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Conserved domains on  [gi|940688317|ref|WP_055021968|]
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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 9.47e-41

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PRK15441:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 93  Bit Score: 129.37  E-value: 9.47e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317  1 MANTAHALHILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGKKGGDLGEFRRGQMVPQFDKVAFSGEILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 940688317 80 RFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
 
Name Accession Description Interval E-value
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-91 9.47e-41

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 129.37  E-value: 9.47e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317  1 MANTAHALHILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGKKGGDLGEFRRGQMVPQFDKVAFSGEILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 940688317 80 RFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 1-91 7.33e-35

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 115.83  E-value: 7.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   1 MANTAHALHILVKH---------KEQAEDIIKQLKKGAKFQTLAKKHSTCP-SGKKGGDLGEFRRGQMVPQFDKVAFS-- 68
Cdd:COG0760    5 SPEEVRASHILVKVppsedrakaEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFAlk 84

                         90       100
                 ....*....|....*....|....
gi 940688317  69 -GEILEPhlVKTRFGWHVIKVLYR 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 1.69e-28

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: 98.14  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   9 HILVKHKE-----------QAEDIIKQLKKGA-KFQTLAKKHST-CPSGKKGGDLGEFRRGQMVPQFDKVAFS---GEIL 72
Cdd:pfam00639  1 HILIKTPEaserdraeakaKAEEILEQLKSGEdSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFAlkpGEIS 80

                         90
                 ....*....|....*.
gi 940688317  73 EPhlVKTRFGWHVIKV 88
Cdd:pfam00639 81 GP--VETRFGFHIIKL 94
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 15-86 1.26e-12

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 61.02  E-value: 1.26e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940688317   15 KEQAEDIIKQLKKG-AKFQTLAKKHSTCPSGKKGGDLGEFRRGQMVPQFDKVAFS---GEILEPhlVKTRFGWHVI 86
Cdd:TIGR02933 142 RTRILAILRRLRGKpAAFAEQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQlaeGELSPP--IESEIGWHLL 215
 
Name Accession Description Interval E-value
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 1-91 9.47e-41

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 129.37  E-value: 9.47e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317  1 MANTAHALHILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGKKGGDLGEFRRGQMVPQFDKVAFSGEILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 940688317 80 RFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 1-91 7.33e-35

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 115.83  E-value: 7.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   1 MANTAHALHILVKH---------KEQAEDIIKQLKKGAKFQTLAKKHSTCP-SGKKGGDLGEFRRGQMVPQFDKVAFS-- 68
Cdd:COG0760    5 SPEEVRASHILVKVppsedrakaEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFAlk 84

                         90       100
                 ....*....|....*....|....
gi 940688317  69 -GEILEPhlVKTRFGWHVIKVLYR 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 1.69e-28

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: 98.14  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   9 HILVKHKE-----------QAEDIIKQLKKGA-KFQTLAKKHST-CPSGKKGGDLGEFRRGQMVPQFDKVAFS---GEIL 72
Cdd:pfam00639  1 HILIKTPEaserdraeakaKAEEILEQLKSGEdSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFAlkpGEIS 80

                         90
                 ....*....|....*.
gi 940688317  73 EPhlVKTRFGWHVIKV 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 8.07e-24

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: 87.04  E-value: 8.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317    1 MANTAHALHILVKH-----------KEQAEDIIKQLKKGAKFQTLAKKHSTCP-SGKKGGDLGEFRRGQMVPQFDKVAFS 68
Cdd:pfam13616  12 APDSVKASHILISYsqavsrteeeaKAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFS 91

                          90       100
                  ....*....|....*....|....*
gi 940688317   69 GEILEPH-LVKTRFGWHVIKVLYRT 92
Cdd:pfam13616  92 LKVGEISgVVKTQFGFHIIKVTDKK 116
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 4-87 2.54e-20

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 78.14  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   4 TAHALHILVKH------------------KEQAEDIIKQLK----KGAK-FQTLAKKHSTCPSGKKGGDLGEFRRGQMVP 60
Cdd:PTZ00356   5 TVRAAHLLIKHtgsrnpvsrrtgkpvtrsKEEAIKELAKWReqivSGEKtFEEIARQRSDCGSAAKGGDLGFFGRGQMQK 84

                         90       100
                 ....*....|....*....|....*...
gi 940688317  61 QFDKVAFSGEILE-PHLVKTRFGWHVIK 87
Cdd:PTZ00356  85 PFEDAAFALKVGEiSDIVHTDSGVHIIL 112
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-88 2.11e-18

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 77.44  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   2 ANTAHALHILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGK-KGGDLG--EFRRGQMVPQFDKVAFS---GEILEPh 75
Cdd:PRK00059 194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKdKGGDLGdvPYSDSGYDKEFMDGAKAlkeGEISAP- 272

                         90
                 ....*....|...
gi 940688317  76 lVKTRFGWHVIKV 88
Cdd:PRK00059 273 -VKTQFGYHIIKA 284
prsA PRK03095
peptidylprolyl isomerase PrsA;
7-88 2.65e-17

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 73.87  E-value: 2.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   7 ALHILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGK-KGGDLGEFRRGQMVPQFDKVAF---SGEILEPhlVKTRFG 82
Cdd:PRK03095 135 ASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKeKGGDLGFFGAGKMVKEFEDAAYklkKDEVSEP--VKSQFG 212


                 ....*.
gi 940688317  83 WHVIKV 88
Cdd:PRK03095 213 YHIIKV 218
prsA PRK03002
peptidylprolyl isomerase PrsA;
7-88 1.04e-16

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 72.28  E-value: 1.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   7 ALHILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGK-KGGDLGEFRRGQMVPQFDKVAFS---GEILEPhlVKTRFG 82
Cdd:PRK03002 139 ASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKeKGGDLGYFNSGRMAPEFETAAYKlkvGQISNP--VKSPNG 216


                 ....*.
gi 940688317  83 WHVIKV 88
Cdd:PRK03002 217 YHIIKL 222
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 9-88 3.89e-15

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 68.07  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   9 HILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGK-KGGDLGEFRRGQMVPQFDKVAF---SGEILEPhlVKTRFGWH 84
Cdd:PRK02998 139 HILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKeQGGEISGFAPGQTVKEFEEAAYkldAGQVSEP--VKTTYGYH 216


                 ....
gi 940688317  85 VIKV 88
Cdd:PRK02998 217 IIKV 220
prsA PRK04405
peptidylprolyl isomerase; Provisional
 9-89 2.16e-14

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 65.96  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   9 HILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGK-KGGDLGEF--RRGQMVPQFDKVAF---SGEIL-EPhlVKTRF 81
Cdd:PRK04405 149 HILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKnKGGKLSAFdsTDTTLDSTFKTAAFklkNGEYTtTP--VKTTY 226


                 ....*...
gi 940688317  82 GWHVIKVL 89
Cdd:PRK04405 227 GYEVIKMI 234
nifM_nitrog TIGR02933
nitrogen fixation protein NifM; Members of this protein family, found in a subset of ...
 15-86 1.26e-12

nitrogen fixation protein NifM; Members of this protein family, found in a subset of nitrogen-fixing bacteria, are the nitrogen fixation protein NifM. NifM, homologous to peptidyl-prolyl cis-trans isomerases, appears to be an accessory protein for NifH, the Fe protein, also called component II or dinitrogenase reductase, of nitrogenase. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131979 [Multi-domain]  Cd Length: 256  Bit Score: 61.02  E-value: 1.26e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 940688317   15 KEQAEDIIKQLKKG-AKFQTLAKKHSTCPSGKKGGDLGEFRRGQMVPQFDKVAFS---GEILEPhlVKTRFGWHVI 86
Cdd:TIGR02933 142 RTRILAILRRLRGKpAAFAEQAMRHSHCPTAMEGGLLGWVSRGLLYPQLDAALFQlaeGELSPP--IESEIGWHLL 215
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 6-89 3.12e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 48.97  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317   6 HALHILVK-----HKEQA----EDIIKQLKKG-AKFQTLAKKHSTCP-SGKKGGDLG---------EFRRGQMvpQFDKv 65
Cdd:PRK10770 268 HARHILLKpspimTDEQAraklEQIAADIKSGkTTFAAAAKEFSQDPgSANQGGDLGwatpdifdpAFRDALM--RLNK- 344

                         90       100
                 ....*....|....*....|....
gi 940688317  66 afsGEILEPhlVKTRFGWHVIKVL 89
Cdd:PRK10770 345 ---GQISAP--VHSSFGWHLIELL 363
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 10-62 4.56e-08

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 48.47  E-value: 4.56e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 940688317  10 ILVKHKEQAEDIIKQLKKGAKFQTLAKKHSTCP-SGKKGGDLGEFRRGQMVPQF 62
Cdd:PRK10788 276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPDEL 329
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
9-88 6.87e-07

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 43.58  E-value: 6.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317    9 HILVKHKEQAEDIIKQLKKGA--KFQTLAKKhstcpSGKKGGDLGEFRRGQMVPQ-FDKVAFS---GEILEPhlVKTRFG 82
Cdd:pfam13145  27 ILVFKDQVAADAALALLKAGAleDFAALAKG-----EGIKAATLDIVESAELLPEeLAKAAFAlkpGEVSGP--IKTGNG 99


                  ....*.
gi 940688317   83 WHVIKV 88
Cdd:pfam13145 100 YYVVRV 105
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 13-88 3.16e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 43.19  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940688317  13 KHKEQAEDIIKQLKKGAKFQTLAKKHSTCPSGKKGGDLGeFRRGQMVP----QFDKVAFSGEILEPhlVKTRFGWHVIKV 88
Cdd:PRK10770 176 EAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMG-WGRIQELPglfaQALSTAKKGDIVGP--IRSGVGFHILKV 252
 
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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