NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|729042251|ref|NP_001289889|]
View 

AH receptor-interacting protein isoform 3 [Homo sapiens]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 139723)

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 super family cl19519
FKBP-type peptidyl-prolyl cis-trans isomerase;
29-90 6.24e-10

FKBP-type peptidyl-prolyl cis-trans isomerase;


The actual alignment was detected with superfamily member pfam00254:

Pssm-ID: 473184  Cd Length: 94  Bit Score: 54.90  E-value: 6.24e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729042251   29 QDGTKATFHYRTlhSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLC 90
Cdd:pfam00254   6 KKGDRVTVHYTG--TLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTI 65
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
29-90 6.24e-10

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 54.90  E-value: 6.24e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729042251   29 QDGTKATFHYRTlhSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLC 90
Cdd:pfam00254   6 KKGDRVTVHYTG--TLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTI 65
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 13-90 1.89e-07

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 48.25  E-value: 1.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729042251  13 IQKRVIQEGRGELPdfQDGTKATFHYRTLHSDdeGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLC 90
Cdd:COG0545    1 LQYKVLKEGTGAKP--KAGDTVTVHYTGTLLD--GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVI 74
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 10-61 7.58e-04

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 39.78  E-value: 7.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 729042251  10 EDGIQKRVIQEGRGELPDFQDGTKATFHYRTLhsddEGTVLDDSRARGKPME 61
Cdd:PRK11570 101 ESGLQFRVLTQGEGAIPARTDRVRVHYTGKLI----DGTVFDSSVARGEPAE 148
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
29-90 6.24e-10

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 54.90  E-value: 6.24e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729042251   29 QDGTKATFHYRTlhSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLC 90
Cdd:pfam00254   6 KKGDRVTVHYTG--TLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTI 65
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 13-90 1.89e-07

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 48.25  E-value: 1.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729042251  13 IQKRVIQEGRGELPdfQDGTKATFHYRTLHSDdeGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLC 90
Cdd:COG0545    1 LQYKVLKEGTGAKP--KAGDTVTVHYTGTLLD--GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVI 74
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 10-61 7.58e-04

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 39.78  E-value: 7.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 729042251  10 EDGIQKRVIQEGRGELPDFQDGTKATFHYRTLhsddEGTVLDDSRARGKPME 61
Cdd:PRK11570 101 ESGLQFRVLTQGEGAIPARTDRVRVHYTGKLI----DGTVFDSSVARGEPAE 148
 
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