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Conserved domains on  [gi|490726262|ref|WP_004588770|]
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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;
1-91 1.98e-38

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PRK15441:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 93  Bit Score: 123.21  E-value: 1.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262  1 MASTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGEFRRGQMVPQFDKIAFNGAILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 490726262 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 1.98e-38

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 123.21  E-value: 1.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262  1 MASTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGEFRRGQMVPQFDKIAFNGAILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 490726262 80 KFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 1-91 7.20e-32

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 108.12  E-value: 7.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   1 MASTAHALHILVKH---------KEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQFDKIAFN-- 68
Cdd:COG0760    5 SPEEVRASHILVKVppsedrakaEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFAlk 84

                         90       100
                 ....*....|....*....|....
gi 490726262  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 1.07e-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: 91.21  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   9 HILVKHKE-----------IAEDIIKQLGKGA-KFQTLAKKYSS-CPSGKKGGDLGEFRRGQMVPQFDKIAFN---GAIL 72
Cdd:pfam00639  1 HILIKTPEaserdraeakaKAEEILEQLKSGEdSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFAlkpGEIS 80

                         90
                 ....*....|....*.
gi 490726262  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 1.98e-38

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 123.21  E-value: 1.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262  1 MASTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGEFRRGQMVPQFDKIAFNGAILEPH-LVKT 79
Cdd:PRK15441  1 MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTgPLHT 80

                        90
                ....*....|..
gi 490726262 80 KFGWHVIKVLYR 91
Cdd:PRK15441 81 QFGYHIIKVLYR 92
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 1-91 7.20e-32

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 108.12  E-value: 7.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   1 MASTAHALHILVKH---------KEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQFDKIAFN-- 68
Cdd:COG0760    5 SPEEVRASHILVKVppsedrakaEAKAEELLAQLKAGADFAELAKEYSQDPgSAANGGDLGWFSRGQLVPEFEEAAFAlk 84

                         90       100
                 ....*....|....*....|....
gi 490726262  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 1.07e-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: 91.21  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   9 HILVKHKE-----------IAEDIIKQLGKGA-KFQTLAKKYSS-CPSGKKGGDLGEFRRGQMVPQFDKIAFN---GAIL 72
Cdd:pfam00639  1 HILIKTPEaserdraeakaKAEEILEQLKSGEdSFAELARKYSDdCPSAANGGDLGWFTRGQLPPEFEKAAFAlkpGEIS 80

                         90
                 ....*....|....*.
gi 490726262  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 ...
 5-92 2.02e-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: 83.57  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262    5 AHALHILVKH-----------KEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQFDKIAFNGAIL 72
Cdd:pfam13616  16 VKASHILISYsqavsrteeeaKAKADSLLAALKNGADFAALAKTYSDDPaSKNNGGDLGWFTKGQMVKEFEDAVFSLKVG 95

                          90       100
                  ....*....|....*....|.
gi 490726262   73 EPH-LVKTKFGWHVIKVLYRT 92
Cdd:pfam13616  96 EISgVVKTQFGFHIIKVTDKK 116
prsA PRK03095
peptidylprolyl isomerase PrsA;
7-88 7.57e-19

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 78.11  E-value: 7.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   7 ALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEFRRGQMVPQFDKIAF---NGAILEPhlVKTKFG 82
Cdd:PRK03095 135 ASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKeKGGDLGFFGAGKMVKEFEDAAYklkKDEVSEP--VKSQFG 212


                 ....*.
gi 490726262  83 WHVIKV 88
Cdd:PRK03095 213 YHIIKV 218
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 1-87 1.25e-18

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 73.91  E-value: 1.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   1 MASTAHALHILVKH------------------KEIAEDIIK----QLGKGAK-FQTLAKKYSSCPSGKKGGDLGEFRRGQ 57
Cdd:PTZ00356   2 EGDTVRAAHLLIKHtgsrnpvsrrtgkpvtrsKEEAIKELAkwreQIVSGEKtFEEIARQRSDCGSAAKGGDLGFFGRGQ 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490726262  58 MVPQFDKIAFNgaiLEP----HLVKTKFGWHVIK 87
Cdd:PTZ00356  82 MQKPFEDAAFA---LKVgeisDIVHTDSGVHIIL 112
prsA PRK00059
peptidylprolyl isomerase; Provisional
 2-88 2.92e-17

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 74.36  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   2 ASTAHALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLG--EFRRGQMVPQFDKIAFN---GAILEPh 75
Cdd:PRK00059 194 PNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSKdKGGDLGdvPYSDSGYDKEFMDGAKAlkeGEISAP- 272

                         90
                 ....*....|...
gi 490726262  76 lVKTKFGWHVIKV 88
Cdd:PRK00059 273 -VKTQFGYHIIKA 284
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 9-88 4.00e-16

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 70.77  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   9 HILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEFRRGQMVPQFDKIAFN---GAILEPhlVKTKFGWH 84
Cdd:PRK02998 139 HILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKeQGGEISGFAPGQTVKEFEEAAYKldaGQVSEP--VKTTYGYH 216


                 ....
gi 490726262  85 VIKV 88
Cdd:PRK02998 217 IIKV 220
prsA PRK03002
peptidylprolyl isomerase PrsA;
7-88 2.83e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 68.42  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   7 ALHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEFRRGQMVPQFDKIAFN---GAILEPhlVKTKFG 82
Cdd:PRK03002 139 ASHILVSDENEAKEIKKKLDAGASFEELAKQESQDLLSKeKGGDLGYFNSGRMAPEFETAAYKlkvGQISNP--VKSPNG 216


                 ....*.
gi 490726262  83 WHVIKV 88
Cdd:PRK03002 217 YHIIKL 222
prsA PRK04405
peptidylprolyl isomerase; Provisional
 9-89 5.52e-13

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 62.11  E-value: 5.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   9 HILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGK-KGGDLGEF--RRGQMVPQFDKIAF---NGAIL-EPhlVKTKF 81
Cdd:PRK04405 149 HILVSKKSTAETVIKKLKDGKDFAKLAKKYSTDTATKnKGGKLSAFdsTDTTLDSTFKTAAFklkNGEYTtTP--VKTTY 226


                 ....*...
gi 490726262  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 490726262   6 HALHILVKH-------------KEIAEDIikQLGKgAKFQTLAKKYSSCP-SGKKGGDLG---------EFRRGQMvpQF 62
Cdd:PRK10770 268 HARHILLKPspimtdeqaraklEQIAADI--KSGK-TTFAAAAKEFSQDPgSANQGGDLGwatpdifdpAFRDALM--RL 342

                         90       100
                 ....*....|....*....|....*..
gi 490726262  63 DKiafnGAILEPhlVKTKFGWHVIKVL 89
Cdd:PRK10770 343 NK----GQISAP--VHSSFGWHLIELL 363
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
8-88 8.07e-06

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 40.89  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262    8 LHILVKHKEIAEDIIKQLGKGAKFQTLAKKYSScpSGKKGGDLGEFRRGQMVPQ-FDKIAFN---GAILEPhlVKTKFGW 83
Cdd:pfam13145  25 LEILVFKDQVAADAALALLKAGALEDFAALAKG--EGIKAATLDIVESAELLPEeLAKAAFAlkpGEVSGP--IKTGNGY 100


                  ....*
gi 490726262   84 HVIKV 88
Cdd:pfam13145 101 YVVRV 105
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 9-88 8.98e-06

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 42.04  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726262   9 HILV------------KHKEIAEDIIKQLGKGAKFQTLAKKYSSCPSGKKGGDLGeFRRGQMVP----QFDKIAFNGAIL 72
Cdd:PRK10770 160 HILIplpenptqdqvdEAESQARSIVDQARNGADFGKLAIAYSADQQALKGGQMG-WGRIQELPglfaQALSTAKKGDIV 238

                         90
                 ....*....|....*.
gi 490726262  73 EPhlVKTKFGWHVIKV 88
Cdd:PRK10770 239 GP--IRSGVGFHILKV 252
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 10-62 5.42e-05

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 39.99  E-value: 5.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490726262  10 ILVKHKEIAEDIIKQLGKGAKFQTLAKKYSSCP-SGKKGGDLGEFRRGQMVPQF 62
Cdd:PRK10788 276 IQTKTEAEAKAVLDELKKGADFATLAKEKSTDIiSARNGGDLGWLEPATTPDEL 329
 
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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