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Conserved domains on  [gi|62526130|ref|NP_035048|]
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NK-tumor recognition protein [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 ...
 7-174 8.45e-83

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: 268.36  E-value: 8.45e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYA 166
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                 ....*...
gi 62526130  167 DVRVIDCG 174
Cdd:cd01926  157 KVVIADCG 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 ...
 7-174 8.45e-83

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: 268.36  E-value: 8.45e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYA 166
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                 ....*...
gi 62526130  167 DVRVIDCG 174
Cdd:cd01926  157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-176 9.81e-69

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 228.96  E-value: 9.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     6 RPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGlgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKG 85
Cdd:PTZ00060   15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    86 GESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPY 165
Cdd:PTZ00060   93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPK 171

                         170
                  ....*....|.
gi 62526130   166 ADVRVIDCGVL 176
Cdd:PTZ00060  172 KPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 13-175 4.43e-58

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: 197.09  E-value: 4.43e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     13 IEINREpvGRIMFQLFSDICPKTCKNFLCLCsgekglgkTTGKklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYgg 92
Cdd:pfam00160    1 IETNGL--GRIVIELFGDKAPKTVENFLQLC--------KKGF---YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     93 YFKDENFI--LKHDRaFLLSMANRG--KHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYADV 168
Cdd:pfam00160   65 PIPDEIFPllLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPV 142


                   ....*..
gi 62526130    169 RVIDCGV 175
Cdd:pfam00160  143 KILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 21-171 1.02e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 159.18  E-value: 1.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   21 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFsEGNGKGGEsiygGY-FKDENF 99
Cdd:COG0652   16 GDIVIELFPDKAPKTVANFVSLA--KEGF---------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP----GYtIPDEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62526130  100 I-LKHDRAfLLSMAN-RGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVI 171
Cdd:COG0652   80 PgLKHKRG-TLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 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 ...
 7-174 8.45e-83

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: 268.36  E-value: 8.45e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYA 166
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                 ....*...
gi 62526130  167 DVRVIDCG 174
Cdd:cd01926  157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-176 9.81e-69

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 228.96  E-value: 9.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     6 RPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGlgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKG 85
Cdd:PTZ00060   15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    86 GESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPY 165
Cdd:PTZ00060   93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPK 171

                         170
                  ....*....|.
gi 62526130   166 ADVRVIDCGVL 176
Cdd:PTZ00060  172 KPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 20-172 1.17e-60

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: 204.42  E-value: 1.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   20 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDFSegNGKGGESIYGGYFKDENF 99
Cdd:cd00317    6 KGRIVIELYGDEAPKTVENFLSLARGGF-----------YDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENF 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62526130  100 ILK-HDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 172
Cdd:cd00317   73 PLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 13-175 4.43e-58

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: 197.09  E-value: 4.43e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     13 IEINREpvGRIMFQLFSDICPKTCKNFLCLCsgekglgkTTGKklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYgg 92
Cdd:pfam00160    1 IETNGL--GRIVIELFGDKAPKTVENFLQLC--------KKGF---YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     93 YFKDENFI--LKHDRaFLLSMANRG--KHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYADV 168
Cdd:pfam00160   65 PIPDEIFPllLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPV 142


                   ....*..
gi 62526130    169 RVIDCGV 175
Cdd:pfam00160  143 KILSCGV 149
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 7-174 1.01e-56

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 194.67  E-value: 1.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130     7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKglgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:PLN03149   19 PVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVI-SGFEVIEQIENLKTDAASRPY 165
Cdd:PLN03149   96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPK 175


                  ....*....
gi 62526130   166 ADVRVIDCG 174
Cdd:PLN03149  176 LACVISECG 184
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 20-172 3.01e-53

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: 183.41  E-value: 3.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   20 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKDENF 99
Cdd:cd01928    9 LGDIKIELFCDDCPKACENFLALCASGY-----------YNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFR 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62526130  100 -ILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 172
Cdd:cd01928   77 eTLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 21-172 2.46e-50

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: 174.96  E-value: 2.46e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   21 GRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKDE-NF 99
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA-----------RNGYYNNTIFHRVIKGFMIQTGD-PTGDGTGGESIWGKEFEDEfSP 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62526130  100 ILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 172
Cdd:cd01927   75 SLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 21-176 8.84e-49

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: 170.67  E-value: 8.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   21 GRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYGGYFKDE-NF 99
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC-----------KKGYYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKP 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62526130  100 ILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVIDCGVL 176
Cdd:cd01923   77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSVF 153
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 21-171 1.02e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 159.18  E-value: 1.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   21 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFsEGNGKGGEsiygGY-FKDENF 99
Cdd:COG0652   16 GDIVIELFPDKAPKTVANFVSLA--KEGF---------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP----GYtIPDEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62526130  100 I-LKHDRAfLLSMAN-RGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVI 171
Cdd:COG0652   80 PgLKHKRG-TLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 20-171 1.77e-43

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: 155.00  E-value: 1.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   20 VGRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKDE-N 98
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELA-----------KRGYYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiH 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62526130   99 FILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYADVRVI 171
Cdd:cd01922   74 PELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKIL 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 20-176 1.07e-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: 136.71  E-value: 1.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   20 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYGGYFKDE-N 98
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEGY-----------YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   99 FILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVI--SGFEVIEqIENLKTDAASRPYADVRVIDCGVL 176
Cdd:cd01925   82 SRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgdTIYNLLK-LAEVETDKDERPVYPPKITSVEVL 160
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 20-170 1.20e-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: 124.76  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   20 VGRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGG------- 92
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQlygrqar 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   93 YFKDE-NFILKHDRAFLLSMANRGKHTNGSQFFIT-TKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRV 170
Cdd:cd01921   74 FFEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 12-176 5.17e-24

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 102.64  E-value: 5.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    12 DIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGKTTGKKLCYKGSTFHRV-VKNFMIQGGDFSEGNgkggESIY 90
Cdd:PTZ00221   58 DISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVdRNNNIIVLGELDSFN----VSST 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    91 GGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRV 170
Cdd:PTZ00221  134 GTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLPVTV 213


                  ....*.
gi 62526130   171 IDCGVL 176
Cdd:PTZ00221  214 SFCGAL 219
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 21-172 3.23e-19

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: 85.96  E-value: 3.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   21 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFSEGNGK-------GGESIYGgy 93
Cdd:cd01920    7 GDIVVELYDDKAPITVENFLAYV--RKGF---------YDNTIFHRVISGFVIQGGGFTPDLAQketlkpiKNEAGNG-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   94 fkdenfiLKHDRAfLLSMA-NRGKHTNGSQFFITTKPAPHLD-----GVHVVFGLVISGFEVIEQIENLKTdAASRPYAD 167
Cdd:cd01920   74 -------LSNTRG-TIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVET-YSFGSYQD 144


                 ....*
gi 62526130  168 VRVID 172
Cdd:cd01920  145 VPVQD 149
PRK10791 PRK10791
peptidylprolyl isomerase B;
21-158 3.62e-09

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 57.16  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    21 GRIMFQLFSDICPKTCKNFLCLCSgeKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFSEG-NGKGGESIyggyFKDE-N 98
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYCR--EGF---------YNNTIFHRVINGFMIQGGGFEPGmKQKATKEP----IKNEaN 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62526130    99 FILKHDRAFLLSMANRGKHTNGSQFFITTKP-------APHLDGV-HVVFGLVISGFEVIEQIENLKT 158
Cdd:PRK10791   74 NGLKNTRGTLAMARTQAPHSATAQFFINVVDndflnfsGESLQGWgYCVFAEVVEGMDVVDKIKGVAT 141
PRK10903 PRK10903
peptidylprolyl isomerase A;
20-182 4.23e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 57.93  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    20 VGRIMFQLFSDICPKTCKNFL-CLCSGekglgkttgkklCYKGSTFHRVVKNFMIQGGDFsegNGKGGESIYGGYFKDE- 97
Cdd:PRK10903   37 AGNIELELNSQKAPVSVKNFVdYVNSG------------FYNNTTFHRVIPGFMIQGGGF---TEQMQQKKPNPPIKNEa 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130    98 NFILKHDRAfLLSMANRG-KHTNGSQFFITTKPAPHLD------GvHVVFGLVISGFEVIEQIENLKTDAASrPYADVRV 170
Cdd:PRK10903  102 DNGLRNTRG-TIAMARTAdKDSATSQFFINVADNAFLDhgqrdfG-YAVFGKVVKGMDVADKISQVPTHDVG-PYQNVPS 178

                         170
                  ....*....|..
gi 62526130   171 IDCGVLATKLTK 182
Cdd:PRK10903  179 KPVVILSAKVLP 190
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 33-154 7.73e-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: 56.68  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62526130   33 PKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDfSEGNGKG---------------------GESIYG 91
Cdd:cd01924   19 PVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGD-PQGKNPGfpdpetgksrtipleikpegqKQPVYG 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62526130   92 ------GYFKDENFILKHDrAFLLSMANRGKHTNG--SQFFI-------TTKPAPHLDGVHVVFGLVISGFEVIEQIE 154
Cdd:cd01924   87 ktleeaGRYDEQPVLPFNA-FGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 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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