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Conserved domains on  [gi|517269171|ref|WP_018457989|]
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MULTISPECIES: peptidylprolyl isomerase [Bradyrhizobium]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10002023)

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

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0000413|GO:0003755
PubMed:  14731520|15998457
SCOP:  4000390

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 26-185 3.18e-64

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


:

Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 195.00  E-value: 3.18e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  26 LDKANAIVIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNfNGTGGSKYPnLKQEFSK 105
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTG-TGTGGPGYT-IPDEFDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171 106 -VHFARGIVGMARRGDsVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGSSGGTVtDPDKMVKVQVAS 184
Cdd:COG0652   81 gLKHKRGTLAMARAQG-PNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPL-EPVVIESVTIVE 158


                 .
gi 517269171 185 D 185
Cdd:COG0652  159 D 159
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 26-185 3.18e-64

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 195.00  E-value: 3.18e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  26 LDKANAIVIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNfNGTGGSKYPnLKQEFSK 105
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTG-TGTGGPGYT-IPDEFDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171 106 -VHFARGIVGMARRGDsVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGSSGGTVtDPDKMVKVQVAS 184
Cdd:COG0652   81 gLKHKRGTLAMARAQG-PNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPL-EPVVIESVTIVE 158


                 .
gi 517269171 185 D 185
Cdd:COG0652  159 D 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 33-180 2.24e-54

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: 169.37  E-value: 2.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  33 VIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNFNGTGGSKYPNLKQEF--SKVHFAR 110
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGYKFPDENfpLKYHHRR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171 111 GIVGMARRGDsvDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGSSGgtvtDPDKMVKV 180
Cdd:cd00317   81 GTLSMANAGP--NTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENG----RPIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 36-182 1.02e-49

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: 157.80  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171   36 STKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGqNFNGTGGSKYPNLKQEF--SKVHFARGIV 113
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDP-TGTGGGGKSIFPIPDEIfpLLLKHKRGAL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517269171  114 GMARRGDSVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPgsSGGTVTDPDKMVKVQV 182
Cdd:pfam00160  83 SMANTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT--DGDRPVKPVKILSCGV 149
PRK10903 PRK10903
peptidylprolyl isomerase A;
3-187 2.24e-25

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 96.84  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171   3 RILAVLAAVlFAVPAFAQALPAGLDKANaIVIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQT 82
Cdd:PRK10903   4 STLAAMAAV-FALSALSPAALAAKGDPH-VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  83 GdgqNFNGTGGSKYPN--LKQEF-SKVHFARGIVGMARRGDSvDTANSQFFIMFADGGSLDN-----QYTVIGEVVQGMD 154
Cdd:PRK10903  82 G---GFTEQMQQKKPNppIKNEAdNGLRNTRGTIAMARTADK-DSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMD 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517269171 155 VVDKLKKAPPGSSGGTVTDPDKMVKVQVASDIK 187
Cdd:PRK10903 158 VADKISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 26-185 3.18e-64

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 195.00  E-value: 3.18e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  26 LDKANAIVIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNfNGTGGSKYPnLKQEFSK 105
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTG-TGTGGPGYT-IPDEFDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171 106 -VHFARGIVGMARRGDsVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGSSGGTVtDPDKMVKVQVAS 184
Cdd:COG0652   81 gLKHKRGTLAMARAQG-PNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPL-EPVVIESVTIVE 158


                 .
gi 517269171 185 D 185
Cdd:COG0652  159 D 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 33-180 2.24e-54

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: 169.37  E-value: 2.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  33 VIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNFNGTGGSKYPNLKQEF--SKVHFAR 110
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGYKFPDENfpLKYHHRR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171 111 GIVGMARRGDsvDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGSSGgtvtDPDKMVKV 180
Cdd:cd00317   81 GTLSMANAGP--NTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENG----RPIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 36-182 1.02e-49

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: 157.80  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171   36 STKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGqNFNGTGGSKYPNLKQEF--SKVHFARGIV 113
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDP-TGTGGGGKSIFPIPDEIfpLLLKHKRGAL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517269171  114 GMARRGDSVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPgsSGGTVTDPDKMVKVQV 182
Cdd:pfam00160  83 SMANTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT--DGDRPVKPVKILSCGV 149
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 34-169 1.48e-29

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: 106.37  E-value: 1.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  34 IDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQtGDGQNFNGTGGSKYPNLKQE-FSKVHFARGI 112
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQ-GGGFTPDLAQKETLKPIKNEaGNGLSNTRGT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517269171 113 VGMARRGDsVDTANSQFFIMFADGGSLDNQ-----YTVIGEVVQGMDVVDKLKKAPPGSSGG 169
Cdd:cd01920   81 IAMARTNA-PDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETYSFGS 141
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 31-167 4.15e-29

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: 105.21  E-value: 4.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  31 AIVIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNFNGTGGSKY-PNLKQEFSKV--H 107
Cdd:cd01928    2 SVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWgKKFEDEFRETlkH 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171 108 FARGIVGMARRGDsvDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGSS 167
Cdd:cd01928   82 DSRGVVSMANNGP--NTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKK 139
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 33-162 8.53e-29

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: 104.47  E-value: 8.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  33 VIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNfNGTGGSKYPN--LKQEFSK-VHFA 109
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGkeFEDEFSPsLKHD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517269171 110 R-GIVGMARRGDsvDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKA 162
Cdd:cd01927   80 RpYTLSMANAGP--NTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENV 131
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 32-166 5.01e-28

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: 102.72  E-value: 5.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  32 IVIDSTK-GRIVIKLRPDLAPQHAERIKQLA-------REGF-YNNVPFHRVMDGFMAQTGDGQNFNGTG-----GSKYP 97
Cdd:cd01926    7 ITIGGEPaGRIVMELFADVVPKTAENFRALCtgekgkgGKPFgYKGSTFHRVIPDFMIQGGDFTRGNGTGgksiyGEKFP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517269171  98 NlkQEFSKVHFARGIVGMARRGdsVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAPPGS 166
Cdd:cd01926   87 D--ENFKLKHTGPGLLSMANAG--PNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN 151
PRK10903 PRK10903
peptidylprolyl isomerase A;
3-187 2.24e-25

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 96.84  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171   3 RILAVLAAVlFAVPAFAQALPAGLDKANaIVIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQT 82
Cdd:PRK10903   4 STLAAMAAV-FALSALSPAALAAKGDPH-VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  83 GdgqNFNGTGGSKYPN--LKQEF-SKVHFARGIVGMARRGDSvDTANSQFFIMFADGGSLDN-----QYTVIGEVVQGMD 154
Cdd:PRK10903  82 G---GFTEQMQQKKPNppIKNEAdNGLRNTRGTIAMARTADK-DSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMD 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517269171 155 VVDKLKKAPPGSSGGTVTDPDKMVKVQVASDIK 187
Cdd:PRK10903 158 VADKISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 33-159 6.94e-21

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: 83.74  E-value: 6.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  33 VIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNfNGTGG-SKY---------PNLKqe 102
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTG-TGRGGaSIYgkkfedeihPELK-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517269171 103 fskvHFARGIVGMARRGdsVDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKL 159
Cdd:cd01922   78 ----HTGAGILSMANAG--PNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM 128
PRK10791 PRK10791
peptidylprolyl isomerase B;
39-168 7.51e-21

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 84.12  E-value: 7.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  39 GRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQtgdgqnfngtGGSKYPNLKQEFSKVHF---------- 108
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQ----------GGGFEPGMKQKATKEPIkneannglkn 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517269171 109 ARGIVGMARRGDSvDTANSQFFIMFADGGSLDNQ--------YTVIGEVVQGMDVVDKLKKAPPGSSG 168
Cdd:PRK10791  79 TRGTLAMARTQAP-HSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSG 145
PTZ00060 PTZ00060
cyclophilin; Provisional
 32-174 1.54e-20

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 84.13  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  32 IVIDSTK-GRIVIKLRPDLAPQHAERIKQL---------AREGFYNNVPFHRVMDGFMAQTGDGQNFNGTGGS-----KY 96
Cdd:PTZ00060  22 ISIDNAPaGRIVFELFSDVTPKTAENFRALcigdkvgssGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGEsiygrKF 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517269171  97 PNlkQEFSKVHFARGIVGMARRGDsvDTANSQFFIMFADGGSLDNQYTVIGEVVQGMDVVDKLKKAppGSSGGTVTDP 174
Cdd:PTZ00060 102 TD--ENFKLKHDQPGLLSMANAGP--NTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKE--GTQSGYPKKP 173
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 33-163 7.07e-19

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: 79.31  E-value: 7.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  33 VIDSTKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNFNGTGGSKYPNLKQEFSK------- 105
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQLYGRQARffepeil 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517269171 106 ---VHFARGIVGMARRGDsvDTANSQFFIMFADG-GSLDNQYTVIGEVVQGMDVVDKLKKAP 163
Cdd:cd01921   81 pllKHSKKGTVSMVNAGD--NLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKINDAI 140
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 39-167 1.42e-18

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 78.72  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  39 GRIVIKLRPDLAPQHAERIKQLA-----REGF---YNNVPFHRVMDGFMAQTGDGQNFNGTG-----GSKYPNlkQEFSK 105
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGcvsiyGSKFED--ENFIA 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517269171 106 VHFARGIVGMARRGdsVDTANSQFFIMFADGGSLDNQYTVIGEVV-QGMDVVDKLKKAPPGSS 167
Cdd:PLN03149 111 KHTGPGLLSMANSG--PNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPN 171
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 37-160 8.10e-13

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: 63.23  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269171  37 TKGRIVIKLRPDLAPQHAERIKQLAREGFYNNVPFHRVMDGFMAQTGDGQNFNGTG------------------GSKYP- 97
Cdd:cd01924    5 DNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFpdpetgksrtipleikpeGQKQPv 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517269171  98 ---------NLKQEFSKVHFARGIVGMARRGDSVDTANSQFFIMFADGGS-------LDNQYTVIGEVVQGMDVVDKLK 160
Cdd:cd01924   85 ygktleeagRYDEQPVLPFNAFGAIAMARTEFDPNSASSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTDGLDILRELK 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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