1 MANTAHALHILVKH-----------KEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQFDKVAFS 68
Cdd:pfam13616  12 APDSVKASHILISYsqavsrteeeaKAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFS 91

                          90       100
                  ....*....|....*....|....*
gi 495739733   69 GAILEPH-LVKTKFGWHVIKVLYRT 92
Cdd:pfam13616  92 LKVGEISgVVKTQFGFHIIKVTDKK 116
prsA PRK03095
peptidylprolyl isomerase PrsA;
7-88 5.84e-19

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 78.50  E-value: 5.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   7 ALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEFRRGQMVPQFDKVAF---SGAILEPhlVKTKFG 82
Cdd:PRK03095 135 ASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKeKGGDLGFFGAGKMVKEFEDAAYklkKDEVSEP--VKSQFG 212


                 ....*.
gi 495739733  83 WHVIKV 88
Cdd:PRK03095 213 YHIIKV 218
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 4-87 7.42e-19

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 74.29  E-value: 7.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   4 TAHALHILVKH------------------KEIAEDIIK----QLGKGAK-FQTLAKKYSSCPSGKKGGDLGEFRRGQMVP 60
Cdd:PTZ00356   5 TVRAAHLLIKHtgsrnpvsrrtgkpvtrsKEEAIKELAkwreQIVSGEKtFEEIARQRSDCGSAAKGGDLGFFGRGQMQK 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495739733  61 QFDKVAFSgaiLEP----HLVKTKFGWHVIK 87
Cdd:PTZ00356  85 PFEDAAFA---LKVgeisDIVHTDSGVHIIL 112
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-88 8.14e-18

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 75.90  E-value: 8.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   2 ANTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLG--EFRRGQMVPQFDKVAFS---GAILEPh 75
Cdd:PRK00059 194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKdKGGDLGdvPYSDSGYDKEFMDGAKAlkeGEISAP- 272

                         90
                 ....*....|...
gi 495739733  76 lVKTKFGWHVIKV 88
Cdd:PRK00059 273 -VKTQFGYHIIKA 284
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 9-88 2.47e-16

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 71.16  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   9 HILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEFRRGQMVPQFDKVAF---SGAILEPhlVKTKFGWH 84
Cdd:PRK02998 139 HILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKeQGGEISGFAPGQTVKEFEEAAYkldAGQVSEP--VKTTYGYH 216


                 ....
gi 495739733  85 VIKV 88
Cdd:PRK02998 217 IIKV 220
prsA PRK03002
peptidylprolyl isomerase PrsA;
7-88 1.61e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 69.19  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   7 ALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEFRRGQMVPQFDKVAFS---GAILEPhlVKTKFG 82
Cdd:PRK03002 139 ASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKeKGGDLGYFNSGRMAPEFETAAYKlkvGQISNP--VKSPNG 216


                 ....*.
gi 495739733  83 WHVIKV 88
Cdd:PRK03002 217 YHIIKL 222
prsA PRK04405
peptidylprolyl isomerase; Provisional
 9-89 1.86e-12

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 60.57  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   9 HILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEF--RRGQMVPQFDKVAF---SGAIL-EPhlVKTKF 81
Cdd:PRK04405 149 HILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKnKGGKLSAFdsTDTTLDSTFKTAAFklkNGEYTtTP--VKTTY 226


                 ....*...
gi 495739733  82 GWHVIKVL 89
Cdd:PRK04405 227 GYEVIKMI 234
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 6-89 3.41e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 45.89  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   6 HALHILVKH-------------KEIAEDIikQLGKgAKFQTLAKKYSSCP-SGKKGGDLG---------EFRRGQMvpQF 62
Cdd:PRK10770 268 HARHILLKPspimtdeqaraklEQIAADI--KSGK-TTFAAAAKEFSQDPgSANQGGDLGwatpdifdpAFRDALM--RL 342

                         90       100
                 ....*....|....*....|....*..
gi 495739733  63 DKvafsGAILEPhlVKTKFGWHVIKVL 89
Cdd:PRK10770 343 NK----GQISAP--VHSSFGWHLIELL 363
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 9-88 7.61e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 42.42  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733   9 HILV------------KHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGeFRRGQMVP----QFDKVAFSGAIL 72
Cdd:PRK10770 160 HILIplpenptqdqvdEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMG-WGRIQELPglfaQALSTAKKGDIV 238

                         90
                 ....*....|....*.
gi 495739733  73 EPhlVKTKFGWHVIKV 88
Cdd:PRK10770 239 GP--IRSGVGFHILKV 252
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
8-88 1.65e-05

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 40.12  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495739733    8 LHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSScpSGKKGGDLGEFRRGQMVPQ-FDKVAFS---GAILEPhlVKTKFGW 83
Cdd:pfam13145  25 LEILVFKDQVAADAALALLKAGALEDFAALAKG--EGIKAATLDIVESAELLPEeLAKAAFAlkpGEVSGP--IKTGNGY 100


                  ....*
gi 495739733   84 HVIKV 88
Cdd:pfam13145 101 YVVRV 105
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 10-71 3.85e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 40.38  E-value: 3.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495739733  10 ILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQF------DKVAFSGAI 71
Cdd:PRK10788 276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPDELknaglkEKGQLSGVI 344
 
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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