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Conserved domains on  [gi|7305061|ref|NP_038930|]
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peptidyl-prolyl cis-trans isomerase FKBP3 [Mus musculus]

Protein Classification

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;
124-221 1.92e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.77  E-value: 1.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061    124 FPKKGDVVHCWYTGTLPDGTVFDTNiqtsskkKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQ 203
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSS-------YDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL 76

                          90
                  ....*....|....*...
gi 7305061    204 PDAKIPPNTKLIFEVELV 221
Cdd:pfam00254  77 AGPVIPPNATLVFEVELL 94
BTHB_FKBP25 cd21063
basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and ...
 7-73 4.63e-34

basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and similar proteins; FKBP25, also called 25 kDa FKBP, FK506-binding protein 3 (FKBP-3), immunophilin FKBP-25, rapamycin-selective 25 kDa immunophilin or rotamase, acts as a peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. FKBP25 binds both FK506 and rapamycin, and thus belongs to a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways.


:

Pssm-ID: 439139  Cd Length: 67  Bit Score: 116.55  E-value: 4.63e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305061    7 QRAWTVEQLRSEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESKRFK 73
Cdd:cd21063   1 ERPWTEEQLASDAVSKKDLIEFLQENASNSFLAEHKLLGKLKNVAKTAKKDQLVEAYNQLFESKAFK 67
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
124-221 1.92e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.77  E-value: 1.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061    124 FPKKGDVVHCWYTGTLPDGTVFDTNiqtsskkKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQ 203
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSS-------YDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL 76

                          90
                  ....*....|....*...
gi 7305061    204 PDAKIPPNTKLIFEVELV 221
Cdd:pfam00254  77 AGPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 115-223 1.26e-36

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 124.14  E-value: 1.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061  115 ILKKGDkTNFPKKGDVVHCWYTGTLPDGTVFDTNIQTSskkkknaKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEP 194
Cdd:COG0545   5 VLKEGT-GAKPKAGDTVTVHYTGTLLDGTVFDSSYDRG-------EPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPP 76

                        90       100
                ....*....|....*....|....*....
gi 7305061  195 EWAYGKKGQPDaKIPPNTKLIFEVELVDI 223
Cdd:COG0545  77 ELAYGERGAGG-VIPPNSTLVFEVELLDV 104
BTHB_FKBP25 cd21063
basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and ...
 7-73 4.63e-34

basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and similar proteins; FKBP25, also called 25 kDa FKBP, FK506-binding protein 3 (FKBP-3), immunophilin FKBP-25, rapamycin-selective 25 kDa immunophilin or rotamase, acts as a peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. FKBP25 binds both FK506 and rapamycin, and thus belongs to a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways.


Pssm-ID: 439139  Cd Length: 67  Bit Score: 116.55  E-value: 4.63e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305061    7 QRAWTVEQLRSEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESKRFK 73
Cdd:cd21063   1 ERPWTEEQLASDAVSKKDLIEFLQENASNSFLAEHKLLGKLKNVAKTAKKDQLVEAYNQLFESKAFK 67
BTHB pfam18410
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ...
 6-76 9.69e-33

Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it has been suggested to have a role in regulating the association state of nucleosomes by interacting with nucleolin. Moreover, this basic domain in FKBP25 forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


Pssm-ID: 465755  Cd Length: 72  Bit Score: 113.24  E-value: 9.69e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305061      6 PQRAWTVEQLRSEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESKRFKGTE 76
Cdd:pfam18410   1 PERQWTEEQLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKRFKGSG 71
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 114-223 3.04e-20

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 84.85  E-value: 3.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061   114 SILKKGDKTnFPKKGDVVHCWYTGTLPDGTVFDTNIQtsskkkkNAKPLSFKVGvgKVIRGWDEALLTMSKGEKARLEIE 193
Cdd:PRK11570 107 RVLTQGEGA-IPARTDRVRVHYTGKLIDGTVFDSSVA-------RGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIP 176

                         90       100       110
                 ....*....|....*....|....*....|
gi 7305061   194 PEWAYGKKGqPDAKIPPNTKLIFEVELVDI 223
Cdd:PRK11570 177 HELAYGERG-AGASIPPFSTLVFEVELLEI 205
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
124-221 1.92e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.77  E-value: 1.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061    124 FPKKGDVVHCWYTGTLPDGTVFDTNiqtsskkKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQ 203
Cdd:pfam00254   4 KAKKGDRVTVHYTGTLEDGTVFDSS-------YDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGL 76

                          90
                  ....*....|....*...
gi 7305061    204 PDAKIPPNTKLIFEVELV 221
Cdd:pfam00254  77 AGPVIPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 115-223 1.26e-36

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 124.14  E-value: 1.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061  115 ILKKGDkTNFPKKGDVVHCWYTGTLPDGTVFDTNIQTSskkkknaKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEP 194
Cdd:COG0545   5 VLKEGT-GAKPKAGDTVTVHYTGTLLDGTVFDSSYDRG-------EPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPP 76

                        90       100
                ....*....|....*....|....*....
gi 7305061  195 EWAYGKKGQPDaKIPPNTKLIFEVELVDI 223
Cdd:COG0545  77 ELAYGERGAGG-VIPPNSTLVFEVELLDV 104
BTHB_FKBP25 cd21063
basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and ...
 7-73 4.63e-34

basic tilted helix bundle (BTHB) domain found in 25 kDa FK506-binding protein (FKBP25) and similar proteins; FKBP25, also called 25 kDa FKBP, FK506-binding protein 3 (FKBP-3), immunophilin FKBP-25, rapamycin-selective 25 kDa immunophilin or rotamase, acts as a peptidyl-prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. FKBP25 binds both FK506 and rapamycin, and thus belongs to a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways.


Pssm-ID: 439139  Cd Length: 67  Bit Score: 116.55  E-value: 4.63e-34
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305061    7 QRAWTVEQLRSEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESKRFK 73
Cdd:cd21063   1 ERPWTEEQLASDAVSKKDLIEFLQENASNSFLAEHKLLGKLKNVAKTAKKDQLVEAYNQLFESKAFK 67
BTHB pfam18410
Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such ...
 6-76 9.69e-33

Basic tilted helix bundle domain; This domain is found on the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it has been suggested to have a role in regulating the association state of nucleosomes by interacting with nucleolin. Moreover, this basic domain in FKBP25 forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


Pssm-ID: 465755  Cd Length: 72  Bit Score: 113.24  E-value: 9.69e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305061      6 PQRAWTVEQLRSEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESKRFKGTE 76
Cdd:pfam18410   1 PERQWTEEQLLSDALPKKDIIKFLQDNASLSFLKEHKLNGALKNVAKTAKKDQLAEAYNKLFESKRFKGSG 71
BTHB cd21035
basic tilted helix bundle (BTHB) domain; BTHB domain is found in the N-terminal region of ...
 9-68 4.35e-24

basic tilted helix bundle (BTHB) domain; BTHB domain is found in the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it may have a role in regulating the association state of nucleosomes by interacting with nucleolin. This basic domain in FKBP25 also forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


Pssm-ID: 439137  Cd Length: 64  Bit Score: 90.64  E-value: 4.35e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7305061    9 AWTVEQLRSE----QLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFE 68
Cdd:cd21035   1 VWTKQFDEAYtasdNLPKKDVVDFLQKYADNSFLREHKLNGSAKSVLKNRNKDQLVEAYNKVFE 64
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 114-223 3.04e-20

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 84.85  E-value: 3.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061   114 SILKKGDKTnFPKKGDVVHCWYTGTLPDGTVFDTNIQtsskkkkNAKPLSFKVGvgKVIRGWDEALLTMSKGEKARLEIE 193
Cdd:PRK11570 107 RVLTQGEGA-IPARTDRVRVHYTGKLIDGTVFDSSVA-------RGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIP 176

                         90       100       110
                 ....*....|....*....|....*....|
gi 7305061   194 PEWAYGKKGqPDAKIPPNTKLIFEVELVDI 223
Cdd:PRK11570 177 HELAYGERG-AGASIPPFSTLVFEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 125-223 7.46e-18

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 79.81  E-value: 7.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061   125 PKKGDVVHCWYTGTLPDGTVFDtniqtSSKKKKnaKPLSFKVGvgKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQP 204
Cdd:PRK10902 161 PKDSDTVVVNYKGTLIDGKEFD-----NSYTRG--EPLSFRLD--GVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231

                         90
                 ....*....|....*....
gi 7305061   205 daKIPPNTKLIFEVELVDI 223
Cdd:PRK10902 232 --GIPANSTLVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 126-220 1.19e-15

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 70.90  E-value: 1.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305061  126 KKGDVVHCWYTGTLPDGTVFDTNiqtsskkkKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGkkgqpd 205
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDST--------FEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG------ 67

                        90
                ....*....|....*
gi 7305061  206 akiPPNTKLIFEVEL 220
Cdd:COG1047  68 ---ERDPELVQTVPR 79
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 10-70 4.49e-10

basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and similar proteins; HectD1, also called E3 ligase for inhibin receptor (EULIR), is a Hect-type E3 ubiquitin transferase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. HectD1 is required for development of head mesenchyme and neural tube closure.


Pssm-ID: 439138  Cd Length: 66  Bit Score: 53.83  E-value: 4.49e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305061   10 WTVEQLR----SEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESK 70
Cdd:cd21062   2 WTVEYVEqslgTGELPKSDVITYLQKNADEAFLRRWKLTGTAKNIRKNRNCSQLIAAYKEFCEHG 66
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 131-205 3.77e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 36.61  E-value: 3.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305061   131 VHcwYTGTLPDGTVFDTNiqtsskkKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKgQPD 205
Cdd:PRK15095  13 VH--FTLKLDDGSTAEST-------RNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP-SPD 77
 
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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