NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958784385|ref|XP_038968730|]
View 

peptidyl-prolyl cis-trans isomerase FKBP1B isoform X4 [Rattus norvegicus]

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 ...
 3-63 2.17e-22

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 82.92  E-value: 2.17e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958784385   3 VEIETISPGDGRTfPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEG 60
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 3-63 2.17e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 82.92  E-value: 2.17e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958784385   3 VEIETISPGDGRTfPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEG 60
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-63 5.70e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 81.47  E-value: 5.70e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1958784385 13 GRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:pfam00254  1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEG 51
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 2-90 8.20e-05

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 39.01  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784385   2 GVEIETISPGDGrTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKqeVIKGFEEGaaqASLESWGSERCLRSP 81
Cdd:PRK11570  103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEA---LTLMPVGSKWELTIP 176


                  ....*....
gi 1958784385  82 DPQAAGGQG 90
Cdd:PRK11570  177 HELAYGERG 185
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 3-63 2.17e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 82.92  E-value: 2.17e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958784385   3 VEIETISPGDGRTfPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEG 60
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-63 5.70e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 81.47  E-value: 5.70e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1958784385 13 GRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:pfam00254  1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEG 51
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 18-62 1.79e-08

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 48.17  E-value: 1.79e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958784385  18 KKGQICVVHYTGMLQNGKKFDSSRDRnKPFKFRIGKQEVIKGFEE 62
Cdd:COG1047     2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEE 45
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 2-90 8.20e-05

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 39.01  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784385   2 GVEIETISPGDGrTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKqeVIKGFEEGaaqASLESWGSERCLRSP 81
Cdd:PRK11570  103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEA---LTLMPVGSKWELTIP 176


                  ....*....
gi 1958784385  82 DPQAAGGQG 90
Cdd:PRK11570  177 HELAYGERG 185
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 25-52 1.91e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 35.07  E-value: 1.91e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958784385  25 VHYTGMLQNGKKFDSSRDRNKPFKFRIG 52
Cdd:PRK15095   13 VHFTLKLDDGSTAESTRNNGKPALFRLG 40
 
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