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Conserved domains on  [gi|1720357063|ref|XP_030098742|]
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peptidyl-prolyl cis-trans isomerase-like 3 isoform X2 [Mus musculus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112576)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; similar to human peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-154 2.58e-111

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: 312.83  E-value: 2.58e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   1 MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLK 80
Cdd:cd01928     1 MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720357063  81 HNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYRPLNDVHIKDITI 154
Cdd:cd01928    81 HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
 
Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-154 2.58e-111

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: 312.83  E-value: 2.58e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   1 MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLK 80
Cdd:cd01928     1 MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720357063  81 HNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYRPLNDVHIKDITI 154
Cdd:cd01928    81 HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 3-154 2.07e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 209.26  E-value: 2.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSiwaKKFEDEYSEYLKHn 82
Cdd:COG0652     9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPG---YTIPDEFDPGLKH- 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720357063  83 VRGVVSMAN-NGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTyRPLNDVHIKDITI 154
Cdd:COG0652    85 KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGD-GPLEPVVIESVTI 156
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-154 1.38e-64

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: 194.40  E-value: 1.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  10 GDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIwaKKFEDEYSEYLKHNVRGVVSM 89
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHKRGALSM 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720357063  90 ANNG--PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtyRPLNDVHIKDITI 154
Cdd:pfam00160  85 ANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD--RPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-151 1.14e-41

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 137.28  E-value: 1.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  10 GDIKIEVFCERTPKTCENFLALCASN---------YYNGCVFHRNIKGFMVQTGDPT-GTGRGGSSIWAKKFEDEySEYL 79
Cdd:PTZ00060   30 GRIVFELFSDVTPKTAENFRALCIGDkvgssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFKL 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720357063  80 KHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLNDVHIKD 151
Cdd:PTZ00060  109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGTQSGYPKKPVVVTD 178
 
Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-154 2.58e-111

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: 312.83  E-value: 2.58e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   1 MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLK 80
Cdd:cd01928     1 MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720357063  81 HNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYRPLNDVHIKDITI 154
Cdd:cd01928    81 HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 3-161 7.34e-84

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: 243.48  E-value: 7.34e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHN 82
Cdd:cd01923     2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720357063  83 VRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNeKTYRPLNDVHIKDITIHANPFAQ 161
Cdd:cd01923    82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDP-GTDRPKEEIKIEDTSVFVDPFEE 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 4-151 2.98e-72

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: 213.66  E-value: 2.98e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSsIWAKKFEDEYSEYLKHNV 83
Cdd:cd00317     1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGS-GPGYKFPDENFPLKYHHR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720357063  84 RGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKD 151
Cdd:cd00317    80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEN-GRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 3-154 2.07e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 209.26  E-value: 2.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSiwaKKFEDEYSEYLKHn 82
Cdd:COG0652     9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPG---YTIPDEFDPGLKH- 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720357063  83 VRGVVSMAN-NGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTyRPLNDVHIKDITI 154
Cdd:COG0652    85 KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGD-GPLEPVVIESVTI 156
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-152 6.34e-65

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: 195.37  E-value: 6.34e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNV 83
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720357063  84 RGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNeKTYRPLNDVHIKDI 152
Cdd:cd01927    81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTD-KNDRPYEDIKIINI 148
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-154 1.38e-64

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: 194.40  E-value: 1.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  10 GDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIwaKKFEDEYSEYLKHNVRGVVSM 89
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHKRGALSM 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720357063  90 ANNG--PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtyRPLNDVHIKDITI 154
Cdd:pfam00160  85 ANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD--RPVKPVKILSCGV 149
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-159 3.83e-61

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: 186.40  E-value: 3.83e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   2 SVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKH 81
Cdd:cd01925     7 KVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRF 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720357063  82 NVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVI-DGLETLDELEKLPVNEKTyRPLNDVHIKDITIHANPF 159
Cdd:cd01925    87 NRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNLLKLAEVETDKDE-RPVYPPKITSVEVLENPF 164
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-149 5.08e-60

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: 182.73  E-value: 5.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNV 83
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720357063  84 RGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLNDVHI 149
Cdd:cd01922    81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVE--VQTQTDRPIDEVKI 144
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 5-159 1.60e-52

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: 164.44  E-value: 1.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   5 LHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIW-------AKKFEDEYSE 77
Cdd:cd01921     2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYsqlygrqARFFEPEILP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  78 YLKHNVRGVVSMANNGPNTNGSQFFITYGKQ-PHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKDITIHA 156
Cdd:cd01921    82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKINDAIVDDD-GRPLKDIRIKHTHILD 160


                  ...
gi 1720357063 157 NPF 159
Cdd:cd01921   161 DPF 163
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-151 4.17e-51

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: 160.50  E-value: 4.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   7 TDVGDIKIEVFCERTPKTCENFLALCASNY--------YNGCVFHRNIKGFMVQTGDPT-GTGRGGSSIWAKKFEDEYSE 77
Cdd:cd01926    12 EPAGRIVMELFADVVPKTAENFRALCTGEKgkggkpfgYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDENFK 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720357063  78 yLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHIKD 151
Cdd:cd01926    92 -LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS--GNGKPKKKVVIAD 162
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-151 1.14e-41

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 137.28  E-value: 1.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  10 GDIKIEVFCERTPKTCENFLALCASN---------YYNGCVFHRNIKGFMVQTGDPT-GTGRGGSSIWAKKFEDEySEYL 79
Cdd:PTZ00060   30 GRIVFELFSDVTPKTAENFRALCIGDkvgssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFKL 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720357063  80 KHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLNDVHIKD 151
Cdd:PTZ00060  109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGTQSGYPKKPVVVTD 178
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 8-132 1.57e-39

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 131.88  E-value: 1.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   8 DVGDIKIEVFCERTPKTCENFLALCASNY--------YNGCVFHRNIKGFMVQTGD-PTGTGRGGSSIWAKKFEDEySEY 78
Cdd:PLN03149   31 PAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKFEDE-NFI 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720357063  79 LKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVI-DGLETLDELE 132
Cdd:PLN03149  110 AKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIE 164
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-154 6.08e-32

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: 111.77  E-value: 6.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSeylKHNV 83
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNG---LSNT 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720357063  84 RGVVSMA-NNGPNTNGSQFFITYGKQPHLDMK-----YTVFGKVIDGLETLDELEKLPVNekTYRPLNDVHIKDITI 154
Cdd:cd01920    78 RGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETY--SFGSYQDVPVQDVII 152
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 7-132 1.83e-21

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: 85.19  E-value: 1.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   7 TDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFED------------- 73
Cdd:cd01924     4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFPDPETGKSRTipleikpegqkqp 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  74 -------EYSEYLKH-----NVRGVVSMAN--NGPNTNGSQFFITYGKQ-------PHLDMKYTVFGKVIDGLETLDELE 132
Cdd:cd01924    84 vygktleEAGRYDEQpvlpfNAFGAIAMARteFDPNSASSQFFFLLKDNeltpsrnNVLDGRYAVFGYVTDGLDILRELK 163
PRK10903 PRK10903
peptidylprolyl isomerase A;
3-154 2.59e-21

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 85.28  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSiwAKKFEDEYSEYLKhN 82
Cdd:PRK10903   31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLR-N 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720357063  83 VRGVVSMANNG-PNTNGSQFFITYGKQPHL-----DMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHIKDITI 154
Cdd:PRK10903  108 TRGTIAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKISQVPT--HDVGPYQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
3-154 2.39e-20

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 82.19  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGdptGTGRGGSSIWAKK-FEDEYSEYLKh 81
Cdd:PRK10791    2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGMKQKATKEpIKNEANNGLK- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  82 NVRGVVSMA-NNGPNTNGSQFFITYGKQPHLDMK--------YTVFGKVIDGLETLDELEKLPVNEKTYR---PLNDVHI 149
Cdd:PRK10791   78 NTRGTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSGMHqdvPKEDVII 157


                  ....*
gi 1720357063 150 KDITI 154
Cdd:PRK10791  158 ESVTV 162
PTZ00221 PTZ00221
cyclophilin; Provisional
 10-149 1.21e-15

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 71.44  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720357063  10 GDIKIEVFCERTPKTCENFLALCAS------------NYYNGCVFHRNIKGFMVQTGDPTGTGrggSSIWAKKFEDEYSE 77
Cdd:PTZ00221   67 GRLVFELFEDVVPETVENFRALITGscgidtntgvklDYLYTPVHHVDRNNNIIVLGELDSFN---VSSTGTPIADEGYR 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720357063  78 YlKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEkTYRPLNDVHI 149
Cdd:PTZ00221  144 H-RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDD-VGRPLLPVTV 213
 
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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