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Conserved domains on  [gi|219842220|ref|NP_001137254|]
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peptidyl-prolyl cis-trans isomerase FKBP11 isoform 3 precursor [Homo sapiens]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446594)

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|GO:0000413|GO:0061077
PubMed:  27664121
SCOP:  4001062

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-133 1.90e-30

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 105.36  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842220   50 CAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRG-FPPS 127
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80


                  ....*.
gi 219842220  128 VPGTKD 133
Cdd:pfam00254  81 IPPNAT 86
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-133 1.90e-30

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 105.36  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842220   50 CAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRG-FPPS 127
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80


                  ....*.
gi 219842220  128 VPGTKD 133
Cdd:pfam00254  81 IPPNAT 86
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 38-130 1.66e-27

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 97.95  E-value: 1.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842220  38 LQVETLVEPPepcAEPAAFGDTLHIHYTGSLVDGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSH 116
Cdd:COG0545    1 LQYKVLKEGT---GAKPKAGDTVTVHYTGTLLDGTVFDSSYDRgEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPE 77

                         90
                 ....*....|....
gi 219842220 117 LAYGKRGFPPSVPG 130
Cdd:COG0545   78 LAYGERGAGGVIPP 91
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 58-129 2.88e-11

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 58.66  E-value: 2.88e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219842220  58 DTLHIHYTGSLVDGRIIDTSLTR-DPlvIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVP 129
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARgEP--AEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIP 191
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 51-109 7.49e-05

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 41.39  E-value: 7.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219842220   51 AEPAAFGDTLHIHYTGSlVDGRIIDtSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:TIGR00115 146 RGAAEKGDRVTIDFEGF-IDGEAFE-GGKAENFSLELGSGQFIPGFEEQLVGMKAGEEK 202
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-133 1.90e-30

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 105.36  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842220   50 CAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRG-FPPS 127
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80


                  ....*.
gi 219842220  128 VPGTKD 133
Cdd:pfam00254  81 IPPNAT 86
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 38-130 1.66e-27

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 97.95  E-value: 1.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842220  38 LQVETLVEPPepcAEPAAFGDTLHIHYTGSLVDGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSH 116
Cdd:COG0545    1 LQYKVLKEGT---GAKPKAGDTVTVHYTGTLLDGTVFDSSYDRgEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPE 77

                         90
                 ....*....|....
gi 219842220 117 LAYGKRGFPPSVPG 130
Cdd:COG0545   78 LAYGERGAGGVIPP 91
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 57-122 3.57e-19

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 77.83  E-value: 3.57e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219842220  57 GDTLHIHYTGSLVDGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKR 122
Cdd:COG1047    4 GDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 58-129 2.88e-11

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 58.66  E-value: 2.88e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219842220  58 DTLHIHYTGSLVDGRIIDTSLTR-DPlvIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVP 129
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARgEP--AEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIP 191
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 58-125 4.94e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 58.62  E-value: 4.94e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219842220  58 DTLHIHYTGSLVDGRIIDTSLTR-DPLVIELgqKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFP 125
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRgEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 48-109 3.28e-05

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 42.42  E-value: 3.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219842220  48 EPCAEPAAFGDTLHIHYTGSlVDGRIIDtSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:COG0544  152 VPVERAAEEGDRVTIDFEGT-IDGEEFE-GGKAEDYSLELGSGSFIPGFEEQLVGMKAGEEK 211
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 51-109 7.49e-05

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 41.39  E-value: 7.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219842220   51 AEPAAFGDTLHIHYTGSlVDGRIIDtSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:TIGR00115 146 RGAAEKGDRVTIDFEGF-IDGEAFE-GGKAENFSLELGSGQFIPGFEEQLVGMKAGEEK 202
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
 56-123 1.14e-04

peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldI is a FKBP-type peptidyl-prolyl cis-trans isomerase (pfam00254) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockout of this gene abolishes the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. This family is only found in Bacteroidetes containing the suite of genes proposed to confer the gliding motility phenotype.


Pssm-ID: 132555  Cd Length: 177  Bit Score: 40.13  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219842220   56 FGDTLHIHYTGSLVDGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRG 123
Cdd:TIGR03516  88 FGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYG 155
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 62-122 1.53e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 36.61  E-value: 1.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219842220  62 IHYTGSLVDGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKR 122
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 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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