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Conserved domains on  [gi|2076599878|gb|KAG8525186|]
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Peptidyl-prolyl cis-trans isomerase A [Galemys pyrenaicus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 12-111 4.97e-70

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


The actual alignment was detected with superfamily member cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 206.72  E-value: 4.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTRHNGTGGKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAM 91
Cdd:cd01926    65 QGGDFTRGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKI 144

                          90       100
                  ....*....|....*....|
gi 2076599878  92 EGFGSRNGKTSKKITIADCG 111
Cdd:cd01926   145 ENVGSGNGKPKKKVVIADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 12-111 4.97e-70

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: 206.72  E-value: 4.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTRHNGTGGKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAM 91
Cdd:cd01926    65 QGGDFTRGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKI 144

                          90       100
                  ....*....|....*....|
gi 2076599878  92 EGFGSRNGKTSKKITIADCG 111
Cdd:cd01926   145 ENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 2-113 4.28e-57

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 174.65  E-value: 4.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   2 FLKVTGSLCSQGGDFTRHNGTGGKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKV 81
Cdd:PTZ00060   71 FHRIIPQFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKV 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2076599878  82 KEGMNIVEAMEGFGSRNGKTSKKITIADCGQI 113
Cdd:PTZ00060  151 IEGMEVVRAMEKEGTQSGYPKKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 12-111 4.50e-32

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: 110.04  E-value: 4.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTrhnGTGGKSIYGEKFDDENFI--LKHtGPGILSMANAG--PNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNI 87
Cdd:pfam00160  49 QGGDPT---GTGGGGKSIFPIPDEIFPllLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDV 124

                          90       100
                  ....*....|....*....|....
gi 2076599878  88 VEAMEGFGSRNGKTSKKITIADCG 111
Cdd:pfam00160 125 LEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 12-107 4.49e-29

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 102.56  E-value: 4.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTRhNGTGGKsiyGEKFDDENFI-LKHTgPGILSMANA-GPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVE 89
Cdd:COG0652    58 QGGDPTG-TGTGGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVD 132

                          90
                  ....*....|....*....
gi 2076599878  90 AME-GFGSRNGKTSKKITI 107
Cdd:COG0652   133 KIAaGPTDPGDGPLEPVVI 151
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 12-111 4.97e-70

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: 206.72  E-value: 4.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTRHNGTGGKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAM 91
Cdd:cd01926    65 QGGDFTRGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKI 144

                          90       100
                  ....*....|....*....|
gi 2076599878  92 EGFGSRNGKTSKKITIADCG 111
Cdd:cd01926   145 ENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 2-113 4.28e-57

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 174.65  E-value: 4.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   2 FLKVTGSLCSQGGDFTRHNGTGGKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKV 81
Cdd:PTZ00060   71 FHRIIPQFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKV 150

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2076599878  82 KEGMNIVEAMEGFGSRNGKTSKKITIADCGQI 113
Cdd:PTZ00060  151 IEGMEVVRAMEKEGTQSGYPKKPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 2-113 4.04e-43

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 139.20  E-value: 4.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   2 FLKVTGSLCSQGGDFTRHNGTGGKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKV 81
Cdd:PLN03149   73 FHRVIKDFMIQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRV 152

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2076599878  82 -KEGMNIVEAMEGFGS-RNGKTSKKITIADCGQI 113
Cdd:PLN03149  153 lGDGLLVVRKIENVATgPNNRPKLACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 2-109 4.52e-40

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: 130.08  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   2 FLKVTGSLCSQGGDFTrhNGTGGKSIYGEKFDDENFILK-HTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGK 80
Cdd:cd00317    39 FHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGK 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 2076599878  81 VKEGMNIVEAMEGFG-SRNGKTSKKITIAD 109
Cdd:cd00317   117 VVEGMDVVDKIERGDtDENGRPIKPVTISD 146
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 2-107 3.42e-36

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: 120.33  E-value: 3.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   2 FLKVTGSLCSQGGDFTrHNGTGGKSIYGEKFDDE-NFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGK 80
Cdd:cd01922    39 FHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGR 117

                          90       100
                  ....*....|....*....|....*..
gi 2076599878  81 VKEGMNIVEAMEGFGSRNGKTSKKITI 107
Cdd:cd01922   118 VSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 1-104 6.41e-33

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: 112.17  E-value: 6.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   1 MFLKVTGSLCSQGGDFTrHNGTGGKSIYGEKFDDE-NFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFG 79
Cdd:cd01927    38 IFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFG 116

                          90       100
                  ....*....|....*....|....*
gi 2076599878  80 KVKEGMNIVEAMEgfgsrNGKTSKK 104
Cdd:cd01927   117 RVVKGMDVVQRIE-----NVKTDKN 136
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 12-111 4.50e-32

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: 110.04  E-value: 4.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTrhnGTGGKSIYGEKFDDENFI--LKHtGPGILSMANAG--PNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNI 87
Cdd:pfam00160  49 QGGDPT---GTGGGGKSIFPIPDEIFPllLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDV 124

                          90       100
                  ....*....|....*....|....
gi 2076599878  88 VEAMEGFGSRNGKTSKKITIADCG 111
Cdd:pfam00160 125 LEKIEKVPTDGDRPVKPVKILSCG 148
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 12-92 1.54e-29

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: 103.65  E-value: 1.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTrHNGTGGKSIYGEKFDDE-NFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEA 90
Cdd:cd01923    51 QGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEA 129


                  ..
gi 2076599878  91 ME 92
Cdd:cd01923   130 ME 131
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 12-107 4.49e-29

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 102.56  E-value: 4.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTRhNGTGGKsiyGEKFDDENFI-LKHTgPGILSMANA-GPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVE 89
Cdd:COG0652    58 QGGDPTG-TGTGGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVD 132

                          90
                  ....*....|....*....
gi 2076599878  90 AME-GFGSRNGKTSKKITI 107
Cdd:COG0652   133 KIAaGPTDPGDGPLEPVVI 151
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 12-92 1.41e-27

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: 98.66  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  12 QGGDFTrHNGTGGKSIYGEKFDDENF-ILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEA 90
Cdd:cd01928    52 QTGDPT-GTGKGGESIWGKKFEDEFReTLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDT 130


                  ..
gi 2076599878  91 ME 92
Cdd:cd01928   131 LE 132
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-81 1.82e-23

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: 88.56  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878   2 FLKVTGSLCSQGGDFTrHNGTGGKSIYGEKFDDE-NFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGK 80
Cdd:cd01925    47 FHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGK 125


                  .
gi 2076599878  81 V 81
Cdd:cd01925   126 V 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 21-89 8.74e-17

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: 71.22  E-value: 8.74e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076599878  21 GTGGKSIYGEK-------FDDE-NFILKHTGPGILSMANAGPNTNGSQFFICTAK-TEWLDGKHVVFGKVKEGMNIVE 89
Cdd:cd01921    57 GAGGESIYSQLygrqarfFEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLE 134
PTZ00221 PTZ00221
cyclophilin; Provisional
 24-111 1.59e-12

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 61.42  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  24 GKSIYGEKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMEGFG-SRNGKTS 102
Cdd:PTZ00221  129 NVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDVGRPL 208


                  ....*....
gi 2076599878 103 KKITIADCG 111
Cdd:PTZ00221  209 LPVTVSFCG 217
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 45-93 5.39e-06

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: 42.43  E-value: 5.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2076599878  45 GILSMA-NAGPNTNGSQFFICTAKTEWLD-----GKHVVFGKVKEGMNIVEAMEG 93
Cdd:cd01920    79 GTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAG 133
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 24-108 3.31e-05

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: 40.89  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  24 GKSIYGEKF-----DDENFILKHTGPGILSMANA--GPNTNGSQFFICTAKTEW-------LDGKHVVFGKVKEGMNIVE 89
Cdd:cd01924    81 KQPVYGKTLeeagrYDEQPVLPFNAFGAIAMARTefDPNSASSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTDGLDILR 160

                          90
                  ....*....|....*....
gi 2076599878  90 AMegfgsrngKTSKKITIA 108
Cdd:cd01924   161 EL--------KVGDKIESA 171
PRK10903 PRK10903
peptidylprolyl isomerase A;
45-98 3.63e-03

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 35.20  E-value: 3.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076599878  45 GILSMA-NAGPNTNGSQFFICTAKTEWLD-GK----HVVFGKVKEGMNIVEAMEGFGSRN 98
Cdd:PRK10903  110 GTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHD 169
 
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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