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Conserved domains on  [gi|1443087444|ref|XP_025882330|]
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peptidyl-prolyl cis-trans isomerase CYP40 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

CYP40/PPID family peptidylprolyl isomerase( domain architecture ID 11549474)

CYP40/PPID family cyclophilin-type peptidylprolyl isomerase contains tetratricopeptide (TPR) repeats and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins; similar to peptidyl-prolyl cis-trans isomerase D (PPID), or cyclophilin-40 (CYP40), that may also act as a co-chaperone in HSP90 complexes

CATH:  2.40.100.10|1.25.40.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413|GO:0005515
PubMed:  11377203|14731520|15998457|15353287|22404999|21153002

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 26-193 3.87e-104

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: 304.56  E-value: 3.87e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  26 PRCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGVGavtGKHLHYKGSCFHRVIKGFMVQGGDITAGDGTGG 105
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 106 ESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEaDRPTS 185
Cdd:cd01926    78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKK 156


                  ....*...
gi 1443087444 186 DVEIVDCG 193
Cdd:cd01926   157 KVVIADCG 164
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
245-363 1.49e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.09  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 245 FKKQDYKAALRKYRKALRyldvcwekedIDEEKSSALrktksiilTNSSACKLKLGDLKGALLDADFALRESEGNAKAFF 324
Cdd:COG0457    19 RRLGRYEEAIEDYEKALE----------LDPDDAEAL--------YNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1443087444 325 RQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAA 363
Cdd:COG0457    81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLA 119
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 26-193 3.87e-104

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: 304.56  E-value: 3.87e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  26 PRCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGVGavtGKHLHYKGSCFHRVIKGFMVQGGDITAGDGTGG 105
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 106 ESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEaDRPTS 185
Cdd:cd01926    78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKK 156


                  ....*...
gi 1443087444 186 DVEIVDCG 193
Cdd:cd01926   157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 24-195 2.53e-88

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 265.17  E-value: 2.53e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  24 KNPRCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGvgAVTGKHLHYKGSCFHRVIKGFMVQGGDITAGDGT 103
Cdd:PTZ00060   14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 104 GGESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHapVG-EADR 182
Cdd:PTZ00060   92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGtQSGY 169

                         170
                  ....*....|...
gi 1443087444 183 PTSDVEIVDCGEL 195
Cdd:PTZ00060  170 PKKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 39-194 8.20e-60

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: 190.54  E-value: 8.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  39 EGRIVIELYASVVPRTAENFRALCTgeKGvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGlkFEDENF 118
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 119 V--LKHERkGMLSMANSG--PNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEaDRPTSDVEIVDCGE 194
Cdd:pfam00160  72 PllLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 40-190 1.62e-57

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 184.99  E-value: 1.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCtgEKGvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGEsiyGLKFEDENFV 119
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443087444 120 -LKHERkGMLSMANS-GPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDVEIV 190
Cdd:COG0652    81 gLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
245-363 1.49e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.09  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 245 FKKQDYKAALRKYRKALRyldvcwekedIDEEKSSALrktksiilTNSSACKLKLGDLKGALLDADFALRESEGNAKAFF 324
Cdd:COG0457    19 RRLGRYEEAIEDYEKALE----------LDPDDAEAL--------YNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1443087444 325 RQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAA 363
Cdd:COG0457    81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLA 119
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 320-353 1.50e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 41.66  E-value: 1.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1443087444  320 AKAFFRQGQAHIALNDIDAAVESFKHALELEPSD 353
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
320-353 2.03e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 41.25  E-value: 2.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1443087444 320 AKAFFRQGQAHIALNDIDAAVESFKHALELEPSD 353
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 300-357 9.63e-05

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 43.77  E-value: 9.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087444 300 GDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIK 357
Cdd:cd24142    14 GNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDGGYEK 71
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 297-394 2.17e-03

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 39.77  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 297 LKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKIADRRNQERK 376
Cdd:PLN03088   47 IKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAEEEKDLVQ 126

                          90
                  ....*....|....*...
gi 1443087444 377 AfARMFQPSGKSDKDNEE 394
Cdd:PLN03088  127 P-VPSDLPSSVTAPPVEE 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 300-391 3.14e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 300 GDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKiadrRNQERKAFA 379
Cdd:TIGR02917  36 NKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYPKNQVLPLLARAYLL----QGKFQQVLD 111

                          90
                  ....*....|..
gi 1443087444 380 RMFQPSGKSDKD 391
Cdd:TIGR02917 112 ELPGKTLLDDEG 123
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 26-193 3.87e-104

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: 304.56  E-value: 3.87e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  26 PRCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGVGavtGKHLHYKGSCFHRVIKGFMVQGGDITAGDGTGG 105
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 106 ESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEaDRPTS 185
Cdd:cd01926    78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKK 156


                  ....*...
gi 1443087444 186 DVEIVDCG 193
Cdd:cd01926   157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 24-195 2.53e-88

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 265.17  E-value: 2.53e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  24 KNPRCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGvgAVTGKHLHYKGSCFHRVIKGFMVQGGDITAGDGT 103
Cdd:PTZ00060   14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 104 GGESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHapVG-EADR 182
Cdd:PTZ00060   92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGtQSGY 169

                         170
                  ....*....|...
gi 1443087444 183 PTSDVEIVDCGEL 195
Cdd:PTZ00060  170 PKKPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 24-195 9.34e-74

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 227.80  E-value: 9.34e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  24 KNPRCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGVGavtGKHLHYKGSCFHRVIKGFMVQGGDITAGDGT 103
Cdd:PLN03149   17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKA---GLPQGYKGCQFHRVIKDFMIQGGDFLKGDGT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 104 GGESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVI-KGMGVVRSVEHAPVGEADR 182
Cdd:PLN03149   94 GCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNR 173

                         170
                  ....*....|...
gi 1443087444 183 PTSDVEIVDCGEL 195
Cdd:PLN03149  174 PKLACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 29-191 2.00e-68

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: 212.89  E-value: 2.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  29 FMDVSIGgeiegRIVIELYASVVPRTAENFRALCTGEkgvgavtgkhlHYKGSCFHRVIKGFMVQGGDITAGDGTGgeSI 108
Cdd:cd00317     1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLARGG-----------FYDGTTFHRVIPGFMIQGGDPTGTGGGG--SG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 109 YGLKFEDENFVLK-HERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDV 187
Cdd:cd00317    63 PGYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPV 142


                  ....
gi 1443087444 188 EIVD 191
Cdd:cd00317   143 TISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 39-194 8.20e-60

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: 190.54  E-value: 8.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  39 EGRIVIELYASVVPRTAENFRALCTgeKGvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGlkFEDENF 118
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 119 V--LKHERkGMLSMANSG--PNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEaDRPTSDVEIVDCGE 194
Cdd:pfam00160  72 PllLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 40-191 1.20e-57

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: 185.33  E-value: 1.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCTGEkgvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGLKFEDENF- 118
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALCASG-----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFRe 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443087444 119 VLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDVEIVD 191
Cdd:cd01928    78 TLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 40-191 1.30e-57

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: 184.97  E-value: 1.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCtgekgvgavtgKHLHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGLKFEDE-NF 118
Cdd:cd01927     7 GDIHIRLFPEEAPKTVENFTTHA-----------RNGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443087444 119 VLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDVEIVD 191
Cdd:cd01927    75 SLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 40-190 1.62e-57

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 184.99  E-value: 1.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCtgEKGvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGEsiyGLKFEDENFV 119
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443087444 120 -LKHERkGMLSMANS-GPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDVEIV 190
Cdd:COG0652    81 gLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 40-191 1.30e-53

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: 175.30  E-value: 1.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCtgekgvgavtgKHLHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGLKFEDE-NF 118
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC-----------KKGYYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKP 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443087444 119 VLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDVEIVD 191
Cdd:cd01923    77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIED 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 40-190 4.53e-50

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: 165.40  E-value: 4.53e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCTgeKGvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGLKFEDE-NF 118
Cdd:cd01922     7 GEITLELYWNHAPKTCKNFYELAK--RG---------YYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443087444 119 VLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVgEADRPTSDVEIV 190
Cdd:cd01922    75 ELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQT-QTDRPIDEVKIL 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 40-201 1.62e-39

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: 138.64  E-value: 1.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCTGEkgvgavtgkhlHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGLKFEDE-NF 118
Cdd:cd01925    15 GDIDIELWSKEAPKACRNFIQLCLEG-----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 119 VLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKG--MGVVRSVEhAPVGEADRPTSDVEIVDCGELP 196
Cdd:cd01925    83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDtiYNLLKLAE-VETDKDERPVYPPKITSVEVLE 161


                  ....*
gi 1443087444 197 EGADD 201
Cdd:cd01925   162 NPFDD 166
PTZ00221 PTZ00221
cyclophilin; Provisional
 27-195 8.40e-36

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 131.53  E-value: 8.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  27 RCFMDVSIGGEIEGRIVIELYASVVPRTAENFRALCTGEKGVGAVTGKHLHYKGSCFHRVIKgfmvQGGDITAGD-GTGG 105
Cdd:PTZ00221   54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVDR----NNNIIVLGElDSFN 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 106 ESIYGLKFEDENFVLKHERKGMLSMANSGPNTNGSQFFITTTRTPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTS 185
Cdd:PTZ00221  130 VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLL 209

                         170
                  ....*....|
gi 1443087444 186 DVEIVDCGEL 195
Cdd:PTZ00221  210 PVTVSFCGAL 219
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 39-189 2.15e-34

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: 125.15  E-value: 2.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  39 EGRIVIELYASVVPRTAENFRALCtgekgvgavtgKHLHYKGSCFHRVIKGFMVQGGDITaGDGTGGESIYGLK------ 112
Cdd:cd01921     6 LGDLVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqar 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 113 -FEDE-NFVLKHERKGMLSMANSGPNTNGSQFFITTTR-TPHLDGKHVVFGRVIKGMGVVRSVEHAPVGEADRPTSDVEI 189
Cdd:cd01921    74 fFEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 40-189 3.39e-21

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: 89.04  E-value: 3.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCtgEKGvgavtgkhlHYKGSCFHRVIKGFMVQGGDITA-------GDGTGGESIYGLK 112
Cdd:cd01920     7 GDIVVELYDDKAPITVENFLAYV--RKG---------FYDNTIFHRVISGFVIQGGGFTPdlaqketLKPIKNEAGNGLS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 113 fedenfvlkhERKGMLSMANSG-PNTNGSQFFITTTRTPHLD-----GKHVVFGRVIKGMGVVRSVEHAPVGE----ADR 182
Cdd:cd01920    76 ----------NTRGTIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSfgsyQDV 145


                  ....*..
gi 1443087444 183 PTSDVEI 189
Cdd:cd01920   146 PVQDVII 152
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 41-173 3.48e-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: 67.47  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  41 RIVIELYASvvPRTAENFRALCtgEKGVgavtgkhlhYKGSCFHRVIKGFMVQGGD-----------------------I 97
Cdd:cd01924    10 TIVLDGYNA--PVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGDpqgknpgfpdpetgksrtipleiK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  98 TAGDgtgGESIYGLKFE-----DENFVLKHERKGMLSMANS--GPNTNGSQFFI-------TTTRTPHLDGKHVVFGRVI 163
Cdd:cd01924    77 PEGQ---KQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVT 153

                         170
                  ....*....|
gi 1443087444 164 KGMGVVRSVE 173
Cdd:cd01924   154 DGLDILRELK 163
PRK10903 PRK10903
peptidylprolyl isomerase A;
39-176 3.85e-13

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 67.56  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  39 EGRIVIELYASVVPRTAENFralctgekgVGAVTGKHlhYKGSCFHRVIKGFMVQGGDITAgDGTGGESIYGLKFEDENf 118
Cdd:PRK10903   37 AGNIELELNSQKAPVSVKNF---------VDYVNSGF--YNNTTFHRVIPGFMIQGGGFTE-QMQQKKPNPPIKNEADN- 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443087444 119 VLKHERkGMLSMA-NSGPNTNGSQFFITTTRTPHLD-GK----HVVFGRVIKGMGVVRSVEHAP 176
Cdd:PRK10903  104 GLRNTR-GTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVP 166
PRK10791 PRK10791
peptidylprolyl isomerase B;
40-189 6.23e-11

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 60.62  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444  40 GRIVIELYASVVPRTAENFRALCTGEkgvgavtgkhlHYKGSCFHRVIKGFMVQGGDITAGdGTGGESIYGLKFEDENFv 119
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYCREG-----------FYNNTIFHRVINGFMIQGGGFEPG-MKQKATKEPIKNEANNG- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 120 LKHERkGMLSMANSG-PNTNGSQFFITTT-------RTPHLDG-KHVVFGRVIKGMGVVRSVEHAPVGEA----DRPTSD 186
Cdd:PRK10791   76 LKNTR-GTLAMARTQaPHSATAQFFINVVdndflnfSGESLQGwGYCVFAEVVEGMDVVDKIKGVATGRSgmhqDVPKED 154


                  ...
gi 1443087444 187 VEI 189
Cdd:PRK10791  155 VII 157
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
245-363 1.49e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.09  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 245 FKKQDYKAALRKYRKALRyldvcwekedIDEEKSSALrktksiilTNSSACKLKLGDLKGALLDADFALRESEGNAKAFF 324
Cdd:COG0457    19 RRLGRYEEAIEDYEKALE----------LDPDDAEAL--------YNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1443087444 325 RQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAA 363
Cdd:COG0457    81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLA 119
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 294-380 3.94e-08

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 52.27  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 294 ACKLKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKiADRRNQ 373
Cdd:COG5010    62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS-LGQDDE 140


                  ....*..
gi 1443087444 374 ERKAFAR 380
Cdd:COG5010   141 AKAALQR 147
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 239-383 5.86e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 51.35  E-value: 5.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 239 AFGNNNFKKQDYKAALRKYRKALRyldvcwekediDEEKSSALRKTKSIILtnssackLKLGDLKGALLDADFALRESEG 318
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALE-----------LDPDNPEAFALLGEIL-------LQLGDLDEAIVLLHEALELDPD 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443087444 319 NAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKiADRRNQERKAFARMFQ 383
Cdd:COG4783    71 EPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA-LGRPDEAIAALEKALE 134
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
241-390 7.83e-08

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 52.61  E-value: 7.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 241 GNNNFKKQDYKAALRKYRKALRyldvcwekedIDEEKSSALRktksiiltNSSACKLKLGDLKGALLDADFALRESEGNA 320
Cdd:COG4785    80 GVAYDSLGDYDLAIADFDQALE----------LDPDLAEAYN--------NRGLAYLLLGDYDAALEDFDRALELDPDYA 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443087444 321 KAFFRQGQAHIALNDIDAAVESFKHALELEPSD--GGIKRELAAAKKKIADRRNQERKAFARMFQPSGKSDK 390
Cdd:COG4785   142 YAYLNRGIALYYLGRYELAIADLEKALELDPNDpeRALWLYLAERKLDPEKALALLLEDWATAYLLQGDTEE 213
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 213-351 8.00e-08

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 51.50  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 213 YPDWPNDLDEKPMEVSWWMDAVESAKAFGNNNFKKQDYKAALRKYRKALryldvcwekedideekssALRKTKSIILTNS 292
Cdd:COG5010    33 GANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQAL------------------QLDPNNPELYYNL 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1443087444 293 SACKLKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEP 351
Cdd:COG5010    95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
220-354 2.75e-07

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 51.07  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 220 LDEKPMEVSWWMDAVESAKAFGNNNFKKQDYKAALRKYRKALRYL-DVCWEKEDIDEEKSSALRKTKSIILTNSSA-CKL 297
Cdd:COG4785     5 ALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAaAALAAAALAAERIDRALALPDLAQLYYERGvAYD 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1443087444 298 KLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDG 354
Cdd:COG4785    85 SLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYA 141
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 252-379 3.03e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.27  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 252 AALRKYRKALRYLdvcwekedideEKSSALRKTKSIILTNSSACKLKLGDLKGALLDADFALRESEGNAKAFFRQGQAHI 331
Cdd:COG2956   121 EQEGDWEKAIEVL-----------ERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYL 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1443087444 332 ALNDIDAAVESFKHALELEPSDGGIKRELAaakkKIADRRNQERKAFA 379
Cdd:COG2956   190 EQGDYEEAIAALERALEQDPDYLPALPRLA----ELYEKLGDPEEALE 233
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
241-380 4.58e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 241 GNNNFKKQDYKAALRKYRKALRyLD------------VCWEKEDIDE-----EKSSALRKTKSIILTNSSACKLKLGDLK 303
Cdd:COG0457    49 GLAYLRLGRYEEALADYEQALE-LDpddaealnnlglALQALGRYEEaledyDKALELDPDDAEALYNLGLALLELGRYD 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443087444 304 GALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKIADRRNQERKAFAR 380
Cdd:COG0457   128 EAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALE 204
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 312-363 4.70e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 48.46  E-value: 4.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443087444 312 ALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAA 363
Cdd:COG4235     9 ALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA 60
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
289-363 8.87e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.62  E-value: 8.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443087444 289 LTNSSACKLKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAA 363
Cdd:COG0457    11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLA 85
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 297-379 2.91e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 46.15  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 297 LKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAkkkiADRRNQERK 376
Cdd:COG4235    28 LRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA----AFQQGDYAE 103


                  ...
gi 1443087444 377 AFA 379
Cdd:COG4235   104 AIA 106
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 241-363 6.42e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.38  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 241 GNNNFKKQDYKAALRKYRKALRYldvcwEKEDIDeekssalrktksiILTNSSACKLKLGDLKGALLDADFALRESEGNA 320
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRL-----DPDNAD-------------ALLDLAEALLAAGDTEEAEELLERALALDPDNP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1443087444 321 KAFFRQGQAHIALNDIDAAVESFKHALELEPSD---GGIKRELAAA 363
Cdd:COG4235    86 EALYLLGLAAFQQGDYAEAIAAWQKLLALLPADapaRLLEASIAEA 131
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
297-377 8.19e-06

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.01  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 297 LKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVEsFKHALELEPSDGGIKRELAaakkKIADRRNQERK 376
Cdd:COG3063     3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLA----ELLLELGDYDE 77


                  .
gi 1443087444 377 A 377
Cdd:COG3063    78 A 78
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 232-379 8.48e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.03  E-value: 8.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 232 DAVESAKAFGNNNFKKQDYKAALRKYRKALryldvcwekeDIDEEKSSALRKtksIILTNssackLKLGDLKGALLDADF 311
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLL----------ERDPDRAEALLE---LAQDY-----LKAGLLDRAEELLEK 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087444 312 ALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAaakkKIADRRNQERKAFA 379
Cdd:COG2956   102 LLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELA----ELYLEQGDYDEAIE 165
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 241-375 9.14e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.68  E-value: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 241 GNNNFKKQDYKAALRKYRKALRYldvcwEKEDIDeekssalrktksiILTNSSACKLKLGDLKGALLDADFALRESEGNA 320
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALAL-----NPDFAE-------------AYLNLGEALRRLGRLEEAIAALRRALELDPDNA 180

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443087444 321 KAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKIADRRNQER 375
Cdd:COG3914   181 EALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDR 235
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
245-352 1.04e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 43.62  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 245 FKKQDYKAALRKYRKALRyldvcwekedIDEEKSSALrktksiilTNSSACKLKLGDLKGALlDADFALRESEGNAKAFF 324
Cdd:COG3063     3 LKLGDLEEAEEYYEKALE----------LDPDNADAL--------NNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALL 63

                          90       100
                  ....*....|....*....|....*...
gi 1443087444 325 RQGQAHIALNDIDAAVESFKHALELEPS 352
Cdd:COG3063    64 NLAELLLELGDYDEALAYLERALELDPS 91
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 320-353 1.50e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 41.66  E-value: 1.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1443087444  320 AKAFFRQGQAHIALNDIDAAVESFKHALELEPSD 353
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
320-353 2.03e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 41.25  E-value: 2.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1443087444 320 AKAFFRQGQAHIALNDIDAAVESFKHALELEPSD 353
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR_8 pfam13181
Tetratricopeptide repeat;
320-352 3.99e-05

Tetratricopeptide repeat;


Pssm-ID: 404131 [Multi-domain]  Cd Length: 33  Bit Score: 40.07  E-value: 3.99e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1443087444 320 AKAFFRQGQAHIALNDIDAAVESFKHALELEPS 352
Cdd:pfam13181   1 AEAYYNLGLIYLKLGDYEEAKEYYEKALELDPD 33
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 320-351 5.69e-05

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 39.81  E-value: 5.69e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1443087444 320 AKAFFRQGQAHIALNDIDAAVESFKHALELEP 351
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDP 32
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 300-357 9.63e-05

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 43.77  E-value: 9.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087444 300 GDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIK 357
Cdd:cd24142    14 GNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDGGYEK 71
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 245-380 3.33e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 245 FKKQDYKAALRKYRKALryldvcwekeDIDEEKSSALRKTKSIiltnssacKLKLGDLKGALLDADFALRESEGNAKAFF 324
Cdd:COG2956   155 LEQGDYDEAIEALEKAL----------KLDPDCARALLLLAEL--------YLEQGDYEEAIAALERALEQDPDYLPALP 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087444 325 RQGQAHIALNDIDAAVESFKHALELEPSDGGIKR--ELAAAKKKIADRRNQERKAFAR 380
Cdd:COG2956   217 RLAELYEKLGDPEEALELLRKALELDPSDDLLLAlaDLLERKEGLEAALALLERQLRR 274
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 297-353 1.16e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1443087444 297 LKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSD 353
Cdd:COG3914    89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDF 145
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 297-394 2.17e-03

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 39.77  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 297 LKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKIADRRNQERK 376
Cdd:PLN03088   47 IKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAEEEKDLVQ 126

                          90
                  ....*....|....*...
gi 1443087444 377 AfARMFQPSGKSDKDNEE 394
Cdd:PLN03088  127 P-VPSDLPSSVTAPPVEE 143
TPR_19 pfam14559
Tetratricopeptide repeat;
300-367 2.49e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.02  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087444 300 GDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDggikRELAAAKKKI 367
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDD----PRYAALLAKL 65
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 300-391 3.14e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 300 GDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKKKiadrRNQERKAFA 379
Cdd:TIGR02917  36 NKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYPKNQVLPLLARAYLL----QGKFQQVLD 111

                          90
                  ....*....|..
gi 1443087444 380 RMFQPSGKSDKD 391
Cdd:TIGR02917 112 ELPGKTLLDDEG 123
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 297-396 4.47e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.30  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087444 297 LKLGDLKGALLDADFALRESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPSDGGIKRELAAAKkkiadRRNQERK 376
Cdd:TIGR02917 578 LGKGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAY-----AVMKNYA 652

                          90       100
                  ....*....|....*....|
gi 1443087444 377 AFARMFQPSGKSDKDNEESK 396
Cdd:TIGR02917 653 KAITSLKRALELKPDNTEAQ 672
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 303-352 6.60e-03

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 38.23  E-value: 6.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1443087444 303 KGALLDADFAL---------RESEGNAKAFFRQGQAHIALNDIDAAVESFKHALELEPS 352
Cdd:PLN03088   10 KEAFVDDDFALavdlytqaiDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPS 68
 
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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