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Conserved domains on  [gi|147899811|ref|NP_001087265|]
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FK506 binding protein 11 precursor [Xenopus laevis]

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List of domain hits

Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-132 3.85e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 249719  Cd Length: 94  Bit Score: 127.74  E-value: 3.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811   42 CTETAVMGDTIHLHYTGRLEDGRIIDSSLSRD-PLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGY-PPS 119
Cdd:pfam00254   1 GPRKAKKGDTVTVHYTGKLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLLGMKVGEKRKLTIPPELAYGEEGLaGGV 80
                          90
                  ....*....|...
gi 147899811  120 IPGDAVLQFETEV 132
Cdd:pfam00254  81 IPPNATLVFEVEL 93
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-132 3.85e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 249719  Cd Length: 94  Bit Score: 127.74  E-value: 3.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811   42 CTETAVMGDTIHLHYTGRLEDGRIIDSSLSRD-PLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGY-PPS 119
Cdd:pfam00254   1 GPRKAKKGDTVTVHYTGKLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLLGMKVGEKRKLTIPPELAYGEEGLaGGV 80
                          90
                  ....*....|...
gi 147899811  120 IPGDAVLQFETEV 132
Cdd:pfam00254  81 IPPNATLVFEVEL 93
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
54-113 7.76e-08

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


Pssm-ID: 237908  Cd Length: 156  Bit Score: 47.78  E-value: 7.76e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 147899811  54 LHYTGRLEDGRIIDSSLSR-DPLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGK 113
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
15-134 1.03e-29

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


Pssm-ID: 223619 [Multi-domain]  Cd Length: 205  Bit Score: 109.04  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811  15 TLRAETPEEDSENVTE--LVIETVEKPDSctETAVMGDTIHLHYTGRLEDGRIIDSSLSRD-PLVVELGkkQVIPGLETS 91
Cdd:COG0545   85 AFLEKNAKEKGVKTLPsgLQYKVLKAGDG--AAPKKGDTVTVHYTGTLIDGTVFDSSYDRGqPAEFPLG--GVIPGWDEG 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 147899811  92 LVGMCVGEKRKVVIPPHLAYGKKGYPPSIPGDAVLQFETEVMA 134
Cdd:COG0545  161 LQGMKVGGKRKLTIPPELAYGERGVPGVIPPNSTLVFEVELLD 203
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
50-133 1.68e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 70.21  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811  50 DTIHLHYTGRLEDGRIIDSSLSR-DPlvVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGYPPSIPGDAVLQF 128
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARgEP--AEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198

                 ....*
gi 147899811 129 ETEVM 133
Cdd:PRK11570 199 EVELL 203
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
37-120 9.15e-07

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: 45.14  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811   37 EKPDSCTETAVMGDTIHLHYTGRLEDGRIIDSSLSRDPLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGY 116
Cdd:TIGR03516  77 QKDTGEGTTPEFGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYGD 156

                  ....
gi 147899811  117 PPSI 120
Cdd:TIGR03516 157 QNKI 160
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-132 3.85e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 249719  Cd Length: 94  Bit Score: 127.74  E-value: 3.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811   42 CTETAVMGDTIHLHYTGRLEDGRIIDSSLSRD-PLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGY-PPS 119
Cdd:pfam00254   1 GPRKAKKGDTVTVHYTGKLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLLGMKVGEKRKLTIPPELAYGEEGLaGGV 80
                          90
                  ....*....|...
gi 147899811  120 IPGDAVLQFETEV 132
Cdd:pfam00254  81 IPPNATLVFEVEL 93
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
54-113 7.76e-08

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


Pssm-ID: 237908  Cd Length: 156  Bit Score: 47.78  E-value: 7.76e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 147899811  54 LHYTGRLEDGRIIDSSLSR-DPLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGK 113
Cdd:PRK15095  13 VHFTLKLDDGSTAESTRNNgKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
PRK10737 PRK10737
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
52-113 2.83e-05

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


Pssm-ID: 236748  Cd Length: 196  Bit Score: 41.47  E-value: 2.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 147899811  52 IHLHYTGRLEDGRIIDSSLSRDPLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGK 113
Cdd:PRK10737   9 VSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQ 70
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
15-134 1.03e-29

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


Pssm-ID: 223619 [Multi-domain]  Cd Length: 205  Bit Score: 109.04  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811  15 TLRAETPEEDSENVTE--LVIETVEKPDSctETAVMGDTIHLHYTGRLEDGRIIDSSLSRD-PLVVELGkkQVIPGLETS 91
Cdd:COG0545   85 AFLEKNAKEKGVKTLPsgLQYKVLKAGDG--AAPKKGDTVTVHYTGTLIDGTVFDSSYDRGqPAEFPLG--GVIPGWDEG 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 147899811  92 LVGMCVGEKRKVVIPPHLAYGKKGYPPSIPGDAVLQFETEVMA 134
Cdd:COG0545  161 LQGMKVGGKRKLTIPPELAYGERGVPGVIPPNSTLVFEVELLD 203
SlpA COG1047
FKBP-type peptidyl-prolyl cis-trans isomerase 2 [Posttranslational modification, protein ...
49-112 7.57e-18

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


Pssm-ID: 223976 [Multi-domain]  Cd Length: 174  Bit Score: 76.52  E-value: 7.57e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 147899811  49 GDTIHLHYTGRLEDGRIIDSSLSRD-PLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYG 112
Cdd:COG1047    6 GDVVSLHYTLKVEDGEVVDTTDENYgPLTFIVGAGQLIPGLEEALLGKEVGEEFTVEIPPEDAFG 70
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
50-133 1.68e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 70.21  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811  50 DTIHLHYTGRLEDGRIIDSSLSR-DPlvVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGYPPSIPGDAVLQF 128
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARgEP--AEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198

                 ....*
gi 147899811 129 ETEVM 133
Cdd:PRK11570 199 EVELL 203
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
36-140 2.63e-15

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 70.18  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811  36 VEKPDScTETAVMGDTIHLHYTGRLEDGRIIDSSLSR-DPLVVELgkKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKK 114
Cdd:PRK10902 152 VEKEGT-GEAPKDSDTVVVNYKGTLIDGKEFDNSYTRgEPLSFRL--DGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKA 228
                         90       100
                 ....*....|....*....|....*.
gi 147899811 115 GYpPSIPGDAVLQFETEVMALfKPTP 140
Cdd:PRK10902 229 GV-PGIPANSTLVFDVELLDV-KPAP 252
ppisom_GldI TIGR03516
peptidyl-prolyl isomerase, gliding motility-associated; Members of this protein family are ...
37-120 9.15e-07

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: 45.14  E-value: 9.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811   37 EKPDSCTETAVMGDTIHLHYTGRLEDGRIIDSSLSRDPLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGKKGY 116
Cdd:TIGR03516  77 QKDTGEGTTPEFGDLVTFEYDIRALDGDVIYSEEELGPQTYKVDQQDLFSGLRDGLKLMKEGETATFLFPSHKAYGYYGD 156

                  ....
gi 147899811  117 PPSI 120
Cdd:TIGR03516 157 QNKI 160
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
33-106 1.12e-05

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


Pssm-ID: 223618 [Multi-domain]  Cd Length: 441  Bit Score: 43.04  E-value: 1.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 147899811  33 IETVEKPdsctetAVMGDTIHLHYTGrLEDGRIIDSsLSRDPLVVELGKKQVIPGLETSLVGMCVGEKR--KVVIP 106
Cdd:COG0544  151 LEPVEGA------AENGDRVTIDFEG-SVDGEEFEG-GKAENFSLELGSGRFIPGFEDQLVGMKAGEEKdiKVTFP 218
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
34-114 1.65e-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: 42.54  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147899811   34 ETVEKpdsctETAVMGDTIHLHYTGrLEDGRIIDSSlSRDPLVVELGKKQVIPGLETSLVGMCVGEKRKVVIPPHLAYGK 113
Cdd:TIGR00115 142 VPVER-----GAAEKGDRVTIDFEG-FIDGEAFEGG-KAENFSLELGSGQFIPGFEEQLVGMKAGEEKEIKVTFPEDYHA 214

                  .
gi 147899811  114 K 114
Cdd:TIGR00115 215 E 215
tig PRK01490
trigger factor; Provisional
33-103 1.77e-03

trigger factor; Provisional


Pssm-ID: 234956 [Multi-domain]  Cd Length: 435  Bit Score: 36.68  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 147899811  33 IETVEKPdsctetAVMGDTIHLHYTGRLeDGRIIDSSlSRDPLVVELGKKQVIPGLETSLVGMCVGEKRKV 103
Cdd:PRK01490 151 LVPVERP------AENGDRVTIDFVGSI-DGEEFEGG-KAEDFSLELGSGRFIPGFEEQLVGMKAGEEKTI 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
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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