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Conserved domains on  [gi|1958784388|ref|XP_038968731|]
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peptidyl-prolyl cis-trans isomerase FKBP1B isoform X5 [Rattus norvegicus]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446594)

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|GO:0000413|GO:0061077
PubMed:  27664121
SCOP:  4001062

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-91 3.18e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 82.24  E-value: 3.18e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958784388 13 GRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQASLeswGSERCLRSPDPQAAGGQGL 91
Cdd:pfam00254  1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKV---GEKRKLTIPPELAYGEEGL 76
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-91 3.18e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 82.24  E-value: 3.18e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958784388 13 GRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQASLeswGSERCLRSPDPQAAGGQGL 91
Cdd:pfam00254  1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKV---GEKRKLTIPPELAYGEEGL 76
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 3-63 4.29e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 82.15  E-value: 4.29e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958784388   3 VEIETISPGDGRTfPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEG 60
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 2-90 8.96e-05

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 39.01  E-value: 8.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784388   2 GVEIETISPGDGrTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKqeVIKGFEEGaaqASLESWGSERCLRSP 81
Cdd:PRK11570  103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEA---LTLMPVGSKWELTIP 176


                  ....*....
gi 1958784388  82 DPQAAGGQG 90
Cdd:PRK11570  177 HELAYGERG 185
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
13-91 3.18e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 82.24  E-value: 3.18e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958784388 13 GRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQASLeswGSERCLRSPDPQAAGGQGL 91
Cdd:pfam00254  1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKV---GEKRKLTIPPELAYGEEGL 76
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 3-63 4.29e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 82.15  E-value: 4.29e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958784388   3 VEIETISPGDGRTfPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEG 63
Cdd:COG0545     1 LQYKVLKEGTGAK-PKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEG 60
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 18-62 1.29e-08

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 48.56  E-value: 1.29e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958784388  18 KKGQICVVHYTGMLQNGKKFDSSRDRnKPFKFRIGKQEVIKGFEE 62
Cdd:COG1047     2 EKGDVVTLHYTLKLEDGEVFDSTFEG-EPLEFLHGAGQLIPGLEE 45
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 2-90 8.96e-05

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 39.01  E-value: 8.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784388   2 GVEIETISPGDGrTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKqeVIKGFEEGaaqASLESWGSERCLRSP 81
Cdd:PRK11570  103 GLQFRVLTQGEG-AIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEA---LTLMPVGSKWELTIP 176


                  ....*....
gi 1958784388  82 DPQAAGGQG 90
Cdd:PRK11570  177 HELAYGERG 185
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 25-52 1.85e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 35.07  E-value: 1.85e-03
                          10        20
                  ....*....|....*....|....*...
gi 1958784388  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.
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