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Conserved domains on  [gi|1326527264|gb|PMH22507|]
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peptidylprolyl isomerase [Vibrio splendidus]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 139723)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755
SCOP:  4001062

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FKBP_C super family cl19519
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-126 2.58e-54

FKBP-type peptidyl-prolyl cis-trans isomerase;


The actual alignment was detected with superfamily member PRK15095:

Pssm-ID: 473184 [Multi-domain]  Cd Length: 156  Bit Score: 167.19  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326527264   1 MKDGSVADSTENMGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFGMPNPDHIHHMDRAKFVGDSEVEVGTI 80
Cdd:PRK15095   19 LDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQYFSRRDFMDAGEPEIGAI 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1326527264  81 MAFSGPDGMEIPGIITEIAGDSVTVDFNHPLAGQDVTFDVNILAVD 126
Cdd:PRK15095   99 MLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEID 144
 
Name Accession Description Interval E-value
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-126 2.58e-54

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 167.19  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326527264   1 MKDGSVADSTENMGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFGMPNPDHIHHMDRAKFVGDSEVEVGTI 80
Cdd:PRK15095   19 LDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQYFSRRDFMDAGEPEIGAI 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1326527264  81 MAFSGPDGMEIPGIITEIAGDSVTVDFNHPLAGQDVTFDVNILAVD 126
Cdd:PRK15095   99 MLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEID 144
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
2-125 1.36e-49

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 154.49  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326527264   2 KDGSVADSTENmGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFGMPNPDHIHHMDRAKFVGDSEVEVGTIM 81
Cdd:COG1047    16 EDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPREQFPEDEELEVGMQV 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1326527264  82 AFSGPDGMEIPGIITEIAGDSVTVDFNHPLAGQDVTFDVNILAV 125
Cdd:COG1047    95 EFQTPDGQEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-54 7.57e-06

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 41.41  E-value: 7.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1326527264   2 KDGSVADSTENMGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFG 54
Cdd:pfam00254  20 EDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYG 72
 
Name Accession Description Interval E-value
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
1-126 2.58e-54

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 167.19  E-value: 2.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326527264   1 MKDGSVADSTENMGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFGMPNPDHIHHMDRAKFVGDSEVEVGTI 80
Cdd:PRK15095   19 LDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVPSPDLIQYFSRRDFMDAGEPEIGAI 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1326527264  81 MAFSGPDGMEIPGIITEIAGDSVTVDFNHPLAGQDVTFDVNILAVD 126
Cdd:PRK15095   99 MLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEID 144
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
2-125 1.36e-49

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 154.49  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326527264   2 KDGSVADSTENmGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFGMPNPDHIHHMDRAKFVGDSEVEVGTIM 81
Cdd:COG1047    16 EDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGERDPELVQTVPREQFPEDEELEVGMQV 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1326527264  82 AFSGPDGMEIPGIITEIAGDSVTVDFNHPLAGQDVTFDVNILAV 125
Cdd:COG1047    95 EFQTPDGQEVPGTVTEVDDDTVTVDFNHPLAGKTLTFDVEVVEV 138
PRK10737 PRK10737
peptidylprolyl isomerase;
2-125 2.04e-13

peptidylprolyl isomerase;


Pssm-ID: 236748  Cd Length: 196  Bit Score: 63.42  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1326527264   2 KDGSVADSTEnMGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFGMPNPDHIHHMDRAKFVGDSEVEVGtiM 81
Cdd:PRK10737   18 EDGVLVDESP-VSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVPKDVFMGVDELQVG--M 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1326527264  82 AF-SGPDGMEIPGIITEIAGDSVTVDFNHPLAGQDVTFDVNILAV 125
Cdd:PRK10737   95 RFlAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAI 139
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
2-54 7.57e-06

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 41.41  E-value: 7.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1326527264   2 KDGSVADSTENMGKPAKFVMGDGSLSENFEQCLIGLETGTEKSIELKAQDAFG 54
Cdd:pfam00254  20 EDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYG 72
 
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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