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Conserved domains on  [gi|2462608030|ref|XP_054211204|]
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probable inactive peptidyl-prolyl cis-trans isomerase-like 6 isoform X5 [Homo sapiens]

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 ...
95-202 4.57e-34

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 PTZ00060:

Pssm-ID: 469651  Cd Length: 183  Bit Score: 121.10  E-value: 4.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030  95 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 174
Cdd:PTZ00060    1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79
                          90       100
                  ....*....|....*....|....*...
gi 2462608030 175 IQGGDIVYGKGDNGESIYGPTFEEKAMK 202
Cdd:PTZ00060   80 CQGGDITNHNGTGGESIYGRKFTDENFK 107
 
Name Accession Description Interval E-value
PTZ00060 PTZ00060
cyclophilin; Provisional
95-202 4.57e-34

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 121.10  E-value: 4.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030  95 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 174
Cdd:PTZ00060    1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79
                          90       100
                  ....*....|....*....|....*...
gi 2462608030 175 IQGGDIVYGKGDNGESIYGPTFEEKAMK 202
Cdd:PTZ00060   80 CQGGDITNHNGTGGESIYGRKFTDENFK 107
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
112-197 7.12e-31

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: 111.97  E-value: 7.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 112 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 191
Cdd:cd01926     3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                  ....*.
gi 2462608030 192 YGPTFE 197
Cdd:cd01926    81 YGEKFP 86
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
121-197 1.06e-18

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: 79.61  E-value: 1.06e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462608030 121 SPIGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVygkGDNGESIYGPTFE 197
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIP 67
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
124-191 1.58e-08

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 52.48  E-value: 1.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIVY-GKGDNGESI 191
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDPTGtGTGGPGYTI 74
 
Name Accession Description Interval E-value
PTZ00060 PTZ00060
cyclophilin; Provisional
95-202 4.57e-34

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 121.10  E-value: 4.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030  95 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 174
Cdd:PTZ00060    1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79
                          90       100
                  ....*....|....*....|....*...
gi 2462608030 175 IQGGDIVYGKGDNGESIYGPTFEEKAMK 202
Cdd:PTZ00060   80 CQGGDITNHNGTGGESIYGRKFTDENFK 107
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
112-197 7.12e-31

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: 111.97  E-value: 7.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 112 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 191
Cdd:cd01926     3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                  ....*.
gi 2462608030 192 YGPTFE 197
Cdd:cd01926    81 YGEKFP 86
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
108-203 1.15e-24

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 96.44  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 108 KHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKagFSQRGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDN 187
Cdd:PLN03149   17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94
                          90
                  ....*....|....*.
gi 2462608030 188 GESIYGPTFEEKAMKA 203
Cdd:PLN03149   95 CVSIYGSKFEDENFIA 110
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
123-198 1.22e-21

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: 87.32  E-value: 1.22e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608030 123 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVYGKGdnGESIYGPTFEE 198
Cdd:cd00317     6 KGRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPD 69
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
121-197 1.06e-18

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: 79.61  E-value: 1.06e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462608030 121 SPIGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVygkGDNGESIYGPTFE 197
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIP 67
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
124-205 4.82e-17

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: 75.55  E-value: 4.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEEKAMKA 203
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFRET 78

                  ..
gi 2462608030 204 IK 205
Cdd:cd01928    79 LK 80
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
123-205 1.21e-15

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: 71.41  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 123 IGRLIFELYCDVCPKTCKNFQVLCTgkagfsqrgiRLHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEEKAMK 202
Cdd:cd01922     6 MGEITLELYWNHAPKTCKNFYELAK----------RGYYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEIHP 74

                  ...
gi 2462608030 203 AIK 205
Cdd:cd01922    75 ELK 77
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
124-198 9.67e-15

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: 69.37  E-value: 9.67e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgkagfsQRGirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEE 198
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC-------KKG---YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKD 72
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
124-197 3.26e-12

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: 62.75  E-value: 3.26e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgkagfsqrgIRLHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFE 197
Cdd:cd01925    15 GDIDIELWSKEAPKACRNFIQLC----------LEGYYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFK 77
PTZ00221 PTZ00221
cyclophilin; Provisional
100-196 8.93e-11

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 60.27  E-value: 8.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 100 SAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGF-SQRGIRLHYKNSIFHRI-VQNGWIQG 177
Cdd:PTZ00221   43 SHRMKEEQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHVdRNNNIIVL 122
                          90       100
                  ....*....|....*....|
gi 2462608030 178 GDIV-YGKGDNGESIYGPTF 196
Cdd:PTZ00221  123 GELDsFNVSSTGTPIADEGY 142
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
124-191 1.58e-08

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 52.48  E-value: 1.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIVY-GKGDNGESI 191
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDPTGtGTGGPGYTI 74
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
124-178 1.46e-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: 46.67  E-value: 1.46e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGG 178
Cdd:cd01920     7 GDIVVELYDDKAPITVENFLAYV--RKGF--------YDNTIFHRVISGFVIQGG 51
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
123-194 1.58e-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: 46.95  E-value: 1.58e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608030 123 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDiVYGKGDNGESIYGP 194
Cdd:cd01921     6 LGDLVIDLFTDECPLACLNFLKLCKLK----------YYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQ 66
PRK10791 PRK10791
peptidylprolyl isomerase B;
124-203 5.95e-03

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 36.36  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDivygkgdngesiYGPTFEEKAMKA 203
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYC--REGF--------YNNTIFHRVINGFMIQGGG------------FEPGMKQKATKE 66
 
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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