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Conserved domains on  [gi|1958775585|ref|XP_038965540|]
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peptidyl-prolyl cis-trans isomerase E isoform X2 [Rattus norvegicus]

Protein Classification

peptidyl-prolyl cis-trans isomerase E( domain architecture ID 10349398)

peptidyl-prolyl cis-trans isomerase E catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins, and is involved in pre-mRNA splicing as a component of the spliceosome

CATH:  2.40.100.10|3.30.70.330
EC:  5.2.1.8
Gene Ontology:  GO:0003723|GO:0000398|GO:0003755|GO:0006457|GO:0000413
PubMed:  22278943|18515081|14731520|15998457|15353287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 74-232 4.00e-111

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.


:

Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 315.74  E-value: 4.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  74 PQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKG-----FGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSI 148
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 149 YGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 228
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 1958775585 229 ADCG 232
Cdd:cd01926   161 ADCG 164
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 1-16 2.05e-05

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


The actual alignment was detected with superfamily member cd12347:

Pssm-ID: 473069 [Multi-domain]  Cd Length: 75  Bit Score: 41.44  E-value: 2.05e-05
                          10
                  ....*....|....*.
gi 1958775585   1 MNESELFGRTIRVNLA 16
Cdd:cd12347    60 MNESELFGRTIRVNLA 75
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 74-232 4.00e-111

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 315.74  E-value: 4.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  74 PQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKG-----FGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSI 148
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 149 YGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 228
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 1958775585 229 ADCG 232
Cdd:cd01926   161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 72-233 1.22e-92

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 269.79  E-value: 1.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  72 SNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHE------KGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGG 145
Cdd:PTZ00060   14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 146 KSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQK 225
Cdd:PTZ00060   94 ESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKP 173


                  ....*...
gi 1958775585 226 VIIADCGE 233
Cdd:PTZ00060  174 VVVTDCGE 181
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 87-233 4.47e-55

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 173.21  E-value: 4.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  87 AGRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTnhnGTGGKSIYGKKFDDENFI--LKHtG 164
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-K 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775585 165 PGLLSMANSG--PNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVIIADCGE 233
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 69-228 2.31e-48

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 156.48  E-value: 2.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  69 KARSNPQVYMDIkignkPAGRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKsi 148
Cdd:COG0652     2 KAAPNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 149 yGKKFDDENFI-LKHTgPGLLSMANS-GPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDG-KPKQK 225
Cdd:COG0652    71 -GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEP 148


                  ...
gi 1958775585 226 VII 228
Cdd:COG0652   149 VVI 151
RRM_PPIE cd12347
RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This ...
 1-16 2.05e-05

RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This subfamily corresponds to the RRM of Cyp33, also termed peptidyl-prolyl cis-trans isomerase E (PPIase E), or cyclophilin E, or rotamase E. Cyp33 is a nuclear RNA-binding cyclophilin with an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal PPIase domain. Cyp33 possesses RNA-binding activity and preferentially binds to polyribonucleotide polyA and polyU, but hardly to polyG and polyC. It binds specifically to mRNA, which can stimulate its PPIase activity. Moreover, Cyp33 interacts with the third plant homeodomain (PHD3) zinc finger cassette of the mixed lineage leukemia (MLL) proto-oncoprotein and a poly-A RNA sequence through its RRM domain. It further mediates downregulation of the expression of MLL target genes HOXC8, HOXA9, CDKN1B, and C-MYC, in a proline isomerase-dependent manner. Cyp33 also possesses a PPIase activity that catalyzes cis-trans isomerization of the peptide bond preceding a proline, which has been implicated in the stimulation of folding and conformational changes in folded and unfolded proteins. The PPIase activity can be inhibited by the immunosuppressive drug cyclosporin A.


Pssm-ID: 409783 [Multi-domain]  Cd Length: 75  Bit Score: 41.44  E-value: 2.05e-05
                          10
                  ....*....|....*.
gi 1958775585   1 MNESELFGRTIRVNLA 16
Cdd:cd12347    60 MNESELFGRTIRVNLA 75
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 74-232 4.00e-111

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 315.74  E-value: 4.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  74 PQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKG-----FGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSI 148
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 149 YGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 228
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 1958775585 229 ADCG 232
Cdd:cd01926   161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 72-233 1.22e-92

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 269.79  E-value: 1.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  72 SNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHE------KGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGG 145
Cdd:PTZ00060   14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 146 KSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQK 225
Cdd:PTZ00060   94 ESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKP 173


                  ....*...
gi 1958775585 226 VIIADCGE 233
Cdd:PTZ00060  174 VVVTDCGE 181
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 72-233 1.45e-79

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 236.66  E-value: 1.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  72 SNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHE---KGF--GFKGSSFHRIIPQFMCQGGDFTNHNGTGGK 146
Cdd:PLN03149   17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 147 SIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEIT-DGLDVLRQIE-AQGSKDGKPKQ 224
Cdd:PLN03149   97 SIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIEnVATGPNNRPKL 176


                  ....*....
gi 1958775585 225 KVIIADCGE 233
Cdd:PLN03149  177 ACVISECGE 185
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 88-230 6.80e-57

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 177.84  E-value: 6.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNHNGtgGKSIYGKKFDDENFILK-HTGPG 166
Cdd:cd00317     7 GRIVIELYGDEAPKTVENFLSLA--RGGF-YDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFPLKyHHRRG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958775585 167 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQG-SKDGKPKQKVIIAD 230
Cdd:cd00317    82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 87-233 4.47e-55

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 173.21  E-value: 4.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  87 AGRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTnhnGTGGKSIYGKKFDDENFI--LKHtG 164
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-K 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775585 165 PGLLSMANSG--PNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVIIADCGE 233
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 88-228 1.58e-48

cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a WD40 domain. This group consists of several hypothetical and putative eukaryotic and bacterial proteins which have a cyclophilin domain and a WD40 domain. Function of the protein is not known.


Pssm-ID: 238908 [Multi-domain]  Cd Length: 148  Bit Score: 156.47  E-value: 1.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFrclCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGPG 166
Cdd:cd01927     7 GDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRPY 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958775585 167 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIE-AQGSKDGKPKQKVII 228
Cdd:cd01927    83 TLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIEnVKTDKNDRPYEDIKI 145
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 69-228 2.31e-48

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 156.48  E-value: 2.31e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  69 KARSNPQVYMDIkignkPAGRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKsi 148
Cdd:COG0652     2 KAAPNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 149 yGKKFDDENFI-LKHTgPGLLSMANS-GPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDG-KPKQK 225
Cdd:COG0652    71 -GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEP 148


                  ...
gi 1958775585 226 VII 228
Cdd:COG0652   149 VVI 151
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 88-228 1.68e-45

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling.


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 148.84  E-value: 1.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGPG 166
Cdd:cd01922     7 GEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGAG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958775585 167 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 228
Cdd:cd01922    83 ILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 88-230 1.18e-43

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 144.48  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGPG 166
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGRG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958775585 167 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIE-AQGSKDGKPKQKVIIAD 230
Cdd:cd01923    85 VLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMEnVPDPGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 88-230 4.19e-43

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 142.96  E-value: 4.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDENF-ILKHTGPG 166
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALCA--SGY-YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFReTLKHDSRG 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958775585 167 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEA-QGSKDGKPKQKVIIAD 230
Cdd:cd01928    86 VVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKlPVDKKYRPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 87-222 2.52e-36

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 125.93  E-value: 2.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  87 AGRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGP 165
Cdd:cd01925    14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958775585 166 GLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEIT-DGL-DVLRQIEAQGSKDGKP 222
Cdd:cd01925    90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIyNLLKLAEVETDKDERP 148
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 88-228 5.49e-27

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 101.65  E-value: 5.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFRCLCtheKGFGFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKK-------FDDE-NFI 159
Cdd:cd01921     7 GDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLygrqarfFEPEiLPL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775585 160 LKHTGPGLLSMANSGPNTNGSQFFLT-CDKTDWLDGKHVVFGEITDGLDVLRQI-EAQGSKDGKPKQKVII 228
Cdd:cd01921    83 LKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 75-232 1.45e-23

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 94.94  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  75 QVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGF----GFK----GSSFHRIIPQF-MCQGGDFTNHNgtgg 145
Cdd:PTZ00221   54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdtntGVKldylYTPVHHVDRNNnIIVLGELDSFN---- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 146 KSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKD-GKPKQ 224
Cdd:PTZ00221  130 VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDvGRPLL 209


                  ....*...
gi 1958775585 225 KVIIADCG 232
Cdd:PTZ00221  210 PVTVSFCG 217
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 87-230 7.27e-16

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 72.09  E-value: 7.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  87 AGRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNHngtggksiyGKKFDDENFILKHTGPG 166
Cdd:cd01920     6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPD---------LAQKETLKPIKNEAGNG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 167 L------LSMANSG-PNTNGSQFFLTCDKTDWLD-----GKHVVFGEITDGLDVLRQIE-----AQGSKDGKPKQKVIIA 229
Cdd:cd01920    74 LsntrgtIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAgvetySFGSYQDVPVQDVIIE 153


                  .
gi 1958775585 230 D 230
Cdd:cd01920   154 S 154
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 88-214 5.01e-15

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 70.55  E-value: 5.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  88 GRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNHN------GTG--------------GKS 147
Cdd:cd01924     7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNpgfpdpETGksrtipleikpegqKQP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 148 IYGKKF-----DDENFILKHTGPGLLSMANS--GPNTNGSQFF-------LTCDKTDWLDGKHVVFGEITDGLDVLRQIE 213
Cdd:cd01924    84 VYGKTLeeagrYDEQPVLPFNAFGAIAMARTefDPNSASSQFFfllkdneLTPSRNNVLDGRYAVFGYVTDGLDILRELK 163


                  .
gi 1958775585 214 A 214
Cdd:cd01924   164 V 164
PRK10903 PRK10903
peptidylprolyl isomerase A;
65-226 3.14e-13

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 66.02  E-value: 3.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  65 PAAKKARSNPQVYMDIKIGNkpagrIQMLLRSDVVPMTAENFrcLCTHEKGFgFKGSSFHRIIPQFMCQGGDFTnhngtg 144
Cdd:PRK10903   20 PAALAAKGDPHVLLTTSAGN-----IELELNSQKAPVSVKNF--VDYVNSGF-YNNTTFHRVIPGFMIQGGGFT------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585 145 gksiygkkfddENFILKHTGPGLLSMANSG-PNTNG--------------SQFFLTCDKTDWLD-GK----HVVFGEITD 204
Cdd:PRK10903   86 -----------EQMQQKKPNPPIKNEADNGlRNTRGtiamartadkdsatSQFFINVADNAFLDhGQrdfgYAVFGKVVK 154

                         170       180
                  ....*....|....*....|..
gi 1958775585 205 GLDVLRQIEAQGSKDGKPKQKV 226
Cdd:PRK10903  155 GMDVADKISQVPTHDVGPYQNV 176
PRK10791 PRK10791
peptidylprolyl isomerase B;
96-228 4.59e-11

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 59.47  E-value: 4.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775585  96 SDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFtnHNGTGGKSIYGKKFDDENFILKHTgPGLLSMANSG- 174
Cdd:PRK10791   17 DDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNGLKNT-RGTLAMARTQa 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775585 175 PNTNGSQFFLTCDKTDWLDGK--------HVVFGEITDGLDVLRQIEA-----QGSKDGKPKQKVII 228
Cdd:PRK10791   91 PHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGvatgrSGMHQDVPKEDVII 157
RRM_PPIE cd12347
RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This ...
 1-16 2.05e-05

RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This subfamily corresponds to the RRM of Cyp33, also termed peptidyl-prolyl cis-trans isomerase E (PPIase E), or cyclophilin E, or rotamase E. Cyp33 is a nuclear RNA-binding cyclophilin with an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal PPIase domain. Cyp33 possesses RNA-binding activity and preferentially binds to polyribonucleotide polyA and polyU, but hardly to polyG and polyC. It binds specifically to mRNA, which can stimulate its PPIase activity. Moreover, Cyp33 interacts with the third plant homeodomain (PHD3) zinc finger cassette of the mixed lineage leukemia (MLL) proto-oncoprotein and a poly-A RNA sequence through its RRM domain. It further mediates downregulation of the expression of MLL target genes HOXC8, HOXA9, CDKN1B, and C-MYC, in a proline isomerase-dependent manner. Cyp33 also possesses a PPIase activity that catalyzes cis-trans isomerization of the peptide bond preceding a proline, which has been implicated in the stimulation of folding and conformational changes in folded and unfolded proteins. The PPIase activity can be inhibited by the immunosuppressive drug cyclosporin A.


Pssm-ID: 409783 [Multi-domain]  Cd Length: 75  Bit Score: 41.44  E-value: 2.05e-05
                          10
                  ....*....|....*.
gi 1958775585   1 MNESELFGRTIRVNLA 16
Cdd:cd12347    60 MNESELFGRTIRVNLA 75
 
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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