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Conserved domains on  [gi|1720357071|ref|XP_030098751|]
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peptidyl-prolyl cis-trans isomerase-like 3 isoform X4 [Mus musculus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 1-105 2.60e-69

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.


The actual alignment was detected with superfamily member cd01928:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 153  Bit Score: 204.21  E-value: 2.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd01928    50 MVQTGDPTGTGKGGESIWGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLD 129

                          90       100
                  ....*....|....*....|....*
gi 1720357071  81 ELEKLPVnEKTYRPLNDVHIKDITI 105
Cdd:cd01928   130 TLEKLPV-DKKYRPLEEIRIKDVTI 153
 
Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-105 2.60e-69

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: 204.21  E-value: 2.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd01928    50 MVQTGDPTGTGKGGESIWGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLD 129

                          90       100
                  ....*....|....*....|....*
gi 1720357071  81 ELEKLPVnEKTYRPLNDVHIKDITI 105
Cdd:cd01928   130 TLEKLPV-DKKYRPLEEIRIKDVTI 153
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-105 5.79e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 140.31  E-value: 5.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSiwaKKFEDEYSEYLKHnVRGVVSMAN-NGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETL 79
Cdd:COG0652    56 MIQGGDPTGTGTGGPG---YTIPDEFDPGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVV 131

                          90       100
                  ....*....|....*....|....*.
gi 1720357071  80 DELEKLPVNEKTyRPLNDVHIKDITI 105
Cdd:COG0652   132 DKIAAGPTDPGD-GPLEPVVIESVTI 156
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 1-105 5.40e-39

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: 127.37  E-value: 5.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIwaKKFEDEYSEYLKHNVRGVVSMANNG--PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLET 78
Cdd:pfam00160  47 MVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDV 124

                          90       100
                  ....*....|....*....|....*..
gi 1720357071  79 LDELEKLPVNEKtyRPLNDVHIKDITI 105
Cdd:pfam00160 125 LEKIEKVPTDGD--RPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-102 3.26e-27

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 98.38  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPT-GTGRGGSSIWAKKFEDEySEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETL 79
Cdd:PTZ00060   79 MCQGGDITnHNGTGGESIYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVV 157

                          90       100
                  ....*....|....*....|...
gi 1720357071  80 DELEKlpVNEKTYRPLNDVHIKD 102
Cdd:PTZ00060  158 RAMEK--EGTQSGYPKKPVVVTD 178
 
Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-105 2.60e-69

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: 204.21  E-value: 2.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd01928    50 MVQTGDPTGTGKGGESIWGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLD 129

                          90       100
                  ....*....|....*....|....*
gi 1720357071  81 ELEKLPVnEKTYRPLNDVHIKDITI 105
Cdd:cd01928   130 TLEKLPV-DKKYRPLEEIRIKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 1-112 1.14e-55

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: 169.90  E-value: 1.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd01923    49 MIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLE 128

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720357071  81 ELEKLPVNeKTYRPLNDVHIKDITIHANPFAQ 112
Cdd:cd01923   129 AMENVPDP-GTDRPKEEIKIEDTSVFVDPFEE 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 1-102 7.59e-45

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: 142.02  E-value: 7.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSsIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd00317    47 MIQGGDPTGTGGGGS-GPGYKFPDENFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVD 125

                          90       100
                  ....*....|....*....|..
gi 1720357071  81 ELEKLPVNEKtYRPLNDVHIKD 102
Cdd:cd00317   126 KIERGDTDEN-GRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-105 5.79e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 140.31  E-value: 5.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSiwaKKFEDEYSEYLKHnVRGVVSMAN-NGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETL 79
Cdd:COG0652    56 MIQGGDPTGTGTGGPG---YTIPDEFDPGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVV 131

                          90       100
                  ....*....|....*....|....*.
gi 1720357071  80 DELEKLPVNEKTyRPLNDVHIKDITI 105
Cdd:COG0652   132 DKIAAGPTDPGD-GPLEPVVIESVTI 156
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 1-103 5.94e-41

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: 132.20  E-value: 5.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd01927    47 MIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQ 126

                          90       100
                  ....*....|....*....|...
gi 1720357071  81 ELEKLPVNeKTYRPLNDVHIKDI 103
Cdd:cd01927   127 RIENVKTD-KNDRPYEDIKIINI 148
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 1-105 5.40e-39

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: 127.37  E-value: 5.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIwaKKFEDEYSEYLKHNVRGVVSMANNG--PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLET 78
Cdd:pfam00160  47 MVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDV 124

                          90       100
                  ....*....|....*....|....*..
gi 1720357071  79 LDELEKLPVNEKtyRPLNDVHIKDITI 105
Cdd:pfam00160 125 LEKIEKVPTDGD--RPVKPVKILSCGV 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 1-100 3.28e-38

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: 125.34  E-value: 3.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLD 80
Cdd:cd01922    47 MIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIE 126

                          90       100
                  ....*....|....*....|
gi 1720357071  81 ELEKlpVNEKTYRPLNDVHI 100
Cdd:cd01922   127 NMVE--VQTQTDRPIDEVKI 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 1-110 2.54e-34

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: 116.30  E-value: 2.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVI-DGLETL 79
Cdd:cd01925    55 IIQGGDPTGTGTGGESIYGEPFKDEFHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNL 134

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720357071  80 DELEKLPVNEKTyRPLNDVHIKDITIHANPF 110
Cdd:cd01925   135 LKLAEVETDKDE-RPVYPPKITSVEVLENPF 164
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 1-102 4.31e-33

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: 112.74  E-value: 4.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPT-GTGRGGSSIWAKKFEDEYSEyLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETL 79
Cdd:cd01926    63 MIQGGDFTrGNGTGGKSIYGEKFPDENFK-LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVV 141

                          90       100
                  ....*....|....*....|...
gi 1720357071  80 DELEKLPVneKTYRPLNDVHIKD 102
Cdd:cd01926   142 KKIENVGS--GNGKPKKKVVIAD 162
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 2-110 1.52e-32

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: 111.66  E-value: 1.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   2 VQTGDPTGTGRGGSSIW-------AKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQ-PHLDMKYTVFGKVI 73
Cdd:cd01921    48 AQTGDPTGTGAGGESIYsqlygrqARFFEPEILPLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVV 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720357071  74 DGLETLDELEKLPVNEKtYRPLNDVHIKDITIHANPF 110
Cdd:cd01921   128 EGFDVLEKINDAIVDDD-GRPLKDIRIKHTHILDDPF 163
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-102 3.26e-27

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 98.38  E-value: 3.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGDPT-GTGRGGSSIWAKKFEDEySEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETL 79
Cdd:PTZ00060   79 MCQGGDITnHNGTGGESIYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVV 157

                          90       100
                  ....*....|....*....|...
gi 1720357071  80 DELEKlpVNEKTYRPLNDVHIKD 102
Cdd:PTZ00060  158 RAMEK--EGTQSGYPKKPVVVTD 178
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 1-83 4.04e-22

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 85.27  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   1 MVQTGD-PTGTGRGGSSIWAKKFEDEySEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVI-DGLET 78
Cdd:PLN03149   81 MIQGGDfLKGDGTGCVSIYGSKFEDE-NFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLV 159


                  ....*
gi 1720357071  79 LDELE 83
Cdd:PLN03149  160 VRKIE 164
PTZ00221 PTZ00221
cyclophilin; Provisional
 31-100 5.62e-16

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 70.67  E-value: 5.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071  31 KHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEkTYRPLNDVHI 100
Cdd:PTZ00221  145 RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDD-VGRPLLPVTV 213
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 33-105 1.84e-10

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: 54.37  E-value: 1.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720357071  33 NVRGVVSMA-NNGPNTNGSQFFITYGKQPHLDMK-----YTVFGKVIDGLETLDELEKLPVNekTYRPLNDVHIKDITI 105
Cdd:cd01920    76 NTRGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETY--SFGSYQDVPVQDVII 152
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 2-83 5.36e-09

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: 50.91  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357071   2 VQTGDPTGTGRGGSSIWAKKFED--------------------EYSEYLKH-----NVRGVVSMAN--NGPNTNGSQFFI 54
Cdd:cd01924    48 VQTGDPQGKNPGFPDPETGKSRTipleikpegqkqpvygktleEAGRYDEQpvlpfNAFGAIAMARteFDPNSASSQFFF 127

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720357071  55 TYGKQ-------PHLDMKYTVFGKVIDGLETLDELE 83
Cdd:cd01924   128 LLKDNeltpsrnNVLDGRYAVFGYVTDGLDILRELK 163
PRK10903 PRK10903
peptidylprolyl isomerase A;
33-105 9.04e-07

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 45.22  E-value: 9.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720357071  33 NVRGVVSMANNG-PNTNGSQFFITYGKQPHL-----DMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHIKDITI 105
Cdd:PRK10903  107 NTRGTIAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKISQVPT--HDVGPYQNVPSKPVVI 183
 
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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