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Conserved domains on  [gi|1720430487|ref|XP_030099970|]
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NK-tumor recognition protein 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 ...
 109-240 1.06e-56

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 cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 193.63  E-value: 1.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  109 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSG---------------------------------NGKGGESI 155
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGekgkggkpfgykgstfhrvipdfmiqggdftrgNGTGGKSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  156 YGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYADVR 235
Cdd:cd01926     81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVV 159


                   ....*
gi 1720430487  236 VIDCG 240
Cdd:cd01926    160 IADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 109-240 1.06e-56

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: 193.63  E-value: 1.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  109 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSG---------------------------------NGKGGESI 155
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGekgkggkpfgykgstfhrvipdfmiqggdftrgNGTGGKSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  156 YGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYADVR 235
Cdd:cd01926     81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVV 159


                   ....*
gi 1720430487  236 VIDCG 240
Cdd:cd01926    160 IADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 108-242 1.01e-47

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 168.87  E-value: 1.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  108 RPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSG----------------------------------NGKGGE 153
Cdd:PTZ00060    15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGdkvgssgknlhykgsifhriipqfmcqggditnhNGTGGE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  154 SIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYAD 233
Cdd:PTZ00060    95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPKKP 173


                   ....*....
gi 1720430487  234 VRVIDCGVL 242
Cdd:PTZ00060   174 VVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 115-241 1.13e-41

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: 150.10  E-value: 1.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  115 IEINREpvGRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYggYFKDENFI--LK 168
Cdd:pfam00160    1 IETNGL--GRIVIELFGDKAPKTVENFLQLCkkgfydgttfhrvipgfmvqggdpTGTGGGGKSIF--PIPDEIFPllLK 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430487  169 HDRaFLLSMANRG--KHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYADVRVIDCGV 241
Cdd:pfam00160   77 HKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 123-237 2.41e-28

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 112.19  E-value: 2.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  123 GRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGEsiygGY-FKDENFI-LKHDRAfLLS 176
Cdd:COG0652     16 GDIVIELFPDKAPKTVANFVSLAkegfydgtifhrvipgfmiqggdpTGTGTGGP----GYtIPDEFDPgLKHKRG-TLA 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430487  177 MAN-RGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVI 237
Cdd:COG0652     91 MARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 109-240 1.06e-56

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: 193.63  E-value: 1.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  109 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSG---------------------------------NGKGGESI 155
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGekgkggkpfgykgstfhrvipdfmiqggdftrgNGTGGKSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  156 YGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYADVR 235
Cdd:cd01926     81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVV 159


                   ....*
gi 1720430487  236 VIDCG 240
Cdd:cd01926    160 IADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 108-242 1.01e-47

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 168.87  E-value: 1.01e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  108 RPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSG----------------------------------NGKGGE 153
Cdd:PTZ00060    15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGdkvgssgknlhykgsifhriipqfmcqggditnhNGTGGE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  154 SIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYAD 233
Cdd:PTZ00060    95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPKKP 173


                   ....*....
gi 1720430487  234 VRVIDCGVL 242
Cdd:PTZ00060   174 VVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 122-238 1.03e-44

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: 158.58  E-value: 1.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  122 VGRIMFQLFSDICPKTCKNFLCLCSG-----------------------NGKGGESIYGGYFKDENFILK-HDRAFLLSM 177
Cdd:cd00317      6 KGRIVIELYGDEAPKTVENFLSLARGgfydgttfhrvipgfmiqggdptGTGGGGSGPGYKFPDENFPLKyHHRRGTLSM 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720430487  178 ANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 238
Cdd:cd00317     86 ANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 122-238 7.30e-42

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: 150.66  E-value: 7.30e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  122 VGRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYGGYFKDENF-ILKHDRAFLLS 176
Cdd:cd01928      9 LGDIKIELFCDDCPKACENFLALCasgyyngcifhrnikgfmvqtgdpTGTGKGGESIWGKKFEDEFReTLKHDSRGVVS 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430487  177 MANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 238
Cdd:cd01928     89 MANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 115-241 1.13e-41

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: 150.10  E-value: 1.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  115 IEINREpvGRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYggYFKDENFI--LK 168
Cdd:pfam00160    1 IETNGL--GRIVIELFGDKAPKTVENFLQLCkkgfydgttfhrvipgfmvqggdpTGTGGGGKSIF--PIPDEIFPllLK 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430487  169 HDRaFLLSMANRG--KHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYADVRVIDCGV 241
Cdd:pfam00160   77 HKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 123-238 8.03e-39

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: 141.83  E-value: 8.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  123 GRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYGGYFKDE-NFILKHDRAFLLSM 177
Cdd:cd01927      7 GDIHIRLFPEEAPKTVENFTTHArngyynntifhrvikgfmiqtgdpTGDGTGGESIWGKEFEDEfSPSLKHDRPYTLSM 86

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720430487  178 ANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 238
Cdd:cd01927     87 ANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 123-242 1.37e-36

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: 136.01  E-value: 1.37e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  123 GRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYGGYFKDE-NFILKHDRAFLLSM 177
Cdd:cd01923      9 GDLNLELHCDKAPKACENFIKLCkkgyydgtifhrsirnfmiqggdpTGTGRGGESIWGKPFKDEfKPNLSHDGRGVLSM 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430487  178 ANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVIDCGVL 242
Cdd:cd01923     89 ANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSVF 153
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 109-240 4.26e-36

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 135.73  E-value: 4.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  109 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSG---------------------------------NGKGGESI 155
Cdd:PLN03149    19 PVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGefrkaglpqgykgcqfhrvikdfmiqggdflkgDGTGCVSI 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  156 YGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVI-SGFEVIEQIENLKTDAASRPYADV 234
Cdd:PLN03149    99 YGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLAC 178


                   ....*.
gi 1720430487  235 RVIDCG 240
Cdd:PLN03149   179 VISECG 184
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 122-237 1.65e-31

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: 121.10  E-value: 1.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  122 VGRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYGGYFKDE-NFILKHDRAFLLS 176
Cdd:cd01922      6 MGEITLELYWNHAPKTCKNFYELAkrgyyngtifhrlikdfmiqggdpTGTGRGGASIYGKKFEDEiHPELKHTGAGILS 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720430487  177 MANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYADVRVI 237
Cdd:cd01922     86 MANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKIL 145
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 123-237 2.41e-28

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 112.19  E-value: 2.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  123 GRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGEsiygGY-FKDENFI-LKHDRAfLLS 176
Cdd:COG0652     16 GDIVIELFPDKAPKTVANFVSLAkegfydgtifhrvipgfmiqggdpTGTGTGGP----GYtIPDEFDPgLKHKRG-TLA 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720430487  177 MAN-RGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVI 237
Cdd:COG0652     91 MARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 122-236 7.47e-26

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: 105.50  E-value: 7.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  122 VGRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYGG-------YFKDE-NFILKH 169
Cdd:cd01921      6 LGDLVIDLFTDECPLACLNFLKLCklkyynfclfynvqkdfiaqtgdpTGTGAGGESIYSQlygrqarFFEPEiLPLLKH 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430487  170 DRAFLLSMANRGKHTNGSQFFIT-TKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRV 236
Cdd:cd01921     86 SKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 122-242 8.21e-26

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: 105.51  E-value: 8.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  122 VGRIMFQLFSDICPKTCKNFLCLC------------------------SGNGKGGESIYGGYFKDE-NFILKHDRAFLLS 176
Cdd:cd01925     14 AGDIDIELWSKEAPKACRNFIQLClegyydntifhrvvpgfiiqggdpTGTGTGGESIYGEPFKDEfHSRLRFNRRGLVG 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720430487  177 MANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVI--SGFEVIEqIENLKTDAASRPYADVRVIDCGVL 242
Cdd:cd01925     94 MANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgdTIYNLLK-LAEVETDKDERPVYPPKITSVEVL 160
PTZ00221 PTZ00221
cyclophilin; Provisional
 114-242 2.54e-15

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 77.60  E-value: 2.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  114 DIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGNG---------------------------------KGGESIYGGYF 160
Cdd:PTZ00221    58 DISIGDVLAGRLVFELFEDVVPETVENFRALITGSCgidtntgvkldylytpvhhvdrnnniivlgeldSFNVSSTGTPI 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  161 KDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVIDCG 240
Cdd:PTZ00221   138 ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLPVTVSFCG 217


                   ..
gi 1720430487  241 VL 242
Cdd:PTZ00221   218 AL 219
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 152-220 1.46e-03

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: 41.28  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430487  152 GESIYG------GYFKDENFILKHDrAFLLSMANRGKHTNG--SQFFI-------TTKPAPHLDGVHVVFGLVISGFEVI 216
Cdd:cd01924     81 KQPVYGktleeaGRYDEQPVLPFNA-FGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDIL 159


                   ....
gi 1720430487  217 EQIE 220
Cdd:cd01924    160 RELK 163
 
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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