NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15240623|ref|NP_196845|]
View 

FKBP-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11425492)

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
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
119-253 8.50e-23

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 89.47  E-value: 8.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623 119 LQYKDLRVGTGPIAKKGDKVVVDWDGYTIGyyGRIFEARNktkggsfegDDKEFFKFTLGSNEVIPAFEEAVSGMALGGI 198
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLD--GTVFDSSY---------DRGEPATFPLGVGQVIPGWDEGLQGMKVGGK 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15240623 199 RRIIVPPELGYpdndynksGPRPmtfsgqraldfvlrNQGLI--DKTLLFDVELLKI 253
Cdd:COG0545  70 RRLVIPPELAY--------GERG--------------AGGVIppNSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
119-253 8.50e-23

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 89.47  E-value: 8.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623 119 LQYKDLRVGTGPIAKKGDKVVVDWDGYTIGyyGRIFEARNktkggsfegDDKEFFKFTLGSNEVIPAFEEAVSGMALGGI 198
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLD--GTVFDSSY---------DRGEPATFPLGVGQVIPGWDEGLQGMKVGGK 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15240623 199 RRIIVPPELGYpdndynksGPRPmtfsgqraldfvlrNQGLI--DKTLLFDVELLKI 253
Cdd:COG0545  70 RRLVIPPELAY--------GERG--------------AGGVIppNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
132-251 2.46e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 85.33  E-value: 2.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   132 AKKGDKVVVDWDGYTIGyyGRIFEarnktkgGSFegDDKEFFKFTLGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPD 211
Cdd:pfam00254   5 AKKGDRVTVHYTGTLED--GTVFD-------SSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15240623   212 NDYNKSGPRPmtfsgqraldfvlrnqgliDKTLLFDVELL 251
Cdd:pfam00254  74 EGLAGPVIPP-------------------NATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
86-255 1.87e-10

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 59.78  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   86 ASASQFADMPALKGKDYGKTKMKYPDYTETQSGLQYKDLRVGTGPIAKKGDKVVVDWDGYTIGyyGRIFEarNKTKGGsf 165
Cdd:PRK10902 115 AKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLID--GKEFD--NSYTRG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623  166 egddkEFFKFTLGSneVIPAFEEAVSGMALGGIRRIIVPPELGYpdndynksgprpmtfsGQRALDFVLRNQglidkTLL 245
Cdd:PRK10902 189 -----EPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAY----------------GKAGVPGIPANS-----TLV 240
                        170
                 ....*....|
gi 15240623  246 FDVELLKIVP 255
Cdd:PRK10902 241 FDVELLDVKP 250
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
132-214 3.26e-07

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: 50.63  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   132 AKKGDKVVVDWDGYTigyygrifearnktKGGSFEGDDKEFFKFTLGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPD 211
Cdd:TIGR00115 149 AEKGDRVTIDFEGFI--------------DGEAFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEIKVTFPEDYHA 214

                  ...
gi 15240623   212 NDY 214
Cdd:TIGR00115 215 EEL 217
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
119-253 8.50e-23

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 89.47  E-value: 8.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623 119 LQYKDLRVGTGPIAKKGDKVVVDWDGYTIGyyGRIFEARNktkggsfegDDKEFFKFTLGSNEVIPAFEEAVSGMALGGI 198
Cdd:COG0545   1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLD--GTVFDSSY---------DRGEPATFPLGVGQVIPGWDEGLQGMKVGGK 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15240623 199 RRIIVPPELGYpdndynksGPRPmtfsgqraldfvlrNQGLI--DKTLLFDVELLKI 253
Cdd:COG0545  70 RRLVIPPELAY--------GERG--------------AGGVIppNSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
132-251 2.46e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 85.33  E-value: 2.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   132 AKKGDKVVVDWDGYTIGyyGRIFEarnktkgGSFegDDKEFFKFTLGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPD 211
Cdd:pfam00254   5 AKKGDRVTVHYTGTLED--GTVFD-------SSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15240623   212 NDYNKSGPRPmtfsgqraldfvlrnqgliDKTLLFDVELL 251
Cdd:pfam00254  74 EGLAGPVIPP-------------------NATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
86-255 1.87e-10

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 59.78  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   86 ASASQFADMPALKGKDYGKTKMKYPDYTETQSGLQYKDLRVGTGPIAKKGDKVVVDWDGYTIGyyGRIFEarNKTKGGsf 165
Cdd:PRK10902 115 AKMEKDAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLID--GKEFD--NSYTRG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623  166 egddkEFFKFTLGSneVIPAFEEAVSGMALGGIRRIIVPPELGYpdndynksgprpmtfsGQRALDFVLRNQglidkTLL 245
Cdd:PRK10902 189 -----EPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAY----------------GKAGVPGIPANS-----TLV 240
                        170
                 ....*....|
gi 15240623  246 FDVELLKIVP 255
Cdd:PRK10902 241 FDVELLDVKP 250
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
96-254 1.05e-08

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 53.65  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   96 ALKGKDYGKTKMKYPDYTETQSGLQYKDLRVGTGPIAKKGDKVVVDWDGYTIGyyGRIFEARNKtkggsfEGDDKEFfkf 175
Cdd:PRK11570  81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLID--GTVFDSSVA------RGEPAEF--- 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240623  176 tlGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPDNDYNKSGPrpmTFSgqraldfvlrnqglidkTLLFDVELLKIV 254
Cdd:PRK11570 150 --PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIP---PFS-----------------TLVFEVELLEIL 206
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
132-253 3.13e-08

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 51.26  E-value: 3.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623 132 AKKGDKVVVDWDGYTIGyyGRIFEArnktkggSFEGDDkefFKFTLGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPd 211
Cdd:COG1047   1 IEKGDVVTLHYTLKLED--GEVFDS-------TFEGEP---LEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG- 67
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240623 212 nDYNKSG--------------PRP-MTFSGQRA------------------LDFvlrNQGLIDKTLLFDVELLKI 253
Cdd:COG1047  68 -ERDPELvqtvpreqfpedeeLEVgMQVEFQTPdgqevpgtvtevdddtvtVDF---NHPLAGKTLTFDVEVVEV 138
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
132-214 3.26e-07

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: 50.63  E-value: 3.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240623   132 AKKGDKVVVDWDGYTigyygrifearnktKGGSFEGDDKEFFKFTLGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPD 211
Cdd:TIGR00115 149 AEKGDRVTIDFEGFI--------------DGEAFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEIKVTFPEDYHA 214

                  ...
gi 15240623   212 NDY 214
Cdd:TIGR00115 215 EEL 217
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
132-196 1.04e-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: 45.89  E-value: 1.04e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240623 132 AKKGDKVVVDWDGyTIGyyGRIFEarnktkGGSFEGddkefFKFTLGSNEVIPAFEEAVSGMALG 196
Cdd:COG0544 158 AEEGDRVTIDFEG-TID--GEEFE------GGKAED-----YSLELGSGSFIPGFEEQLVGMKAG 208
 
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