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Conserved domains on  [gi|488614518|ref|WP_002551367|]
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MULTISPECIES: FKBP-type peptidyl-prolyl cis-trans isomerase [Pseudomonas]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11425492)

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
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
131-224 1.35e-38

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 129.15  E-value: 1.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 131 LTPGTGPKPDANGRVEVRYVGRLPDGTIFDQST---QPQWFRLDS--VISGWTSALQTMPTGAKWRLVIPSDQAYGAEGA 205
Cdd:COG0545    6 LKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYdrgEPATFPLGVgqVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGA 85
                         90
                 ....*....|....*....
gi 488614518 206 GDLIDPFTPLVFEIELIAV 224
Cdd:COG0545   86 GGVIPPNSTLVFEVELLDV 104
PRK11570 super family cl29491
peptidyl-prolyl cis-trans isomerase; Provisional
33-224 6.60e-36

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: 125.68  E-value: 6.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518  33 AYSLGASLGERLHQE-VPDLDLKALVDGLKQAYQGKPLALKQERIDQVLRE-HDaaiaQAETAGTDAPTEAALKAERtFM 110
Cdd:PRK11570  14 SYGIGLQVGQQLSESgLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREiHE----RADAVRRERQQAMAAEGVK-FL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 111 DSEKAKPGVKVLADGILMTELTPGTGPKPDANGRVEVRYVGRLPDGTIFDQSTQ---PQWFRLDSVISGWTSALQTMPTG 187
Cdd:PRK11570  89 EENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVArgePAEFPVNGVIPGWIEALTLMPVG 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488614518 188 AKWRLVIPSDQAYGAEGAGDLIDPFTPLVFEIELIAV 224
Cdd:PRK11570 169 SKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
131-224 1.35e-38

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 129.15  E-value: 1.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 131 LTPGTGPKPDANGRVEVRYVGRLPDGTIFDQST---QPQWFRLDS--VISGWTSALQTMPTGAKWRLVIPSDQAYGAEGA 205
Cdd:COG0545    6 LKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYdrgEPATFPLGVgqVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGA 85
                         90
                 ....*....|....*....
gi 488614518 206 GDLIDPFTPLVFEIELIAV 224
Cdd:COG0545   86 GGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
33-224 6.60e-36

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 125.68  E-value: 6.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518  33 AYSLGASLGERLHQE-VPDLDLKALVDGLKQAYQGKPLALKQERIDQVLRE-HDaaiaQAETAGTDAPTEAALKAERtFM 110
Cdd:PRK11570  14 SYGIGLQVGQQLSESgLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREiHE----RADAVRRERQQAMAAEGVK-FL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 111 DSEKAKPGVKVLADGILMTELTPGTGPKPDANGRVEVRYVGRLPDGTIFDQSTQ---PQWFRLDSVISGWTSALQTMPTG 187
Cdd:PRK11570  89 EENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVArgePAEFPVNGVIPGWIEALTLMPVG 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488614518 188 AKWRLVIPSDQAYGAEGAGDLIDPFTPLVFEIELIAV 224
Cdd:PRK11570 169 SKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
136-222 3.17e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 94.57  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518  136 GPKPDANG-RVEVRYVGRLPDGTIFDQST---QPQWFRLDS--VISGWTSALQTMPTGAKWRLVIPSDQAYGAEG-AGDL 208
Cdd:pfam00254   1 GPEKAKKGdRVTVHYTGTLEDGTVFDSSYdrgKPFEFTLGSgqVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80
                          90
                  ....*....|....
gi 488614518  209 IDPFTPLVFEIELI 222
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
32-126 1.56e-15

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: 69.45  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518   32 LAYSLGASLGERLHQEVPDLDLKALVDGLKQAYQGKPLALKQErIDQVLREHDAAIAQAEtagtDAPTEAALKAERTFMD 111
Cdd:pfam01346   4 VSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPLLTDEE-AQEALQAFQEKLQAKQ----EEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*
gi 488614518  112 SEKAKPGVKVLADGI 126
Cdd:pfam01346  79 ENKKKEGVKTTESGL 93
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
131-224 1.35e-38

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 129.15  E-value: 1.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 131 LTPGTGPKPDANGRVEVRYVGRLPDGTIFDQST---QPQWFRLDS--VISGWTSALQTMPTGAKWRLVIPSDQAYGAEGA 205
Cdd:COG0545    6 LKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYdrgEPATFPLGVgqVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGA 85
                         90
                 ....*....|....*....
gi 488614518 206 GDLIDPFTPLVFEIELIAV 224
Cdd:COG0545   86 GGVIPPNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
33-224 6.60e-36

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 125.68  E-value: 6.60e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518  33 AYSLGASLGERLHQE-VPDLDLKALVDGLKQAYQGKPLALKQERIDQVLRE-HDaaiaQAETAGTDAPTEAALKAERtFM 110
Cdd:PRK11570  14 SYGIGLQVGQQLSESgLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREiHE----RADAVRRERQQAMAAEGVK-FL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 111 DSEKAKPGVKVLADGILMTELTPGTGPKPDANGRVEVRYVGRLPDGTIFDQSTQ---PQWFRLDSVISGWTSALQTMPTG 187
Cdd:PRK11570  89 EENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVArgePAEFPVNGVIPGWIEALTLMPVG 168
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488614518 188 AKWRLVIPSDQAYGAEGAGDLIDPFTPLVFEIELIAV 224
Cdd:PRK11570 169 SKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
33-224 1.70e-28

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 108.31  E-value: 1.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518  33 AYSLGASLGERLHQEVPD-------LDLKALVDGLKQAYQGKPlALKQERIDQVLREHDAAI---AQAETAGTDAPTEAA 102
Cdd:PRK10902  49 AYALGASLGRYMENSLKEqeklgikLDKDQLIAGVQDAFADKS-KLSDQEIEQTLQAFEARVksaAQAKMEKDAADNEAK 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518 103 LKAERTFMDSEKakpGVKVLADGILMTELTPGTGPKPDANGRVEVRYVGRLPDGTIFDQS---TQPQWFRLDSVISGWTS 179
Cdd:PRK10902 128 GKKYREKFAKEK---GVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSytrGEPLSFRLDGVIPGWTE 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488614518 180 ALQTMPTGAKWRLVIPSDQAYGAEGAGDlIDPFTPLVFEIELIAV 224
Cdd:PRK10902 205 GLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
136-222 3.17e-25

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 94.57  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518  136 GPKPDANG-RVEVRYVGRLPDGTIFDQST---QPQWFRLDS--VISGWTSALQTMPTGAKWRLVIPSDQAYGAEG-AGDL 208
Cdd:pfam00254   1 GPEKAKKGdRVTVHYTGTLEDGTVFDSSYdrgKPFEFTLGSgqVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80
                          90
                  ....*....|....
gi 488614518  209 IDPFTPLVFEIELI 222
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
32-126 1.56e-15

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: 69.45  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488614518   32 LAYSLGASLGERLHQEVPDLDLKALVDGLKQAYQGKPLALKQErIDQVLREHDAAIAQAEtagtDAPTEAALKAERTFMD 111
Cdd:pfam01346   4 VSYAIGLQIGQQLKQQGIELDLDAFLAGLKDALAGKPLLTDEE-AQEALQAFQEKLQAKQ----EEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*
gi 488614518  112 SEKAKPGVKVLADGI 126
Cdd:pfam01346  79 ENKKKEGVKTTESGL 93
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
145-201 3.01e-05

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 42.40  E-value: 3.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488614518 145 VEVRYVGRLPDGTIFDQST--QPQWFRL--DSVISGWTSALQTMPTGAKWRLVIPSDQAYG 201
Cdd:COG1047    7 VTLHYTLKLEDGEVFDSTFegEPLEFLHgaGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 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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