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Conserved domains on  [gi|291556857|emb|CBL33974|]
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PPIC-type PPIASE domain [[Eubacterium] siraeum V10Sc8a]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
prsA super family cl35053
peptidylprolyl isomerase; Provisional
100-427 1.28e-13

peptidylprolyl isomerase; Provisional


The actual alignment was detected with superfamily member PRK00059:

Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 71.67  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 100 RKNIIDMLTNEKLILRKAKELGLDQLTEEEMAEVEKAYtknlsdwyasfekkaktalgistdgtsgtedsANDEKILEKE 179
Cdd:PRK00059  86 KEQILDSLITEKVLLQKAKELKLIPSEEELNKEVDKKI--------------------------------NEIKKQFNND 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 180 KELFNEYIAGFGLTEDTFLMWQTNTAIQKKVNDYLLKDITVSDSEIDDYitklkaeakqaYEKSASSYATdseykkvwip 259
Cdd:PRK00059 134 EEQFEEALKATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKY-----------YNENKSKFTE---------- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 260 edaryikyiavgiassdyaeinaarNESGADDAEIDKKRDEKLAEIKEKADAalkkatadGADFDAVVKEYSSAYSESTA 339
Cdd:PRK00059 193 -------------------------KPNTMHLAHILVKTEDEAKKVKKRLDK--------GEDFAKVAKEVSQDPGSKDK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 340 GEQILVLNSkgliSDALYDAVFALE----KPGDISGLIPTDSGYYIVKYVSDAKVTDSDLSNYRKTVRQELLTSRQSEKT 415
Cdd:PRK00059 240 GGDLGDVPY----SDSGYDKEFMDGakalKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVF 315
                        330
                 ....*....|..
gi 291556857 416 NAILEEWRSAVN 427
Cdd:PRK00059 316 KKKIEEWKKALK 327
 
Name Accession Description Interval E-value
prsA PRK00059
peptidylprolyl isomerase; Provisional
100-427 1.28e-13

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 71.67  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 100 RKNIIDMLTNEKLILRKAKELGLDQLTEEEMAEVEKAYtknlsdwyasfekkaktalgistdgtsgtedsANDEKILEKE 179
Cdd:PRK00059  86 KEQILDSLITEKVLLQKAKELKLIPSEEELNKEVDKKI--------------------------------NEIKKQFNND 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 180 KELFNEYIAGFGLTEDTFLMWQTNTAIQKKVNDYLLKDITVSDSEIDDYitklkaeakqaYEKSASSYATdseykkvwip 259
Cdd:PRK00059 134 EEQFEEALKATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKY-----------YNENKSKFTE---------- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 260 edaryikyiavgiassdyaeinaarNESGADDAEIDKKRDEKLAEIKEKADAalkkatadGADFDAVVKEYSSAYSESTA 339
Cdd:PRK00059 193 -------------------------KPNTMHLAHILVKTEDEAKKVKKRLDK--------GEDFAKVAKEVSQDPGSKDK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 340 GEQILVLNSkgliSDALYDAVFALE----KPGDISGLIPTDSGYYIVKYVSDAKVTDSDLSNYRKTVRQELLTSRQSEKT 415
Cdd:PRK00059 240 GGDLGDVPY----SDSGYDKEFMDGakalKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVF 315
                        330
                 ....*....|..
gi 291556857 416 NAILEEWRSAVN 427
Cdd:PRK00059 316 KKKIEEWKKALK 327
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
294-427 3.55e-13

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 66.52  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 294 IDKKRDEKLAEIKEKADAALKKATAdGADFDAVVKEYSSAY-SESTAGEqiLVLNSKGLISDALYDAVFALeKPGDISGL 372
Cdd:COG0760   16 VKVPPSEDRAKAEAKAEELLAQLKA-GADFAELAKEYSQDPgSAANGGD--LGWFSRGQLVPEFEEAAFAL-KPGEISGP 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 291556857 373 IPTDSGYYIVKYVSDAKVTDSDLSNYRKTVRQELltsrQSEKTNAILEEWRSAVN 427
Cdd:COG0760   92 VKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQEL----FQQALEAWLEELRKKAK 142
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
294-383 5.23e-10

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: 56.15  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857  294 IDKKRDEKLAEIKEKADAALKKATADGADFDAVVKEYSSAYSESTAGEqILVLNSKGLISDALYDAVFALeKPGDISGLI 373
Cdd:pfam00639   6 TPEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGG-DLGWFTRGQLPPEFEKAAFAL-KPGEISGPV 83
                          90
                  ....*....|
gi 291556857  374 PTDSGYYIVK 383
Cdd:pfam00639  84 ETRFGFHIIK 93
 
Name Accession Description Interval E-value
prsA PRK00059
peptidylprolyl isomerase; Provisional
100-427 1.28e-13

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 71.67  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 100 RKNIIDMLTNEKLILRKAKELGLDQLTEEEMAEVEKAYtknlsdwyasfekkaktalgistdgtsgtedsANDEKILEKE 179
Cdd:PRK00059  86 KEQILDSLITEKVLLQKAKELKLIPSEEELNKEVDKKI--------------------------------NEIKKQFNND 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 180 KELFNEYIAGFGLTEDTFLMWQTNTAIQKKVNDYLLKDITVSDSEIDDYitklkaeakqaYEKSASSYATdseykkvwip 259
Cdd:PRK00059 134 EEQFEEALKATGFTEETFKEYLKNQIIIEKVINEVVKDVKVTDKDAQKY-----------YNENKSKFTE---------- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 260 edaryikyiavgiassdyaeinaarNESGADDAEIDKKRDEKLAEIKEKADAalkkatadGADFDAVVKEYSSAYSESTA 339
Cdd:PRK00059 193 -------------------------KPNTMHLAHILVKTEDEAKKVKKRLDK--------GEDFAKVAKEVSQDPGSKDK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 340 GEQILVLNSkgliSDALYDAVFALE----KPGDISGLIPTDSGYYIVKYVSDAKVTDSDLSNYRKTVRQELLTSRQSEKT 415
Cdd:PRK00059 240 GGDLGDVPY----SDSGYDKEFMDGakalKEGEISAPVKTQFGYHIIKAIKKKEYPVKPFDSVKEDIKKQLLQEKQSEVF 315
                        330
                 ....*....|..
gi 291556857 416 NAILEEWRSAVN 427
Cdd:PRK00059 316 KKKIEEWKKALK 327
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
294-427 3.55e-13

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


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 66.52  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 294 IDKKRDEKLAEIKEKADAALKKATAdGADFDAVVKEYSSAY-SESTAGEqiLVLNSKGLISDALYDAVFALeKPGDISGL 372
Cdd:COG0760   16 VKVPPSEDRAKAEAKAEELLAQLKA-GADFAELAKEYSQDPgSAANGGD--LGWFSRGQLVPEFEEAAFAL-KPGEISGP 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 291556857 373 IPTDSGYYIVKYVSDAKVTDSDLSNYRKTVRQELltsrQSEKTNAILEEWRSAVN 427
Cdd:COG0760   92 VKTQFGYHIIKVEDRRPAETPPFEEVKQQIRQEL----FQQALEAWLEELRKKAK 142
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
294-383 5.23e-10

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: 56.15  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857  294 IDKKRDEKLAEIKEKADAALKKATADGADFDAVVKEYSSAYSESTAGEqILVLNSKGLISDALYDAVFALeKPGDISGLI 373
Cdd:pfam00639   6 TPEASERDRAEAKAKAEEILEQLKSGEDSFAELARKYSDDCPSAANGG-DLGWFTRGQLPPEFEKAAFAL-KPGEISGPV 83
                          90
                  ....*....|
gi 291556857  374 PTDSGYYIVK 383
Cdd:pfam00639  84 ETRFGFHIIK 93
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
282-383 4.06e-05

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: 42.74  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857  282 AARNESGADDAEIDKKRDEKLAEIKEkadaalkkatadGADFDAVVKEYSS-AYSESTAGEqiLVLNSKGLISDALYDAV 360
Cdd:pfam13616  24 SYSQAVSRTEEEAKAKADSLLAALKN------------GADFAALAKTYSDdPASKNNGGD--LGWFTKGQMVKEFEDAV 89
                          90       100
                  ....*....|....*....|...
gi 291556857  361 FALeKPGDISGLIPTDSGYYIVK 383
Cdd:pfam13616  90 FSL-KVGEISGVVKTQFGFHIIK 111
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
302-383 6.71e-05

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 42.43  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857  302 LAEIKEKADAALKKATADGADFDAVVKEYSSAYSESTAGEqilVLNSKGLISDALYDAVFALeKPGDISGLIPTDSGYYI 381
Cdd:pfam13145  27 ILVFKDQVAADAALALLKAGALEDFAALAKGEGIKAATLD---IVESAELLPEELAKAAFAL-KPGEVSGPIKTGNGYYV 102

                  ..
gi 291556857  382 VK 383
Cdd:pfam13145 103 VR 104
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
294-383 3.96e-03

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


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 37.31  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 294 IDKKRDEKLAEIKEKADAALKKATADGADFDAVVKEYSSAYSESTAGEQ--ILVLNSKGLISDALYDAVFALeKPGDISG 371
Cdd:PTZ00356  22 VSRRTGKPVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKggDLGFFGRGQMQKPFEDAAFAL-KVGEISD 100
                         90
                 ....*....|..
gi 291556857 372 LIPTDSGYYIVK 383
Cdd:PTZ00356 101 IVHTDSGVHIIL 112
prsA PRK01326
foldase protein PrsA; Reviewed
201-415 8.42e-03

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 38.26  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 201 QTNTAIQKKVNDYLLKDI-------TVSDSEIDDYItklkAEAKQAYEKSASSYATDSEYKKVWIPEDARYIKYIAVGIA 273
Cdd:PRK01326  48 KNNPSAQQAMLNLTISRVfekqygdKVSDKEVEKAY----AKTAKQYGASFSRALAQAGLTPETYKAQIRTSKLVEYAVK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291556857 274 SSDYAEINAARNESGADDAEIDKKRDEKLAEIKEKADAALKKATADGADFDAVVKEYSSAYSEstaGEQILVLNSKGLIS 353
Cdd:PRK01326 124 EAAKKELTDEAYKKAYEEYTPEVTAQIIRLDNEDKAKSVLEEAKAEGADFAQIAKENTTTKEK---KGEYKFDSGSTNVP 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291556857 354 DALYDAVFALEKpGDISGLIPT------DSGYYIVKYVSDAKvTDSDLSNYRKTVRQELLTSRQSEKT 415
Cdd:PRK01326 201 EQVKKAAFALDE-DGVSDVISVldptayQSKYYIVKVTKKTE-KKSDWKDYKKRLKAIILAQKQNDSN 266
 
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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