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Conserved domains on  [gi|1245250603|gb|PBY78627|]
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peptidylprolyl isomerase [Pseudomonas aeruginosa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11570 super family cl29491
peptidyl-prolyl cis-trans isomerase; Provisional
1-205 8.50e-81

peptidyl-prolyl cis-trans isomerase; Provisional


The actual alignment was detected with superfamily member PRK11570:

Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 239.31  E-value: 8.50e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603   1 MSELNLTTDEARVSYGIGRQLGDQLRENPVPGMTLDAVLAGLSDAFAGIDSRVSGEALSASFQVIRERMQAEAQAKAEVA 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603  81 AGEGRAYLAENAKREGVTVLPSGLQFEVLSTGEGAKPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVGGVIAGWVE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1245250603 161 ALQLMNAGSKWRLHVPSELAYGGQAVG-SIPPHSVLVFDVELLEIL 205
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVFEVELLEIL 206
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-205 8.50e-81

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 239.31  E-value: 8.50e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603   1 MSELNLTTDEARVSYGIGRQLGDQLRENPVPGMTLDAVLAGLSDAFAGIDSRVSGEALSASFQVIRERMQAEAQAKAEVA 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603  81 AGEGRAYLAENAKREGVTVLPSGLQFEVLSTGEGAKPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVGGVIAGWVE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1245250603 161 ALQLMNAGSKWRLHVPSELAYGGQAVG-SIPPHSVLVFDVELLEIL 205
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-204 1.86e-51

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 161.12  E-value: 1.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603 104 LQFEVLSTGEGAKPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVG--GVIAGWVEALQLMNAGSKWRLHVPSELAY 181
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1245250603 182 GGQAVG-SIPPHSVLVFDVELLEI 204
Cdd:COG0545    81 GERGAGgVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
116-202 3.51e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 127.31  E-value: 3.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603 116 KPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVG--GVIAGWVEALQLMNAGSKWRLHVPSELAYG--GQAVGSIPP 191
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGsgQVIPGWDEGLVGMKVGEKRKLTIPPELAYGeeGLAGPVIPP 83
                          90
                  ....*....|.
gi 1245250603 192 HSVLVFDVELL 202
Cdd:pfam00254  84 NATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-205 8.50e-81

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 239.31  E-value: 8.50e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603   1 MSELNLTTDEARVSYGIGRQLGDQLRENPVPGMTLDAVLAGLSDAFAGIDSRVSGEALSASFQVIRERMQAEAQAKAEVA 80
Cdd:PRK11570    1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603  81 AGEGRAYLAENAKREGVTVLPSGLQFEVLSTGEGAKPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVGGVIAGWVE 160
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1245250603 161 ALQLMNAGSKWRLHVPSELAYGGQAVG-SIPPHSVLVFDVELLEIL 205
Cdd:PRK11570  161 ALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVFEVELLEIL 206
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
8-204 3.44e-53

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 171.10  E-value: 3.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603   8 TDEARVSYGIGRQLG----DQLRENPVPGMTLDA--VLAGLSDAFAGiDSRVSGEALSASFQVIRERMQAEAQAKAEVAA 81
Cdd:PRK10902   43 NDDQQSAYALGASLGrymeNSLKEQEKLGIKLDKdqLIAGVQDAFAD-KSKLSDQEIEQTLQAFEARVKSAAQAKMEKDA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603  82 GE----GRAYLAENAKREGVTVLPSGLQFEVLSTGEGAKPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVGGVIAG 157
Cdd:PRK10902  122 ADneakGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPG 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1245250603 158 WVEALQLMNAGSKWRLHVPSELAYGGQAVGSIPPHSVLVFDVELLEI 204
Cdd:PRK10902  202 WTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLDV 248
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-204 1.86e-51

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 161.12  E-value: 1.86e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603 104 LQFEVLSTGEGAKPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVG--GVIAGWVEALQLMNAGSKWRLHVPSELAY 181
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                          90       100
                  ....*....|....*....|....
gi 1245250603 182 GGQAVG-SIPPHSVLVFDVELLEI 204
Cdd:COG0545    81 GERGAGgVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
116-202 3.51e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 127.31  E-value: 3.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603 116 KPSREDTVRTHYHGTLIDGTVFDSSYQRGQPAEFPVG--GVIAGWVEALQLMNAGSKWRLHVPSELAYG--GQAVGSIPP 191
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGsgQVIPGWDEGLVGMKVGEKRKLTIPPELAYGeeGLAGPVIPP 83
                          90
                  ....*....|.
gi 1245250603 192 HSVLVFDVELL 202
Cdd:pfam00254  84 NATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
10-108 4.37e-31

Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the amino terminus of pfam00254. This entry represents the N-terminal domain found in FKBP-type peptidylprolyl isomerases (PPIase). The N-terminal domain forms the dimer interface by the mutual exchange of two beta-strands between monomers.


Pssm-ID: 460169  Cd Length: 97  Bit Score: 109.12  E-value: 4.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1245250603  10 EARVSYGIGRQLGDQLrENPVPGMTLDAVLAGLSDAFAGiDSRVSGEALSASFQVIRERMQAEAQAKAEVAAGEGRAYLA 89
Cdd:pfam01346   1 KDKVSYAIGLQIGQQL-KQQGIELDLDAFLAGLKDALAG-KPLLTDEEAQEALQAFQEKLQAKQEEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*....
gi 1245250603  90 ENAKREGVTVLPSGLQFEV 108
Cdd:pfam01346  79 ENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
121-182 9.71e-10

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 54.72  E-value: 9.71e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1245250603 121 DTVRTHYHGTLIDGTVFDSSYQRgQPAEFPVGG--VIAGWVEALQLMNAGSKWRLHVPSELAYG 182
Cdd:COG1047     5 DVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAgqLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
 
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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