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Conserved domains on  [gi|663070952|ref|NP_001284574|]
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spliceosome-associated protein CWC27 homolog isoform 3 [Homo sapiens]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112476)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413
PubMed:  14731520|15998457|15353287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 1.78e-133

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: 378.62  E-value: 1.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 663070952 168 FNPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 1.78e-133

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: 378.62  E-value: 1.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 663070952 168 FNPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 1.09e-59

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 190.38  E-value: 1.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGEsiyGAPFKDEFH 88
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  89 SRLRfNRRGLVAMANA-GSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKIKSCE 165
Cdd:COG0652   80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                 ..
gi 663070952 166 VL 167
Cdd:COG0652  156 IV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 1.88e-59

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: 189.39  E-value: 1.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663070952  100 AMANAGS--HDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLSEVDIDDDeRPHNPHKIKSCEV 166
Cdd:pfam00160  83 SMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 2.30e-34

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 125.34  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDEfHSR 90
Cdd:PTZ00060  29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070952  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLSEVDIDDDERPHNPHKIKSC 164
Cdd:PTZ00060 108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
 
Name Accession Description Interval E-value
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 8-178 1.78e-133

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: 378.62  E-value: 1.78e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   8 EPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEF 87
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  88 HSRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01925   81 HSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSVEVL 160

                        170
                 ....*....|.
gi 663070952 168 FNPFDDIIPRE 178
Cdd:cd01925  161 ENPFDDIVPRI 171
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 15-171 2.63e-63

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: 199.56  E-value: 2.63e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFN 94
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663070952  95 RRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlSEVDIDDDERPHNPHKIKSCEVLFNPF 171
Cdd:cd01923   82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGglETLEAM---ENVPDPGTDRPKEEIKIEDTSVFVDPF 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 17-163 1.08e-59

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: 189.78  E-value: 1.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGeSIYGAPFKDEFHSRLRFNRR 96
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663070952  97 GLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYNMlrlSEVDIDDDERPHNPHKIKS 163
Cdd:cd00317   81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEgmDVVDKI---ERGDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 9-167 1.09e-59

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 190.38  E-value: 1.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   9 PPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGEsiyGAPFKDEFH 88
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  89 SRLRfNRRGLVAMANA-GSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKIKSCE 165
Cdd:COG0652   80 PGLK-HKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEgmDVV---DKIAAGPTDPGDGPLEPVVIESVT 155


                 ..
gi 663070952 166 VL 167
Cdd:COG0652  156 IV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 20-166 1.88e-59

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: 189.39  E-value: 1.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952   20 TAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYgaPFKDEFHSRLRFNRRGLV 99
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663070952  100 AMANAGS--HDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVYnmlRLSEVDIDDDeRPHNPHKIKSCEV 166
Cdd:pfam00160  83 SMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEgmDVLE---KIEKVPTDGD-RPVKPVKILSCGV 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 15-162 1.30e-57

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: 184.95  E-value: 1.30e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFN 94
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663070952  95 RRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVT-GDTVYNMLRLSEVDIDDdeRPHNPHKIK 162
Cdd:cd01928   83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIdGFETLDTLEKLPVDKKY--RPLEEIRIK 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 16-161 5.77e-56

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: 180.35  E-value: 5.77e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNR 95
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663070952  96 RGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTG--DTVynmLRLSEVDIDDDERPHNPHKI 161
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKgmDVV---QRIENVKTDKNDRPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-155 1.07e-55

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: 179.65  E-value: 1.07e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNR 95
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  96 RGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVyNMLRLSEVDIDDDeRP 155
Cdd:cd01922   81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMK-VIENMVEVQTQTD-RP 138
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 16-174 7.08e-48

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: 160.20  E-value: 7.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESIYG-------APFKDEFH 88
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  89 SRLRFNRRGLVAMANAGSHDNGSQFFFTLGRA-DELNNKHTIFGKVTgDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVL 167
Cdd:cd01921   81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVV-EGFDVLEKINDAIVDDDGRPLKDIRIKHTHIL 159


                 ....*..
gi 663070952 168 FNPFDDI 174
Cdd:cd01921  160 DDPFPDP 166
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 21-134 1.70e-37

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: 132.77  E-value: 1.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  21 AGDIDIELWSKEAPKACRNFIQLC--------LEAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDE-FHsr 90
Cdd:cd01926   14 AGRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDEnFK-- 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 663070952  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVT 134
Cdd:cd01926   92 LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV 135
PTZ00060 PTZ00060
cyclophilin; Provisional
 21-164 2.30e-34

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 125.34  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  21 AGDIDIELWSKEAPKACRNFIQLCL---------EAYYDNTIFHRVVPGFIVQGGDPT-GTGSGGESIYGAPFKDEfHSR 90
Cdd:PTZ00060  29 AGRIVFELFSDVTPKTAENFRALCIgdkvgssgkNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFK 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070952  91 LRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTvyNMLRLSEVDIDDDERPHNPHKIKSC 164
Cdd:PTZ00060 108 LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGM--EVVRAMEKEGTQSGYPKKPVVVTDC 179
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 10-164 6.89e-34

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 124.18  E-value: 6.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  10 PTNGKVLLKTT-----AGDIDIELWSKEAPKACRNFIQLCLEAY--------YDNTIFHRVVPGFIVQGGD-PTGTGSGG 75
Cdd:PLN03149  16 PKNPVVFFDVTiggipAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  76 ESIYGAPFKDE-FHSRlrFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDER 154
Cdd:PLN03149  96 VSIYGSKFEDEnFIAK--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVVRKIENVATGPNNR 173

                        170
                 ....*....|
gi 663070952 155 PHNPHKIKSC 164
Cdd:PLN03149 174 PKLACVISEC 183
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 16-135 9.82e-25

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: 98.67  E-value: 9.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  16 LLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSGGESiyGAPFKDEFHSRLRfNR 95
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLS-NT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663070952  96 RGLVAMA-NAGSHDNGSQFFFTLGRADELNNK-----HTIFGKVTG 135
Cdd:cd01920   78 RGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTE 123
PRK10903 PRK10903
peptidylprolyl isomerase A;
15-167 1.57e-24

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 99.15  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSggESIYGAPFKDEFHSRLRfN 94
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQ--QKKPNPPIKNEADNGLR-N 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  95 RRGLVAMANAGSHDNG-SQFFFTLGRADELNNKHTIFG-KVTGDTVYNML---RLSEVDIDD----DERPHNPHKIKSCE 165
Cdd:PRK10903 108 TRGTIAMARTADKDSAtSQFFINVADNAFLDHGQRDFGyAVFGKVVKGMDvadKISQVPTHDvgpyQNVPSKPVVILSAK 187


                 ..
gi 663070952 166 VL 167
Cdd:PRK10903 188 VL 189
PRK10791 PRK10791
peptidylprolyl isomerase B;
15-124 3.80e-16

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 75.26  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  15 VLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGdptGTGSG-GESIYGAPFKDEFHSRLRf 93
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGmKQKATKEPIKNEANNGLK- 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 663070952  94 NRRGLVAMANAGS-HDNGSQFFFTLGRADELN 124
Cdd:PRK10791  78 NTRGTLAMARTQApHSATAQFFINVVDNDFLN 109
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 17-134 4.69e-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: 72.48  E-value: 4.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  17 LKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVVPGFIVQGGDPTGTGSG---------------------G 75
Cdd:cd01924    2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqK 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663070952  76 ESIYGAP------FKDEFhsRLRFNRRGLVAMANAGSHDNG--SQFFFTLG-------RADELNNKHTIFGKVT 134
Cdd:cd01924   82 QPVYGKTleeagrYDEQP--VLPFNAFGAIAMARTEFDPNSasSQFFFLLKdneltpsRNNVLDGRYAVFGYVT 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 73-170 1.34e-07

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 52.18  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663070952  73 SGGESIYGAPFKDEFHsRLRFNRRGLVAMANAGSHDNGSQFFFTLGRADELNNKHTIFGKVTgDTVYNMLRLSEVDIDDD 152
Cdd:PTZ00221 127 SFNVSSTGTPIADEGY-RHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV-DDLSLLEKLESLPLDDV 204

                         90
                 ....*....|....*...
gi 663070952 153 ERPHNPHKIKSCEVLFNP 170
Cdd:PTZ00221 205 GRPLLPVTVSFCGALTGE 222
 
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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