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Conserved domains on  [gi|15982815|gb|AAL09755|]
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At2g18040/T27K22.9 [Arabidopsis thaliana]

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;
5-119 2.13e-52

PPIC-type PPIASE domain;


The actual alignment was detected with superfamily member PTZ00356:

Pssm-ID: 452928 [Multi-domain]  Cd Length: 115  Bit Score: 160.58  E-value: 2.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    5 DQVKASHILIKHQGSRRKASWKdpEGKIIlTTTREAAVEQLKSIREDIVSGKANFEEVATRVSDCSSAKRGGDLGSFGRG 84
Cdd:PTZ00356   4 DTVRAAHLLIKHTGSRNPVSRR--TGKPV-TRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15982815   85 QMQKPFEEATYALKVGDISDIVDTDSGVHIIKRTA 119
Cdd:PTZ00356  81 QMQKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 5-119 2.13e-52

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 160.58  E-value: 2.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    5 DQVKASHILIKHQGSRRKASWKdpEGKIIlTTTREAAVEQLKSIREDIVSGKANFEEVATRVSDCSSAKRGGDLGSFGRG 84
Cdd:PTZ00356   4 DTVRAAHLLIKHTGSRNPVSRR--TGKPV-TRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15982815   85 QMQKPFEEATYALKVGDISDIVDTDSGVHIIKRTA 119
Cdd:PTZ00356  81 QMQKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 11-119 8.98e-30

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: 102.76  E-value: 8.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    11 HILIKHQGSRRKaswkdpegkiilttTREAAVEQLKSIREDIVSGKANFEEVATRVS-DCSSAKRGGDLGSFGRGQMQKP 89
Cdd:pfam00639   1 HILIKTPEASER--------------DRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPE 66

                          90       100       110
                  ....*....|....*....|....*....|
gi 15982815    90 FEEATYALKVGDISDIVDTDSGVHIIKRTA 119
Cdd:pfam00639  67 FEKAAFALKPGEISGPVETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 2-116 8.84e-29

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.58  E-value: 8.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815   2 ASRDQVKASHILIKHQGSRrkaswkdpegkiilttTREAAVEQLKSIREDIVSGkANFEEVATRVS-DCSSAKRGGDLGS 80
Cdd:COG0760   4 DSPEEVRASHILVKVPPSE----------------DRAKAEAKAEELLAQLKAG-ADFAELAKEYSqDPGSAANGGDLGW 66

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15982815  81 FGRGQMQKPFEEATYALKVGDISDIVDTDSGVHIIK 116
Cdd:COG0760  67 FSRGQLVPEFEEAAFALKPGEISGPVKTQFGYHIIK 102
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 5-119 2.13e-52

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 160.58  E-value: 2.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    5 DQVKASHILIKHQGSRRKASWKdpEGKIIlTTTREAAVEQLKSIREDIVSGKANFEEVATRVSDCSSAKRGGDLGSFGRG 84
Cdd:PTZ00356   4 DTVRAAHLLIKHTGSRNPVSRR--TGKPV-TRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRG 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15982815   85 QMQKPFEEATYALKVGDISDIVDTDSGVHIIKRTA 119
Cdd:PTZ00356  81 QMQKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 11-119 8.98e-30

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: 102.76  E-value: 8.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    11 HILIKHQGSRRKaswkdpegkiilttTREAAVEQLKSIREDIVSGKANFEEVATRVS-DCSSAKRGGDLGSFGRGQMQKP 89
Cdd:pfam00639   1 HILIKTPEASER--------------DRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPE 66

                          90       100       110
                  ....*....|....*....|....*....|
gi 15982815    90 FEEATYALKVGDISDIVDTDSGVHIIKRTA 119
Cdd:pfam00639  67 FEKAAFALKPGEISGPVETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 2-116 8.84e-29

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 101.58  E-value: 8.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815   2 ASRDQVKASHILIKHQGSRrkaswkdpegkiilttTREAAVEQLKSIREDIVSGkANFEEVATRVS-DCSSAKRGGDLGS 80
Cdd:COG0760   4 DSPEEVRASHILVKVPPSE----------------DRAKAEAKAEELLAQLKAG-ADFAELAKEYSqDPGSAANGGDLGW 66

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15982815  81 FGRGQMQKPFEEATYALKVGDISDIVDTDSGVHIIK 116
Cdd:COG0760  67 FSRGQLVPEFEEAAFALKPGEISGPVKTQFGYHIIK 102
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 5-116 1.18e-21

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: 82.41  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815     5 DQVKASHILIkhqgsrrkASWKDPegkiilTTTREAAVEQLKSIREDIVSGkANFEEVATRVS-DCSSAKRGGDLGSFGR 83
Cdd:pfam13616  14 DSVKASHILI--------SYSQAV------SRTEEEAKAKADSLLAALKNG-ADFAALAKTYSdDPASKNNGGDLGWFTK 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15982815    84 GQMQKPFEEATYALKVGDISDIVDTDSGVHIIK 116
Cdd:pfam13616  79 GQMVKEFEDAVFSLKVGEISGVVKTQFGFHIIK 111
prsA PRK03095
peptidylprolyl isomerase PrsA;
4-118 8.25e-15

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 68.10  E-value: 8.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    4 RDQVKASHILIKHQgsrrkaswkdpegkiiltttreaavEQLKSIREDIVSGKAnFEEVATRVS-DCSSAKRGGDLGSFG 82
Cdd:PRK03095 130 KPEIKASHILVKDE-------------------------ATAKKVKEELGQGKS-FEELAKQYSeDTGSKEKGGDLGFFG 183

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15982815   83 RGQMQKPFEEATYALKVGDISDIVDTDSGVHIIKRT 118
Cdd:PRK03095 184 AGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVT 219
prsA PRK03002
peptidylprolyl isomerase PrsA;
6-118 1.79e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 67.27  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    6 QVKASHILIKHQgsrrkaswkdpegkiiltttreaavEQLKSIREDIVSGkANFEEVATRVS-DCSSAKRGGDLGSFGRG 84
Cdd:PRK03002 136 EIKASHILVSDE-------------------------NEAKEIKKKLDAG-ASFEELAKQESqDLLSKEKGGDLGYFNSG 189

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15982815   85 QMQKPFEEATYALKVGDISDIVDTDSGVHIIKRT 118
Cdd:PRK03002 190 RMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLT 223
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 46-118 7.35e-12

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 59.98  E-value: 7.35e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15982815   46 KSIREDIVSGKaNFEEVATRVS-DCSSAKRGGDLGSFGRGQMQKPFEEATYALKVGDISDIVDTDSGVHIIKRT 118
Cdd:PRK02998 149 KEVKEKVNNGE-DFAALAKQYSeDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVT 221
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 33-116 6.47e-10

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 51.95  E-value: 6.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815   33 ILTTTREAAVEQLKSIREDivsgkANFEEVATRVSDCSSAKRGGDLGSFGRGQMQKPFEEATYALKVGDISDIVDTDSGV 112
Cdd:PRK15441  10 ILVKEEKLALDLLEQIKNG-----ADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGY 84


                 ....
gi 15982815  113 HIIK 116
Cdd:PRK15441  85 HIIK 88
prsA PRK00059
peptidylprolyl isomerase; Provisional
 31-119 3.76e-09

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 52.79  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815   31 KIILTTTREAaveqlKSIREDIVSGkANFEEVATRVS-DCSSAKRGGDLG--SFGRGQMQKPFEEATYALKVGDISDIVD 107
Cdd:PRK00059 201 HILVKTEDEA-----KKVKKRLDKG-EDFAKVAKEVSqDPGSKDKGGDLGdvPYSDSGYDKEFMDGAKALKEGEISAPVK 274

                         90
                 ....*....|..
gi 15982815  108 TDSGVHIIKRTA 119
Cdd:PRK00059 275 TQFGYHIIKAIK 286
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 6-116 2.03e-08

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 50.51  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15982815    6 QVKASHILIKHQgsrrkaswkdpegkiiLTTTREAAVEQLKSIREDIVSGKANFEEVATRVS-DCSSAKRGGDLGsFGRG 84
Cdd:PRK10770 266 EVHARHILLKPS----------------PIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSqDPGSANQGGDLG-WATP 328

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15982815   85 QMQKP-FEEATYALKVGDISDIVDTDSGVHIIK 116
Cdd:PRK10770 329 DIFDPaFRDALMRLNKGQISAPVHSSFGWHLIE 361
 
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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