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Conserved domains on  [gi|7706131|ref|NP_057678|]
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peptidyl-prolyl cis-trans isomerase FKBP11 isoform 1 precursor [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-141 1.39e-33

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 278674  Cd Length: 94  Bit Score: 116.91  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131     50 CAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGF-PPS 127
Cdd:pfam00254   1 GPEKAKKGDTVTVHYTGKLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGGV 80
                          90
                  ....*....|....
gi 7706131    128 VPADAVVQYDVELI 141
Cdd:pfam00254  81 IPPNATLVFEVELL 94
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-141 1.39e-33

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 278674  Cd Length: 94  Bit Score: 116.91  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131     50 CAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGF-PPS 127
Cdd:pfam00254   1 GPEKAKKGDTVTVHYTGKLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGGV 80
                          90
                  ....*....|....
gi 7706131    128 VPADAVVQYDVELI 141
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
62-136 2.99e-04

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


Pssm-ID: 237908  Cd Length: 156  Bit Score: 38.53  E-value: 2.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7706131    62 IHYTGSLVDGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKrgfppsvPADAVVQY 136
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV-------PSPDLIQY 81
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
57-142 4.21e-25

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


Pssm-ID: 223619 [Multi-domain]  Cd Length: 205  Bit Score: 97.87  E-value: 4.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131   57 GDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQkqVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVPADAVVQ 135
Cdd:COG0545 119 GDTVTVHYTGTLIDGTVFDSSYDRGqPAEFPLGG--VIPGWDEGLQGMKVGGKRKLTIPPELAYGERGVPGVIPPNSTLV 196

                ....*..
gi 7706131  136 YDVELIA 142
Cdd:COG0545 197 FEVELLD 203
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
58-141 2.65e-14

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 67.87  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131    58 DTLHIHYTGSLVDGRIIDTSLTR-DPLVIELgqKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFpPSVPADAVVQY 136
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRgEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVF 241

                 ....*
gi 7706131   137 DVELI 141
Cdd:PRK10902 242 DVELL 246
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
56-123 1.04e-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 [Multi-domain]  Cd Length: 177  Bit Score: 40.13  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706131     56 FGDTLHIHYTGSLVDGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRG 123
Cdd:TIGR03516  88 FGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYG 155
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
50-141 1.39e-33

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 278674  Cd Length: 94  Bit Score: 116.91  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131     50 CAEPAAFGDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGF-PPS 127
Cdd:pfam00254   1 GPEKAKKGDTVTVHYTGKLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGGV 80
                          90
                  ....*....|....
gi 7706131    128 VPADAVVQYDVELI 141
Cdd:pfam00254  81 IPPNATLVFEVELL 94
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
62-136 2.99e-04

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


Pssm-ID: 237908  Cd Length: 156  Bit Score: 38.53  E-value: 2.99e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7706131    62 IHYTGSLVDGRIIDTSLTR-DPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKrgfppsvPADAVVQY 136
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV-------PSPDLIQY 81
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
57-142 4.21e-25

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


Pssm-ID: 223619 [Multi-domain]  Cd Length: 205  Bit Score: 97.87  E-value: 4.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131   57 GDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQkqVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVPADAVVQ 135
Cdd:COG0545 119 GDTVTVHYTGTLIDGTVFDSSYDRGqPAEFPLGG--VIPGWDEGLQGMKVGGKRKLTIPPELAYGERGVPGVIPPNSTLV 196

                ....*..
gi 7706131  136 YDVELIA 142
Cdd:COG0545 197 FEVELLD 203
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
58-141 2.65e-14

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 67.87  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131    58 DTLHIHYTGSLVDGRIIDTSLTR-DPLVIELgqKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFpPSVPADAVVQY 136
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRgEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGV-PGIPANSTLVF 241

                 ....*
gi 7706131   137 DVELI 141
Cdd:PRK10902 242 DVELL 246
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
58-144 3.65e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 66.74  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7706131    58 DTLHIHYTGSLVDGRIIDTSLTR-DPlvIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRGFPPSVPADAVVQY 136
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARgEP--AEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198

                 ....*...
gi 7706131   137 DVELIALI 144
Cdd:PRK11570 199 EVELLEIL 206
SlpA COG1047
FKBP-type peptidyl-prolyl cis-trans isomerase 2 [Posttranslational modification, protein ...
57-122 5.41e-14

FKBP-type peptidyl-prolyl cis-trans isomerase 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223976 [Multi-domain]  Cd Length: 174  Bit Score: 65.74  E-value: 5.41e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7706131   57 GDTLHIHYTGSLVDGRIIDTSLTRD-PLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKR 122
Cdd:COG1047   6 GDVVSLHYTLKVEDGEVVDTTDENYgPLTFIVGAGQLIPGLEEALLGKEVGEEFTVEIPPEDAFGEY 72
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
56-123 1.04e-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 [Multi-domain]  Cd Length: 177  Bit Score: 40.13  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7706131     56 FGDTLHIHYTGSLVDGRIIDTSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKRRAIIPSHLAYGKRG 123
Cdd:TIGR03516  88 FGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYG 155
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
48-109 1.80e-04

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


Pssm-ID: 223618 [Multi-domain]  Cd Length: 441  Bit Score: 40.34  E-value: 1.80e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7706131   48 EPCAEPAAFGDTLHIHYTGSlVDGRIIDtSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:COG0544 152 EPVEGAAENGDRVTIDFEGS-VDGEEFE-GGKAENFSLELGSGRFIPGFEDQLVGMKAGEEK 211
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
51-109 3.69e-04

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: 39.08  E-value: 3.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 7706131     51 AEPAAFGDTLHIHYTGSlVDGRIIDtSLTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:TIGR00115 146 RGAAEKGDRVTIDFEGF-IDGEAFE-GGKAENFSLELGSGQFIPGFEEQLVGMKAGEEK 202
tig PRK01490
trigger factor; Provisional
48-109 6.62e-03

trigger factor; Provisional


Pssm-ID: 234956 [Multi-domain]  Cd Length: 435  Bit Score: 35.52  E-value: 6.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7706131    48 EPCAEPAAFGDTLHIHYTGSlVDGRIIDTSlTRDPLVIELGQKQVIPGLEQSLLDMCVGEKR 109
Cdd:PRK01490 152 VPVERPAENGDRVTIDFVGS-IDGEEFEGG-KAEDFSLELGSGRFIPGFEEQLVGMKAGEEK 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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