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Conserved domains on  [gi|1370484230|ref|XP_024309307|]
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NK-tumor recognition protein isoform X1 [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 ...
 7-174 8.62e-83

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: 268.36  E-value: 8.62e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYA 166
Cdd:cd01926     78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                   ....*...
gi 1370484230  167 DVRVIDCG 174
Cdd:cd01926    157 KVVIADCG 164
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 799-988 5.02e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.90  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230  799 SESRSSLDYSSDSEQSSVQATQSAQEKEKQGQMERTHNKQEKNRGEEKSKSERECPHSKKRTLKENLSDHLRNGSKPKRK 878
Cdd:NF033609   696 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230  879 NYAGSKWDSESNSERDVTKNSKNDSHPSSDKE---EGEATSDSESEVSEIHIKVKPTTKSSTNTSLPDDNGAWKSSKQRT 955
Cdd:NF033609   776 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 855

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370484230  956 STSDSEG-SCSNSENNRGKPQKHKHGSKENLKRE 988
Cdd:NF033609   856 SESDSNSdSESGSNNNVVPPNSPKNGTNASNKNE 889
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-174 8.62e-83

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: 268.36  E-value: 8.62e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYA 166
Cdd:cd01926     78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                   ....*...
gi 1370484230  167 DVRVIDCG 174
Cdd:cd01926    157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-176 5.81e-69

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 229.73  E-value: 5.81e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230    6 RPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGlgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKG 85
Cdd:PTZ00060    15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   86 GESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPY 165
Cdd:PTZ00060    93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPK 171

                          170
                   ....*....|.
gi 1370484230  166 ADVRVIDCGVL 176
Cdd:PTZ00060   172 KPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 13-175 4.46e-58

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: 197.09  E-value: 4.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   13 IEINREpvGRIMFQLFSDICPKTCKNFLCLCsgekglgkTTGKklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYgg 92
Cdd:pfam00160    1 IETNGL--GRIVIELFGDKAPKTVENFLQLC--------KKGF---YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   93 YFKDENFI--LKHDRaFLLSMANRG--KHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYADV 168
Cdd:pfam00160   65 PIPDEIFPllLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPV 142


                   ....*..
gi 1370484230  169 RVIDCGV 175
Cdd:pfam00160  143 KILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 21-171 1.03e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 159.18  E-value: 1.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   21 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFsEGNGKGGEsiygGY-FKDENF 99
Cdd:COG0652     16 GDIVIELFPDKAPKTVANFVSLA--KEGF---------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP----GYtIPDEFD 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484230  100 I-LKHDRAfLLSMAN-RGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVI 171
Cdd:COG0652     80 PgLKHKRG-TLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 799-988 5.02e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.90  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230  799 SESRSSLDYSSDSEQSSVQATQSAQEKEKQGQMERTHNKQEKNRGEEKSKSERECPHSKKRTLKENLSDHLRNGSKPKRK 878
Cdd:NF033609   696 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230  879 NYAGSKWDSESNSERDVTKNSKNDSHPSSDKE---EGEATSDSESEVSEIHIKVKPTTKSSTNTSLPDDNGAWKSSKQRT 955
Cdd:NF033609   776 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 855

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370484230  956 STSDSEG-SCSNSENNRGKPQKHKHGSKENLKRE 988
Cdd:NF033609   856 SESDSNSdSESGSNNNVVPPNSPKNGTNASNKNE 889
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-174 8.62e-83

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: 268.36  E-value: 8.62e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYA 166
Cdd:cd01926     78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                   ....*...
gi 1370484230  167 DVRVIDCG 174
Cdd:cd01926    157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-176 5.81e-69

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 229.73  E-value: 5.81e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230    6 RPQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGlgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKG 85
Cdd:PTZ00060    15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   86 GESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPY 165
Cdd:PTZ00060    93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPK 171

                          170
                   ....*....|.
gi 1370484230  166 ADVRVIDCGVL 176
Cdd:PTZ00060   172 KPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 20-172 1.18e-60

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: 204.42  E-value: 1.18e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   20 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDFSegNGKGGESIYGGYFKDENF 99
Cdd:cd00317      6 KGRIVIELYGDEAPKTVENFLSLARGGF-----------YDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENF 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484230  100 ILK-HDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 172
Cdd:cd00317     73 PLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 13-175 4.46e-58

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: 197.09  E-value: 4.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   13 IEINREpvGRIMFQLFSDICPKTCKNFLCLCsgekglgkTTGKklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYgg 92
Cdd:pfam00160    1 IETNGL--GRIVIELFGDKAPKTVENFLQLC--------KKGF---YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF-- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   93 YFKDENFI--LKHDRaFLLSMANRG--KHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAAsRPYADV 168
Cdd:pfam00160   65 PIPDEIFPllLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPV 142


                   ....*..
gi 1370484230  169 RVIDCGV 175
Cdd:pfam00160  143 KILSCGV 149
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 7-174 1.01e-56

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 194.67  E-value: 1.01e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230    7 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKglgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 86
Cdd:PLN03149    19 PVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   87 ESIYGGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVI-SGFEVIEQIENLKTDAASRPY 165
Cdd:PLN03149    96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPK 175


                   ....*....
gi 1370484230  166 ADVRVIDCG 174
Cdd:PLN03149   176 LACVISECG 184
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 20-172 3.53e-53

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: 183.02  E-value: 3.53e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   20 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKDENF 99
Cdd:cd01928      9 LGDIKIELFCDDCPKACENFLALCASGY-----------YNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFR 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484230  100 -ILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 172
Cdd:cd01928     77 eTLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 21-172 1.56e-50

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: 175.34  E-value: 1.56e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   21 GRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKDE-NF 99
Cdd:cd01927      7 GDIHIRLFPEEAPKTVENFTTHA-----------RNGYYNNTIFHRVIKGFMIQTGD-PTGDGTGGESIWGKEFEDEfSP 74

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370484230  100 ILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVID 172
Cdd:cd01927     75 SLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 21-176 7.27e-49

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: 171.06  E-value: 7.27e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   21 GRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYGGYFKDE-NF 99
Cdd:cd01923      9 GDLNLELHCDKAPKACENFIKLC-----------KKGYYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKP 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370484230  100 ILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVIDCGVL 176
Cdd:cd01923     77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSVF 153
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 21-171 1.03e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 159.18  E-value: 1.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   21 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFsEGNGKGGEsiygGY-FKDENF 99
Cdd:COG0652     16 GDIVIELFPDKAPKTVANFVSLA--KEGF---------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP----GYtIPDEFD 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370484230  100 I-LKHDRAfLLSMAN-RGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRVI 171
Cdd:COG0652     80 PgLKHKRG-TLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 20-171 1.79e-43

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: 155.00  E-value: 1.79e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   20 VGRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKDE-N 98
Cdd:cd01922      6 MGEITLELYWNHAPKTCKNFYELA-----------KRGYYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiH 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370484230   99 FILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDaASRPYADVRVI 171
Cdd:cd01922     74 PELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKIL 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 20-176 9.04e-37

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: 136.71  E-value: 9.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   20 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYGGYFKDE-N 98
Cdd:cd01925     14 AGDIDIELWSKEAPKACRNFIQLCLEGY-----------YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfH 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   99 FILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVI--SGFEVIEqIENLKTDAASRPYADVRVIDCGVL 176
Cdd:cd01925     82 SRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgdTIYNLLK-LAEVETDKDERPVYPPKITSVEVL 160
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 20-170 1.21e-32

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: 124.76  E-value: 1.21e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   20 VGRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGG------- 92
Cdd:cd01921      6 LGDLVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQlygrqar 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   93 YFKDE-NFILKHDRAFLLSMANRGKHTNGSQFFIT-TKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRV 170
Cdd:cd01921     74 FFEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 12-176 1.95e-24

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 104.18  E-value: 1.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   12 DIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGKTTGKKLCYKGSTFHRV-VKNFMIQGGDFSEGNgkggESIY 90
Cdd:PTZ00221    58 DISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVdRNNNIIVLGELDSFN----VSST 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   91 GGYFKDENFILKHDRAFLLSMANRGKHTNGSQFFITTKPAPHLDGVHVVFGLVISGFEVIEQIENLKTDAASRPYADVRV 170
Cdd:PTZ00221   134 GTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLPVTV 213


                   ....*.
gi 1370484230  171 IDCGVL 176
Cdd:PTZ00221   214 SFCGAL 219
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 21-172 3.25e-19

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: 85.96  E-value: 3.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   21 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFSEGNGK-------GGESIYGgy 93
Cdd:cd01920      7 GDIVVELYDDKAPITVENFLAYV--RKGF---------YDNTIFHRVISGFVIQGGGFTPDLAQketlkpiKNEAGNG-- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   94 fkdenfiLKHDRAfLLSMA-NRGKHTNGSQFFITTKPAPHLD-----GVHVVFGLVISGFEVIEQIENLKTdAASRPYAD 167
Cdd:cd01920     74 -------LSNTRG-TIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVET-YSFGSYQD 144


                   ....*
gi 1370484230  168 VRVID 172
Cdd:cd01920    145 VPVQD 149
PRK10903 PRK10903
peptidylprolyl isomerase A;
20-182 2.81e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 58.32  E-value: 2.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   20 VGRIMFQLFSDICPKTCKNFL-CLCSGekglgkttgkklCYKGSTFHRVVKNFMIQGGDFsegNGKGGESIYGGYFKDE- 97
Cdd:PRK10903    37 AGNIELELNSQKAPVSVKNFVdYVNSG------------FYNNTTFHRVIPGFMIQGGGF---TEQMQQKKPNPPIKNEa 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   98 NFILKHDRAfLLSMANRG-KHTNGSQFFITTKPAPHLD------GvHVVFGLVISGFEVIEQIENLKTDAASrPYADVRV 170
Cdd:PRK10903   102 DNGLRNTRG-TIAMARTAdKDSATSQFFINVADNAFLDhgqrdfG-YAVFGKVVKGMDVADKISQVPTHDVG-PYQNVPS 178

                          170
                   ....*....|..
gi 1370484230  171 IDCGVLATKSIK 182
Cdd:PRK10903   179 KPVVILSAKVLP 190
PRK10791 PRK10791
peptidylprolyl isomerase B;
21-158 6.67e-09

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 56.39  E-value: 6.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   21 GRIMFQLFSDICPKTCKNFLCLCSgeKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFSEG-NGKGGESIyggyFKDE-N 98
Cdd:PRK10791     9 GDIVIKTFDDKAPETVKNFLDYCR--EGF---------YNNTIFHRVINGFMIQGGGFEPGmKQKATKEP----IKNEaN 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370484230   99 FILKHDRAFLLSMANRGKHTNGSQFFITTKP-------APHLDGV-HVVFGLVISGFEVIEQIENLKT 158
Cdd:PRK10791    74 NGLKNTRGTLAMARTQAPHSATAQFFINVVDndflnfsGESLQGWgYCVFAEVVEGMDVVDKIKGVAT 141
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 33-154 7.79e-09

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: 56.68  E-value: 7.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230   33 PKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDfSEGNGKG---------------------GESIYG 91
Cdd:cd01924     19 PVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGD-PQGKNPGfpdpetgksrtipleikpegqKQPVYG 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370484230   92 ------GYFKDENFILKHDrAFLLSMANRGKHTNG--SQFFI-------TTKPAPHLDGVHVVFGLVISGFEVIEQIE 154
Cdd:cd01924     87 ktleeaGRYDEQPVLPFNA-FGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 799-988 5.02e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.90  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230  799 SESRSSLDYSSDSEQSSVQATQSAQEKEKQGQMERTHNKQEKNRGEEKSKSERECPHSKKRTLKENLSDHLRNGSKPKRK 878
Cdd:NF033609   696 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 775

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370484230  879 NYAGSKWDSESNSERDVTKNSKNDSHPSSDKE---EGEATSDSESEVSEIHIKVKPTTKSSTNTSLPDDNGAWKSSKQRT 955
Cdd:NF033609   776 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 855

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1370484230  956 STSDSEG-SCSNSENNRGKPQKHKHGSKENLKRE 988
Cdd:NF033609   856 SESDSNSdSESGSNNNVVPPNSPKNGTNASNKNE 889
 
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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