NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|226693321|ref|NP_001013123|]
View 

peptidyl-prolyl cis-trans isomerase FKBP11 precursor [Rattus norvegicus]

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
SCOP:  4001062

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-141 3.24e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 121.92  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321   50 CTESAAFGDTLHIHYTGSLADGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGY-PPS 127
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 226693321  128 IPADAVVQYDVELI 141
Cdd:pfam00254  81 IPPNATLVFEVELL 94
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-141 3.24e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 121.92  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321   50 CTESAAFGDTLHIHYTGSLADGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGY-PPS 127
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 226693321  128 IPADAVVQYDVELI 141
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 38-142 5.44e-33

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.12  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321  38 LQVETLVQPPescTESAAFGDTLHIHYTGSLADGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSH 116
Cdd:COG0545    1 LQYKVLKEGT---GAKPKAGDTVTVHYTGTLLDGTVFDSSYDRgEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPE 77

                         90       100
                 ....*....|....*....|....*.
gi 226693321 117 LAYGKRGYPPSIPADAVVQYDVELIA 142
Cdd:COG0545   78 LAYGERGAGGVIPPNSTLVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 58-141 3.13e-14

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 69.02  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321  58 DTLHIHYTGSLADGRIIDTSLTR-DPLVIELgqKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGYpPSIPADAVVQY 136
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRgEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVF 241


                 ....*
gi 226693321 137 DVELI 141
Cdd:PRK10902 242 DVELL 246
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
 51-140 1.08e-05

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: 43.98  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321   51 TESAAFGDTLHIHYTGSLADGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGYPPSIPA 130
Cdd:TIGR03516  83 GTTPEFGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYGDQNKIGP 162

                          90
                  ....*....|
gi 226693321  131 DAVVQYDVEL 140
Cdd:TIGR03516 163 NLPIISTVTL 172
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-141 3.24e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 121.92  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321   50 CTESAAFGDTLHIHYTGSLADGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGY-PPS 127
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPV 80

                          90
                  ....*....|....
gi 226693321  128 IPADAVVQYDVELI 141
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 38-142 5.44e-33

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.12  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321  38 LQVETLVQPPescTESAAFGDTLHIHYTGSLADGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSH 116
Cdd:COG0545    1 LQYKVLKEGT---GAKPKAGDTVTVHYTGTLLDGTVFDSSYDRgEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPE 77

                         90       100
                 ....*....|....*....|....*.
gi 226693321 117 LAYGKRGYPPSIPADAVVQYDVELIA 142
Cdd:COG0545   78 LAYGERGAGGVIPPNSTLVFEVELLD 103
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 57-122 7.47e-20

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 81.30  E-value: 7.47e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226693321  57 GDTLHIHYTGSLADGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKR 122
Cdd:COG1047    4 GDVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGER 69
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 58-141 3.13e-14

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 69.02  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321  58 DTLHIHYTGSLADGRIIDTSLTR-DPLVIELgqKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGYpPSIPADAVVQY 136
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRgEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVF 241


                 ....*
gi 226693321 137 DVELI 141
Cdd:PRK10902 242 DVELL 246
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 58-144 6.06e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 67.52  E-value: 6.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321  58 DTLHIHYTGSLADGRIIDTSLTR-DPlvIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGYPPSIPADAVVQY 136
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARgEP--AEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*...
gi 226693321 137 DVELIALI 144
Cdd:PRK11570 199 EVELLEIL 206
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
 51-140 1.08e-05

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: 43.98  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693321   51 TESAAFGDTLHIHYTGSLADGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKRGYPPSIPA 130
Cdd:TIGR03516  83 GTTPEFGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYGDQNKIGP 162

                          90
                  ....*....|
gi 226693321  131 DAVVQYDVEL 140
Cdd:TIGR03516 163 NLPIISTVTL 172
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 62-136 1.29e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 40.85  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226693321  62 IHYTGSLADGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAVIPSHLAYGKrgyppsiPADAVVQY 136
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV-------PSPDLIQY 81
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 52-109 9.26e-03

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: 36.38  E-value: 9.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 226693321   52 ESAAFGDTLHIHYTGSLaDGRIIDtSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:TIGR00115 147 GAAEKGDRVTIDFEGFI-DGEAFE-GGKAENFSLELGSGQFIPGFEEQLVGMKAGEEK 202
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH