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Conserved domains on  [gi|488975797|ref|WP_002886687|]
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MULTISPECIES: FKBP-type peptidyl-prolyl cis-trans isomerase [Klebsiella]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 11485412)

FKBP-type peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 5.94e-152

peptidyl-prolyl cis-trans isomerase; Provisional


:

Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 419.20  E-value: 5.94e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797   1 MATPTFDTIEAQASYGIGLQVGQQLSESGLQGLLPEALVAGIADALEGNQPQVPVEAVHRALREIHERADAVRRERFQAM 80
Cdd:PRK11570   1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797  81 AADGQKYLDENREKEGVNSTESGLQFRVLTQGEGPIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVTGVIGGWIE 160
Cdd:PRK11570  81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488975797 161 ALTLMPVGSKWELTIPHNLAYGERGAGASIPPFSTLIFEVELLDII 206
Cdd:PRK11570 161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 5.94e-152

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 419.20  E-value: 5.94e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797   1 MATPTFDTIEAQASYGIGLQVGQQLSESGLQGLLPEALVAGIADALEGNQPQVPVEAVHRALREIHERADAVRRERFQAM 80
Cdd:PRK11570   1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797  81 AADGQKYLDENREKEGVNSTESGLQFRVLTQGEGPIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVTGVIGGWIE 160
Cdd:PRK11570  81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488975797 161 ALTLMPVGSKWELTIPHNLAYGERGAGASIPPFSTLIFEVELLDII 206
Cdd:PRK11570 161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-205 6.87e-54

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 167.28  E-value: 6.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797 104 LQFRVLTQGEGPIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--TGVIGGWIEALTLMPVGSKWELTIPHNLAY 181
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLgvGQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 488975797 182 GERGAGASIPPFSTLIFEVELLDI 205
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-203 8.65e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.16  E-value: 8.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797  117 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--TGVIGGWIEALTLMPVGSKWELTIPHNLAYGERG-AGASIPPF 193
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 488975797  194 STLIFEVELL 203
Cdd:pfam00254  85 ATLVFEVELL 94
 
Name Accession Description Interval E-value
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-206 5.94e-152

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 419.20  E-value: 5.94e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797   1 MATPTFDTIEAQASYGIGLQVGQQLSESGLQGLLPEALVAGIADALEGNQPQVPVEAVHRALREIHERADAVRRERFQAM 80
Cdd:PRK11570   1 MTTPTFDSIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGLADALEGKHPAVPVDVVHRALREIHERADAVRRERQQAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797  81 AADGQKYLDENREKEGVNSTESGLQFRVLTQGEGPIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVTGVIGGWIE 160
Cdd:PRK11570  81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488975797 161 ALTLMPVGSKWELTIPHNLAYGERGAGASIPPFSTLIFEVELLDII 206
Cdd:PRK11570 161 ALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEIL 206
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
104-205 6.87e-54

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 167.28  E-value: 6.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797 104 LQFRVLTQGEGPIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--TGVIGGWIEALTLMPVGSKWELTIPHNLAY 181
Cdd:COG0545    1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLgvGQVIPGWDEGLQGMKVGGKRRLVIPPELAY 80
                         90       100
                 ....*....|....*....|....
gi 488975797 182 GERGAGASIPPFSTLIFEVELLDI 205
Cdd:COG0545   81 GERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
2-205 3.65e-43

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 145.68  E-value: 3.65e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797   2 ATPTFDTIEAQASYGIGLQVGQQLSES-------GLQgLLPEALVAGIADALeGNQPQVPVEAVHRALREIHERADAVRR 74
Cdd:PRK10902  37 SKAAFKNDDQQSAYALGASLGRYMENSlkeqeklGIK-LDKDQLIAGVQDAF-ADKSKLSDQEIEQTLQAFEARVKSAAQ 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797  75 ERFQAMAAD----GQKYLDENREKEGVNSTESGLQFRVLTQGEGPIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFP 150
Cdd:PRK10902 115 AKMEKDAADneakGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFR 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488975797 151 VTGVIGGWIEALTLMPVGSKWELTIPHNLAYGERGAgASIPPFSTLIFEVELLDI 205
Cdd:PRK10902 195 LDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVFDVELLDV 248
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
117-203 8.65e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.16  E-value: 8.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797  117 PARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPV--TGVIGGWIEALTLMPVGSKWELTIPHNLAYGERG-AGASIPPF 193
Cdd:pfam00254   5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLgsGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPVIPPN 84
                          90
                  ....*....|
gi 488975797  194 STLIFEVELL 203
Cdd:pfam00254  85 ATLVFEVELL 94
FKBP_N pfam01346
Domain amino terminal to FKBP-type peptidyl-prolyl isomerase; This family is only found at the ...
10-108 7.26e-26

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: 95.64  E-value: 7.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797   10 EAQASYGIGLQVGQQLSESGLqGLLPEALVAGIADALEGNQPQVPVEAvHRALREIHERADAVRRERFQAMAADGQKYLD 89
Cdd:pfam01346   1 KDKVSYAIGLQIGQQLKQQGI-ELDLDAFLAGLKDALAGKPLLTDEEA-QEALQAFQEKLQAKQEEQAEKNKAEGEAFLA 78
                          90
                  ....*....|....*....
gi 488975797   90 ENREKEGVNSTESGLQFRV 108
Cdd:pfam01346  79 ENKKKEGVKTTESGLQYKV 97
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
121-184 4.31e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 55.49  E-value: 4.31e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488975797 121 DRVRVHYTGKLIDGTVFDSSVaRGEPAEFpvtgVIG-GWI-----EALTLMPVGSKWELTIPHNLAYGER 184
Cdd:COG1047    5 DVVTLHYTLKLEDGEVFDSTF-EGEPLEF----LHGaGQLipgleEALEGMEVGDKKTVTLPPEEAYGER 69
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
123-184 8.01e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 35.45  E-value: 8.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488975797 123 VRVHYTGKLIDGTVFDSSVARGEPAEFPV-TGVIGGWIEA-LTLMPVGSKWELTIPHNLAYGER 184
Cdd:PRK15095  11 VLVHFTLKLDDGSTAESTRNNGKPALFRLgDGSLSEGLEQqLLGLKVGDKKTFSLEPEAAFGVP 74
 
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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