NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|551894761|ref|NP_001272755|]
View 

peptidyl-prolyl cis-trans isomerase-like 3 isoform 1 [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)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.48e-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: 2.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   1 MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLK 80
Cdd:cd01928    1 MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551894761  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 2.48e-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: 2.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   1 MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLK 80
Cdd:cd01928    1 MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551894761  81 HNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYRPLNDVHIKDITI 154
Cdd:cd01928   81 HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
3-152 3.25e-66

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 organisms studied so far and catalyze peptidyl-prolyl isomerisation 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: 425493 [Multi-domain]  Cd Length: 151  Bit Score: 198.64  E-value: 3.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761    3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTG-----RGGSSiwaKKFEDEYSE 77
Cdd:pfam00160   2 VDIETSLGRIVIELFGDKAPKTAENFLQLCKKGFYDGTTFHRVIPNFMVQGGDPTGTGgpgdgKGGES---FPFPDEIDS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 551894761   78 YLKHnVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKDI 152
Cdd:pfam00160  79 LLKH-KRGALSMANTGPNSNGSQFFITLGPAPHLDGKYTVFGRVVEGMDVLEKIEKVPTDGK-DRPVKPVKILSC 151
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
2-154 8.14e-64

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


Pssm-ID: 223725 [Multi-domain]  Cd Length: 158  Bit Score: 192.82  E-value: 8.14e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   2 SVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGT-GRGGSSIwakKFEDEYSEYLK 80
Cdd:COG0652    1 TVILETNKGDITIELYPDKAPKTVANFLQLVKEGFYDGTIFHRVIPGFMIQGGDPTGGdGTGGPGP---PFKDENFALNG 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551894761  81 H-NVRGVVSMANNG-PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTY---RPLNDVHIKDITI 154
Cdd:COG0652   78 DrHKRGTLSMARAGdPNSNGSQFFITVVDNPFLDGKYTVFGQVVEGMDVVDKIKNGDTDDSGYvqdVPADPVKILSVKI 156
PTZ00060 PTZ00060
cyclophilin; Provisional
10-151 1.09e-41

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 137.28  E-value: 1.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761  10 GDIKIEVFCERTPKTCENFLALCASN---------YYNGCVFHRNIKGFMVQTGDPT-GTGRGGSSIWAKKFEDEySEYL 79
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCIGDkvgssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFKL 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 551894761  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 2.48e-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: 2.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   1 MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLK 80
Cdd:cd01928    1 MSVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551894761  81 HNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYRPLNDVHIKDITI 154
Cdd:cd01928   81 HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
3-161 7.04e-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: 7.04e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHN 82
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551894761  83 VRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNeKTYRPLNDVHIKDITIHANPFAQ 161
Cdd:cd01923   82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDP-GTDRPKEEIKIEDTSVFVDPFEE 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
4-151 2.86e-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: 2.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSsIWAKKFEDEYSEYLKHNV 83
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGS-GPGYKFPDENFPLKYHHR 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 551894761  84 RGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKD 151
Cdd:cd00317   80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEN-GRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
3-152 3.25e-66

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 organisms studied so far and catalyze peptidyl-prolyl isomerisation 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: 425493 [Multi-domain]  Cd Length: 151  Bit Score: 198.64  E-value: 3.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761    3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTG-----RGGSSiwaKKFEDEYSE 77
Cdd:pfam00160   2 VDIETSLGRIVIELFGDKAPKTAENFLQLCKKGFYDGTTFHRVIPNFMVQGGDPTGTGgpgdgKGGES---FPFPDEIDS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 551894761   78 YLKHnVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKDI 152
Cdd:pfam00160  79 LLKH-KRGALSMANTGPNSNGSQFFITLGPAPHLDGKYTVFGRVVEGMDVLEKIEKVPTDGK-DRPVKPVKILSC 151
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
4-152 6.08e-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: 6.08e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNV 83
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551894761  84 RGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNeKTYRPLNDVHIKDI 152
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTD-KNDRPYEDIKIINI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
2-154 8.14e-64

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


Pssm-ID: 223725 [Multi-domain]  Cd Length: 158  Bit Score: 192.82  E-value: 8.14e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   2 SVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGT-GRGGSSIwakKFEDEYSEYLK 80
Cdd:COG0652    1 TVILETNKGDITIELYPDKAPKTVANFLQLVKEGFYDGTIFHRVIPGFMIQGGDPTGGdGTGGPGP---PFKDENFALNG 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551894761  81 H-NVRGVVSMANNG-PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTY---RPLNDVHIKDITI 154
Cdd:COG0652   78 DrHKRGTLSMARAGdPNSNGSQFFITVVDNPFLDGKYTVFGQVVEGMDVVDKIKNGDTDDSGYvqdVPADPVKILSVKI 156
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
2-159 3.68e-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: 3.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   2 SVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKH 81
Cdd:cd01925    7 KVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRF 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 551894761  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 4.87e-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: 4.87e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSEYLKHNV 83
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 551894761  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 1.53e-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: 1.53e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   5 LHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIW-------AKKFEDEYSE 77
Cdd:cd01921    2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYsqlygrqARFFEPEILP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761  78 YLKHNVRGVVSMANNGPNTNGSQFFITYGKQ-PHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKDITIHA 156
Cdd:cd01921   82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKINDAIVDDD-GRPLKDIRIKHTHILD 160

                 ...
gi 551894761 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 4.00e-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: 4.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   7 TDVGDIKIEVFCERTPKTCENFLALCASNY--------YNGCVFHRNIKGFMVQTGDPT-GTGRGGSSIWAKKFEDEYSE 77
Cdd:cd01926   12 EPAGRIVMELFADVVPKTAENFRALCTGEKgkggkpfgYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDENFK 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551894761  78 yLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHIKD 151
Cdd:cd01926   92 -LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS--GNGKPKKKVVIAD 162
PTZ00060 PTZ00060
cyclophilin; Provisional
10-151 1.09e-41

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 137.28  E-value: 1.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761  10 GDIKIEVFCERTPKTCENFLALCASN---------YYNGCVFHRNIKGFMVQTGDPT-GTGRGGSSIWAKKFEDEySEYL 79
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCIGDkvgssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFKL 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 551894761  80 KHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLNDVHIKD 151
Cdd:PTZ00060 109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGTQSGYPKKPVVVTD 178
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
8-132 1.51e-39

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 131.88  E-value: 1.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   8 DVGDIKIEVFCERTPKTCENFLALCASNY--------YNGCVFHRNIKGFMVQTGD-PTGTGRGGSSIWAKKFEDEySEY 78
Cdd:PLN03149  31 PAGRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKFEDE-NFI 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 551894761  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 5.83e-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: 5.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   4 TLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFEDEYSeylKHNV 83
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNG---LSNT 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 551894761  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 1.75e-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: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   7 TDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSIWAKKFED------------- 73
Cdd:cd01924    4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFPDPETGKSRTipleikpegqkqp 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761  74 -------EYSEYLKH-----NVRGVVSMAN--NGPNTNGSQFFITYGKQ-------PHLDMKYTVFGKVIDGLETLDELE 132
Cdd:cd01924   84 vygktleEAGRYDEQpvlpfNAFGAIAMARteFDPNSASSQFFFLLKDNeltpsrnNVLDGRYAVFGYVTDGLDILRELK 163
PRK10903 PRK10903
peptidylprolyl isomerase A;
3-154 2.49e-21

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 85.28  E-value: 2.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGDPTGTGRGGSSiwAKKFEDEYSEYLKhN 82
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLR-N 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 551894761  83 VRGVVSMANNG-PNTNGSQFFITYGKQPHL-----DMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHIKDITI 154
Cdd:PRK10903 108 TRGTIAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKISQVPT--HDVGPYQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
3-154 2.29e-20

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 82.19  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761   3 VTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCVFHRNIKGFMVQTGdptGTGRGGSSIWAKK-FEDEYSEYLKh 81
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGMKQKATKEpIKNEANNGLK- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761  82 NVRGVVSMA-NNGPNTNGSQFFITYGKQPHLDMK--------YTVFGKVIDGLETLDELEKLPVNEKTYR---PLNDVHI 149
Cdd:PRK10791  78 NTRGTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSGMHqdvPKEDVII 157

                 ....*
gi 551894761 150 KDITI 154
Cdd:PRK10791 158 ESVTV 162
PTZ00221 PTZ00221
cyclophilin; Provisional
10-149 1.16e-15

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 71.44  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551894761  10 GDIKIEVFCERTPKTCENFLALCAS------------NYYNGCVFHRNIKGFMVQTGDPTGTGrggSSIWAKKFEDEYSE 77
Cdd:PTZ00221  67 GRLVFELFEDVVPETVENFRALITGscgidtntgvklDYLYTPVHHVDRNNNIIVLGELDSFN---VSSTGTPIADEGYR 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 551894761  78 YlKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEkTYRPLNDVHI 149
Cdd:PTZ00221 144 H-RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDD-VGRPLLPVTV 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH