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Conserved domains on  [gi|15232123|ref|NP_186797|]
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cyclophilin 38 [Arabidopsis thaliana]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112474)

cyclophilin-type peptidylprolyl isomerase 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_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
250-424 4.82e-103

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: 303.60  E-value: 4.82e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 250 NPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDG-FVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGE 328
Cdd:cd01924   1 GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGgFVVQTGDPQGKNPGFPDPETGKSRTIPLEIKPEGQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 329 KTPFYGSTLEELGLYKAQVVIPFNAFGTMAMAREEFENDSGSSQVFWLLKESELTPSNSNILDGRYAVFGYVTDNEDFLA 408
Cdd:cd01924  81 KQPVYGKTLEEAGRYDEQPVLPFNAFGAIAMARTEFDPNSASSQFFFLLKDNELTPSRNNVLDGRYAVFGYVTDGLDILR 160
                       170
                ....*....|....*.
gi 15232123 409 DLKVGDVIESIQVVSG 424
Cdd:cd01924 161 ELKVGDKIESARVVEG 176
 
Name Accession Description Interval E-value
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
250-424 4.82e-103

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: 303.60  E-value: 4.82e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 250 NPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDG-FVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGE 328
Cdd:cd01924   1 GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGgFVVQTGDPQGKNPGFPDPETGKSRTIPLEIKPEGQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 329 KTPFYGSTLEELGLYKAQVVIPFNAFGTMAMAREEFENDSGSSQVFWLLKESELTPSNSNILDGRYAVFGYVTDNEDFLA 408
Cdd:cd01924  81 KQPVYGKTLEEAGRYDEQPVLPFNAFGAIAMARTEFDPNSASSQFFFLLKDNELTPSRNNVLDGRYAVFGYVTDGLDILR 160
                       170
                ....*....|....*.
gi 15232123 409 DLKVGDVIESIQVVSG 424
Cdd:cd01924 161 ELKVGDKIESARVVEG 176
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
258-424 1.62e-25

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 101.79  E-value: 1.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPAEGfiDPstekTRTVPLEImVTGEKtpfygst 336
Cdd:COG0652  18 IVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRViPGFMIQGGDPTGTGTG--GP----GYTIPDEF-DPGLK------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 337 leelglykaqvvipfNAFGTMAMAREEfENDSGSSQVFwllkeseLTPSNSNILDGRYAVFGYVTDNEDFLADLKVGD-- 414
Cdd:COG0652  84 ---------------HKRGTLAMARAQ-GPNSAGSQFF-------IVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPtd 140
                       170
                ....*....|....*....
gi 15232123 415 ---------VIESIQVVSG 424
Cdd:COG0652 141 pgdgplepvVIESVTIVED 159
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
258-423 2.02e-23

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: 95.40  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123   258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPaegfiDPSTEKTRTVPLEIMVTGektpfygst 336
Cdd:pfam00160   9 IVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRViPGFMVQGGDPTGT-----GGGGKSIFPIPDEIFPLL--------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123   337 leelglykaqvviPFNAFGTMAMAREEFENDSGSSQVFwllkeseLTPSNSNILDGRYAVFGYVTDNEdfladlkvgDVI 416
Cdd:pfam00160  75 -------------LKHKRGALSMANTGPAPNSNGSQFF-------ITLGPAPHLDGKYTVFGKVVEGM---------DVL 125

                  ....*..
gi 15232123   417 ESIQVVS 423
Cdd:pfam00160 126 EKIEKVP 132
PRK10903 PRK10903
peptidylprolyl isomerase A;
252-420 4.23e-06

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 47.14  E-value: 4.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123  252 NIEdcvfrIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGdpegpaeGFIDPSTEKTRTVPLEimvtgekt 330
Cdd:PRK10903  39 NIE-----LELNSQKAPVSVKNFVDYVNSGFYNNTTFHRViPGFMIQGG-------GFTEQMQQKKPNPPIK-------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123  331 pfygsTLEELGLYkaqvvipfNAFGTMAMAREEfENDSGSSQVFwllkeseLTPSNSNILD-GR----YAVFGYVTDNED 405
Cdd:PRK10903  99 -----NEADNGLR--------NTRGTIAMARTA-DKDSATSQFF-------INVADNAFLDhGQrdfgYAVFGKVVKGMD 157
                        170
                 ....*....|....*
gi 15232123  406 fladlkVGDVIESIQ 420
Cdd:PRK10903 158 ------VADKISQVP 166
 
Name Accession Description Interval E-value
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
250-424 4.82e-103

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: 303.60  E-value: 4.82e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 250 NPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDG-FVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGE 328
Cdd:cd01924   1 GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGgFVVQTGDPQGKNPGFPDPETGKSRTIPLEIKPEGQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 329 KTPFYGSTLEELGLYKAQVVIPFNAFGTMAMAREEFENDSGSSQVFWLLKESELTPSNSNILDGRYAVFGYVTDNEDFLA 408
Cdd:cd01924  81 KQPVYGKTLEEAGRYDEQPVLPFNAFGAIAMARTEFDPNSASSQFFFLLKDNELTPSRNNVLDGRYAVFGYVTDGLDILR 160
                       170
                ....*....|....*.
gi 15232123 409 DLKVGDVIESIQVVSG 424
Cdd:cd01924 161 ELKVGDKIESARVVEG 176
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
260-415 1.51e-27

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: 106.96  E-value: 1.51e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 260 IVLDGYNAPVTAGNFVDLVERHFYDGMEIQR-SDGFVVQTGDPEGPAEGFIDPStektRTVPLEIMvtgektpfygstle 338
Cdd:cd00317  11 IELYGDEAPKTVENFLSLARGGFYDGTTFHRvIPGFMIQGGDPTGTGGGGSGPG----YKFPDENF-------------- 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232123 339 elglykaqVVIPFNAFGTMAMAREefENDSGSSQVFWllkeselTPSNSNILDGRYAVFGYVTDNEDFLADLKVGDV 415
Cdd:cd00317  73 --------PLKYHHRRGTLSMANA--GPNTNGSQFFI-------TTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDT 132
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
258-424 1.62e-25

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 101.79  E-value: 1.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPAEGfiDPstekTRTVPLEImVTGEKtpfygst 336
Cdd:COG0652  18 IVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRViPGFMIQGGDPTGTGTG--GP----GYTIPDEF-DPGLK------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 337 leelglykaqvvipfNAFGTMAMAREEfENDSGSSQVFwllkeseLTPSNSNILDGRYAVFGYVTDNEDFLADLKVGD-- 414
Cdd:COG0652  84 ---------------HKRGTLAMARAQ-GPNSAGSQFF-------IVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPtd 140
                       170
                ....*....|....*....
gi 15232123 415 ---------VIESIQVVSG 424
Cdd:COG0652 141 pgdgplepvVIESVTIVED 159
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
258-423 2.02e-23

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: 95.40  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123   258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPaegfiDPSTEKTRTVPLEIMVTGektpfygst 336
Cdd:pfam00160   9 IVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRViPGFMVQGGDPTGT-----GGGGKSIFPIPDEIFPLL--------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123   337 leelglykaqvviPFNAFGTMAMAREEFENDSGSSQVFwllkeseLTPSNSNILDGRYAVFGYVTDNEdfladlkvgDVI 416
Cdd:pfam00160  75 -------------LKHKRGALSMANTGPAPNSNGSQFF-------ITLGPAPHLDGKYTVFGKVVEGM---------DVL 125

                  ....*..
gi 15232123   417 ESIQVVS 423
Cdd:pfam00160 126 EKIEKVP 132
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
258-413 2.23e-13

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: 67.47  E-value: 2.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGdpegpaeGFIDPSTEKTRTVPLeimvtgEKTPFYGST 336
Cdd:cd01920   9 IVVELYDDKAPITVENFLAYVRKGFYDNTIFHRViSGFVIQGG-------GFTPDLAQKETLKPI------KNEAGNGLS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 337 leelglykaqvvipfNAFGTMAMAREEfENDSGSSQVFWLLKE-SELTPSNSNildGRYAVFGYVTDNEDFL---ADLKV 412
Cdd:cd01920  76 ---------------NTRGTIAMARTN-APDSATSQFFINLKDnASLDYQNEQ---WGYTVFGEVTEGMDVVdkiAGVET 136

                .
gi 15232123 413 G 413
Cdd:cd01920 137 Y 137
PRK10903 PRK10903
peptidylprolyl isomerase A;
252-420 4.23e-06

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 47.14  E-value: 4.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123  252 NIEdcvfrIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGdpegpaeGFIDPSTEKTRTVPLEimvtgekt 330
Cdd:PRK10903  39 NIE-----LELNSQKAPVSVKNFVDYVNSGFYNNTTFHRViPGFMIQGG-------GFTEQMQQKKPNPPIK-------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123  331 pfygsTLEELGLYkaqvvipfNAFGTMAMAREEfENDSGSSQVFwllkeseLTPSNSNILD-GR----YAVFGYVTDNED 405
Cdd:PRK10903  99 -----NEADNGLR--------NTRGTIAMARTA-DKDSATSQFF-------INVADNAFLDhGQrdfgYAVFGKVVKGMD 157
                        170
                 ....*....|....*
gi 15232123  406 fladlkVGDVIESIQ 420
Cdd:PRK10903 158 ------VADKISQVP 166
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
253-416 7.19e-06

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: 46.18  E-value: 7.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 253 IEDCVFRIVLDGY--NAPVTAGNFVDLVERHFYDG---MEIQRSdgFVVQTGDPEGPAEGFID-PSTEKtrtvpleimvt 326
Cdd:cd01921   2 LETTLGDLVIDLFtdECPLACLNFLKLCKLKYYNFclfYNVQKD--FIAQTGDPTGTGAGGESiYSQLY----------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 327 GEKTPFYGSTLEELglykaqvvIPFNAFGTMAMArEEFENDSGSsQVFWLLKEseltpsNSNILDGRYAVFGYVTDNEDF 406
Cdd:cd01921  69 GRQARFFEPEILPL--------LKHSKKGTVSMV-NAGDNLNGS-QFYITLGE------NLDYLDGKHTVFGQVVEGFDV 132
                       170
                ....*....|
gi 15232123 407 LAdlKVGDVI 416
Cdd:cd01921 133 LE--KINDAI 140
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
265-410 8.08e-06

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: 45.87  E-value: 8.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 265 YNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPAEGfidpstektrtvpleimvtGEKtpFYGSTLEElgly 343
Cdd:cd01923  18 DKAPKACENFIKLCKKGYYDGTIFHRSiRNFMIQGGDPTGTGRG-------------------GES--IWGKPFKD---- 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 344 kaqVVIPFN---AFGTMAMAREefENDSGSSQVFwllkeseLTPSNSNILDGRYAVFGYVTDNEDFLADL 410
Cdd:cd01923  73 ---EFKPNLshdGRGVLSMANS--GPNTNGSQFF-------ITYRSCKHLDGKHTVFGRVVGGLETLEAM 130
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
267-431 1.94e-05

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: 45.04  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 267 APVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPAEGfidpstektrtvpleimvtGEKtpFYGSTLEElglyKA 345
Cdd:cd01925  26 APKACRNFIQLCLEGYYDNTIFHRVvPGFIIQGGDPTGTGTG-------------------GES--IYGEPFKD----EF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232123 346 QVVIPFNAFGTMAMAREefENDSGSSQVFwllkeseLTPSNSNILDGRYAVFGYVTDNEDF----LADLKV--GDVIESI 419
Cdd:cd01925  81 HSRLRFNRRGLVGMANA--GDDSNGSQFF-------FTLDKADELNNKHTLFGKVTGDTIYnllkLAEVETdkDERPVYP 151
                       170
                ....*....|..
gi 15232123 420 QVVSGLENLANP 431
Cdd:cd01925 152 PKITSVEVLENP 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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