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Conserved domains on  [gi|442631355|ref|NP_001261636|]
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cyclophilin 40, isoform D [Drosophila melanogaster]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11624249)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

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 ...
 15-181 5.66e-78

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: 237.54  E-value: 5.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  15 PLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGECGIGtlGKPLHYKGTKFHKIKRVFVVQSGDVVKNDGSSGE 94
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  95 SIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAP 174
Cdd:cd01926   79 SIYGEKFPDENFKLKHTGPGLLSMANAG-PNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                 ....*..
gi 442631355 175 IVIRDCG 181
Cdd:cd01926  158 VVIADCG 164
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
231-370 6.70e-10

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.86  E-value: 6.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKAnryyhylsrqfgwqqlnplkkhlvdedlLKVDGFSVVNNINAAAVDLKVGNYTSAREVCN 310
Cdd:COG0457   15 GLAYRRLGRYEEAIEDYEKA----------------------------LELDPDDAEALYNLGLAYLRLGRYEEALADYE 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQY 370
Cdd:COG0457   67 QALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRY 126
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 15-181 5.66e-78

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: 237.54  E-value: 5.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  15 PLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGECGIGtlGKPLHYKGTKFHKIKRVFVVQSGDVVKNDGSSGE 94
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  95 SIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAP 174
Cdd:cd01926   79 SIYGEKFPDENFKLKHTGPGLLSMANAG-PNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                 ....*..
gi 442631355 175 IVIRDCG 181
Cdd:cd01926  158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 12-183 4.59e-69

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 215.48  E-value: 4.59e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  12 STNPLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGEcGIGTLGKPLHYKGTKFHKIKRVFVVQSGDVVKNDGS 91
Cdd:PTZ00060  13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGD-KVGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  92 SGESIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDP 171
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAG-PNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYP 170

                        170
                 ....*....|..
gi 442631355 172 TAPIVIRDCGEI 183
Cdd:PTZ00060 171 KKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 27-182 3.72e-42

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: 144.71  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355   27 DAGRMIIELRKDVVPKTAENFRALCTGEcgigtlgkplHYKGTKFHKIKRVFVVQSGDVVkNDGSSGESIYGpvFDDENF 106
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442631355  107 ELS-HNEEGVVSMANYGK-PNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAPIVIRDCGE 182
Cdd:pfam00160  72 PLLlKHKRGALSMANTGPaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-178 3.22e-32

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 118.73  E-value: 3.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  13 TNPLVYLDISigkedAGRMIIELRKDVVPKTAENFRALCTGEcgigtlgkplHYKGTKFHkikRV---FVVQSGDVvKND 89
Cdd:COG0652    5 PNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLAKEG----------FYDGTIFH---RVipgFMIQGGDP-TGT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  90 GSSGEsiyGPVFDDENF-ELSHnEEGVVSMANYGKPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDE 168
Cdd:COG0652   66 GTGGP---GYTIPDEFDpGLKH-KRGTLAMARAQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP 141

                        170
                 ....*....|.
gi 442631355 169 GD-PTAPIVIR 178
Cdd:COG0652  142 GDgPLEPVVIE 152
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
231-370 6.70e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.86  E-value: 6.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKAnryyhylsrqfgwqqlnplkkhlvdedlLKVDGFSVVNNINAAAVDLKVGNYTSAREVCN 310
Cdd:COG0457   15 GLAYRRLGRYEEAIEDYEKA----------------------------LELDPDDAEALYNLGLAYLRLGRYEEALADYE 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQY 370
Cdd:COG0457   67 QALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRY 126
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 293-352 2.26e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 45.93  E-value: 2.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 293 AAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPE 352
Cdd:PLN03088  43 AQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPG 102
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 240-353 4.96e-04

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 42.28  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  240 YHEARAKYRKA---------NRYYHYLSRQFGWQQLNPLKKHlvdEDLLK-VDGFSVVNN--INAAAVDLKVGNYTSARE 307
Cdd:TIGR00990 310 YEEAARAFEKAldlgklgekEAIALNLRGTFKCLKGKHLEAL---ADLSKsIELDPRVTQsyIKRASMNLELGDPDKAEE 386

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 442631355  308 VCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:TIGR00990 387 DFDKALKLNSEDPDIYYHRAQLHFIKGEFAQAGKDYQKSIDLDPDF 432
TPR_1 pfam00515
Tetratricopeptide repeat;
320-353 2.40e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 2.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 442631355  320 SKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 320-353 6.24e-03

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: 33.96  E-value: 6.24e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 442631355   320 SKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 15-181 5.66e-78

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: 237.54  E-value: 5.66e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  15 PLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGECGIGtlGKPLHYKGTKFHKIKRVFVVQSGDVVKNDGSSGE 94
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  95 SIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAP 174
Cdd:cd01926   79 SIYGEKFPDENFKLKHTGPGLLSMANAG-PNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                 ....*..
gi 442631355 175 IVIRDCG 181
Cdd:cd01926  158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 12-183 4.59e-69

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 215.48  E-value: 4.59e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  12 STNPLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGEcGIGTLGKPLHYKGTKFHKIKRVFVVQSGDVVKNDGS 91
Cdd:PTZ00060  13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGD-KVGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  92 SGESIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDP 171
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAG-PNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYP 170

                        170
                 ....*....|..
gi 442631355 172 TAPIVIRDCGEI 183
Cdd:PTZ00060 171 KKPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 7-183 1.96e-57

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 185.42  E-value: 1.96e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355   7 LRAVKSTNPLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGECGIGtlGKPLHYKGTKFHKIKRVFVVQSGDVV 86
Cdd:PLN03149  11 LRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKA--GLPQGYKGCQFHRVIKDFMIQGGDFL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  87 KNDGSSGESIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVL-RGLGIVAEMEQNC 165
Cdd:PLN03149  89 KGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSG-PNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVA 167

                        170
                 ....*....|....*....
gi 442631355 166 TDEGD-PTAPIVIRDCGEI 183
Cdd:PLN03149 168 TGPNNrPKLACVISECGEM 186
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 27-182 3.72e-42

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: 144.71  E-value: 3.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355   27 DAGRMIIELRKDVVPKTAENFRALCTGEcgigtlgkplHYKGTKFHKIKRVFVVQSGDVVkNDGSSGESIYGpvFDDENF 106
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442631355  107 ELS-HNEEGVVSMANYGK-PNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAPIVIRDCGE 182
Cdd:pfam00160  72 PLLlKHKRGALSMANTGPaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 27-179 8.43e-38

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: 133.33  E-value: 8.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  27 DAGRMIIELRKDVVPKTAENFRALCTGEcgigtlgkplHYKGTKFHKIKRVFVVQSGDvVKNDGSSGESIYGPVFDDENF 106
Cdd:cd01928    8 NLGDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFR 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442631355 107 E-LSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGD-PTAPIVIRD 179
Cdd:cd01928   77 EtLKHDSRGVVSMANNG-PNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYrPLEEIRIKD 150
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-178 3.22e-32

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 118.73  E-value: 3.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  13 TNPLVYLDISigkedAGRMIIELRKDVVPKTAENFRALCTGEcgigtlgkplHYKGTKFHkikRV---FVVQSGDVvKND 89
Cdd:COG0652    5 PNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLAKEG----------FYDGTIFH---RVipgFMIQGGDP-TGT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  90 GSSGEsiyGPVFDDENF-ELSHnEEGVVSMANYGKPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDE 168
Cdd:COG0652   66 GTGGP---GYTIPDEFDpGLKH-KRGTLAMARAQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP 141

                        170
                 ....*....|.
gi 442631355 169 GD-PTAPIVIR 178
Cdd:COG0652  142 GDgPLEPVVIE 152
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 29-177 3.83e-30

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: 112.94  E-value: 3.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  29 GRMIIELRKDVVPKTAENFRALCtgecgigtlgKPLHYKGTKFHKIKRVFVVQSGDVVkNDGSSGESIYGPVFDDE-NFE 107
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA----------RNGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442631355 108 LSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGD-PTAPIVI 177
Cdd:cd01927   76 LKHDRPYTLSMANAG-PNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDrPYEDIKI 145
PTZ00221 PTZ00221
cyclophilin; Provisional
 1-181 4.93e-29

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 113.04  E-value: 4.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355   1 MEERKLLRAvkstnplvYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGECGIGT-LGKPLHYKGTKFHKIKRvfv 79
Cdd:PTZ00221  47 KEEQNSCRA--------FLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTnTGVKLDYLYTPVHHVDR--- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  80 vQSGDVVKND-GSSGESIYGPVFDDENFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIV 158
Cdd:PTZ00221 116 -NNNIIVLGElDSFNVSSTGTPIADEGYRHRHTERGLLTMISEG-PHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLL 193

                        170       180
                 ....*....|....*....|....
gi 442631355 159 AEMEQNCTDE-GDPTAPIVIRDCG 181
Cdd:PTZ00221 194 EKLESLPLDDvGRPLLPVTVSFCG 217
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 18-177 1.32e-26

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: 103.38  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  18 YLDISIGKedagrMIIELRKDVVPKTAENFRALCTGEcgigtlgkplHYKGTKFHKIKRVFVVQSGDVVKNdGSSGESIY 97
Cdd:cd01922    1 TLETTMGE-----ITLELYWNHAPKTCKNFYELAKRG----------YYNGTIFHRLIKDFMIQGGDPTGT-GRGGASIY 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  98 GPVFDDE-NFELSHNEEGVVSMANYGkPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAPIV 176
Cdd:cd01922   65 GKKFEDEiHPELKHTGAGILSMANAG-PNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVK 143


                 .
gi 442631355 177 I 177
Cdd:cd01922  144 I 144
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 29-178 8.90e-18

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: 80.08  E-value: 8.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  29 GRMIIELRKDVVPKTAENFRALCtgecgigtlgKPLHYKGTKFHKIKRVFVVQSGDvVKNDGSSGESIYGPV-------F 101
Cdd:cd01921    7 GDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQLygrqarfF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 102 DDE-NFELSHNEEGVVSMANyGKPNSNNSQFFIS-AAGCENLNGTNVVVGRVLRGLGIVAEM-EQNCTDEGDPTAPIVIR 178
Cdd:cd01921   76 EPEiLPLLKHSKKGTVSMVN-AGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRIK 154
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 27-179 3.75e-12

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: 63.62  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  27 DAGRMIIELRKDVVPKTAENFRALCtgECGigtlgkplHYKGTKFHKIKRVFVVQSGDVvkNDGSSGESIYGPVFDDENF 106
Cdd:cd01920    5 SLGDIVVELYDDKAPITVENFLAYV--RKG--------FYDNTIFHRVISGFVIQGGGF--TPDLAQKETLKPIKNEAGN 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 107 ELShNEEGVVSMANYGKPNSNNSQFFISAAGCENLNGTN-----VVVGRVLRGLGIVAEME-----QNCTDEGDPTAPIV 176
Cdd:cd01920   73 GLS-NTRGTIAMARTNAPDSATSQFFINLKDNASLDYQNeqwgyTVFGEVTEGMDVVDKIAgvetySFGSYQDVPVQDVI 151


                 ...
gi 442631355 177 IRD 179
Cdd:cd01920  152 IES 154
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
231-370 6.70e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.86  E-value: 6.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKAnryyhylsrqfgwqqlnplkkhlvdedlLKVDGFSVVNNINAAAVDLKVGNYTSAREVCN 310
Cdd:COG0457   15 GLAYRRLGRYEEAIEDYEKA----------------------------LELDPDDAEALYNLGLAYLRLGRYEEALADYE 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQY 370
Cdd:COG0457   67 QALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRY 126
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 231-353 5.94e-09

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: 53.86  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKAnryyhylsrqfgwQQLNPLkkhlvDEDLLkvdgfsvvnnINAAAVDLKVGNYTSAREVCN 310
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKA-------------LRLDPD-----NADAL----------LDLAEALLAAGDTEEAEELLE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:COG4235   76 RALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
231-381 1.22e-08

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 54.92  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKAnryyhylsrqfgwQQLNPlkkhlvdedllkvdGFSVVNNiNAAAVDLKVGNYTSAREVCN 310
Cdd:COG4785   80 GVAYDSLGDYDLAIADFDQA-------------LELDP--------------DLAEAYN-NRGLAYLLLGDYDAALEDFD 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNstkqlLAQYNRQQRNALKNL 381
Cdd:COG4785  132 RALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLY-----LAERKLDPEKALALL 197
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
290-372 1.48e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 55.01  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 290 INAAAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQ 369
Cdd:COG0457   12 NNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGR 91


                 ...
gi 442631355 370 YNR 372
Cdd:COG0457   92 YEE 94
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 222-381 1.54e-08

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: 55.12  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 222 ELLTGIRQSGNHFYQLGRYHEARAKYRKANRYYhylsrqfgwqqlnplkkhlvdEDLLKVDGFSVVNNINAAAVDLKVGN 301
Cdd:COG2956  101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVL---------------------ERLLKLGPENAHAYCELAELYLEQGD 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 302 YTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELnstKQLLAQYNRQQRnALKNL 381
Cdd:COG2956  160 YDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRL---AELYEKLGDPEE-ALELL 235
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 27-170 1.85e-08

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: 53.60  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  27 DAGRMIIELRKDVVPKTAENFRALCtgECGIgtlgkplhYKGTKFHKIKRVFVVQSGDVVKN-----DGSSGES------ 95
Cdd:cd01924    5 DNGTITIVLDGYNAPVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDPQGKnpgfpDPETGKSrtiple 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  96 ---------IYG-----PVFDDENFELSHNEEGVVSMA-NYGKPNSNNSQFFISAAGCEN-------LNGTNVVVGRVLR 153
Cdd:cd01924   75 ikpegqkqpVYGktleeAGRYDEQPVLPFNAFGAIAMArTEFDPNSASSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTD 154

                        170
                 ....*....|....*..
gi 442631355 154 GLGIVAEMeqnctDEGD 170
Cdd:cd01924  155 GLDILREL-----KVGD 166
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 228-370 2.06e-08

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.15  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 228 RQSGNHFYQLGRYHEARAKYRKAnryyhylsrqfgwQQLNPlkkhlvdedllkvDGFSVVNNINAAAVDLkvGNYTSARE 307
Cdd:COG3914   82 ELAALLLQALGRYEEALALYRRA-------------LALNP-------------DNAEALFNLGNLLLAL--GRLEEALA 133

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442631355 308 VCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQY 370
Cdd:COG3914  134 ALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRL 196
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 231-373 3.48e-08

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: 54.35  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKANR-------YYHYLSRQFGWQ-QLNPLKKHLvdEDLLKVDGFSVVNNINAAAVDLKVGNY 302
Cdd:COG2956  117 AEIYEQEGDWEKAIEVLERLLKlgpenahAYCELAELYLEQgDYDEAIEAL--EKALKLDPDCARALLLLAELYLEQGDY 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442631355 303 TSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILN------ELNSTKQLLAQYNRQ 373
Cdd:COG2956  195 EEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLAladlleRKEGLEAALALLERQ 271
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 234-372 4.39e-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: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 234 FYQLGRYHEARAKYRKANRYYHYLSRQFGWQQLNPLKKHLVDEDLLKVDGFSVVNNINAAAVDLKVGNYTSAREVCNEAI 313
Cdd:COG5010    2 RALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQAL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442631355 314 RLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQYNR 372
Cdd:COG5010   82 QLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDE 140
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 293-360 2.17e-07

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: 49.81  E-value: 2.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442631355 293 AAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNEL 360
Cdd:COG4783   11 AQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 231-353 2.28e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 52.69  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKAnryyhyLsrqfgwqQLNPlkkhlvdedllkvDGFSVVNNINAAAVDLkvGNYTSAREVCN 310
Cdd:COG3914  119 GNLLLALGRLEEALAALRRA------L-------ALNP-------------DFAEAYLNLGEALRRL--GRLEEAIAALR 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:COG3914  171 RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDN 213
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 235-370 3.34e-07

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: 49.03  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 235 YQLGRYHEARAKYRKANRYYhylsrqfgwqqlnplkkhlvdEDLLKVDGFSVVNNINAAAVDLKVGNYTSAREVCNEAIR 314
Cdd:COG4783    8 YALAQALLLAGDYDEAEALL---------------------EKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALE 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442631355 315 LDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQY 370
Cdd:COG4783   67 LDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 228-353 3.64e-07

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: 49.03  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 228 RQSGNHFYQLGRYHEARAKYRKA------NRYYHYLSRQFGWQQ------LNPLKKhlvdedLLKVDGFSVVNNINAAAV 295
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKAleldpdNPEAFALLGEILLQLgdldeaIVLLHE------ALELDPDEPEARLNLGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442631355 296 DLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:COG4783   82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 235-381 5.28e-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: 50.50  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 235 YQLGRYHEARAKYRKANRYYhylsrqfgwqqlnplkkhlvdEDLLKVDGFSVVNNINAAAVDLKVGNYTSAREVCNEAIR 314
Cdd:COG2956   46 LALGNLYRRRGEYDRAIRIH---------------------QKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 315 LDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNElnstkqlLAQYNRQQRN---ALKNL 381
Cdd:COG2956  105 LDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE-------LAELYLEQGDydeAIEAL 167
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 203-351 5.93e-07

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: 48.80  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 203 AYPQDWPRKLDKFTGDGAVELLTGIRQSGNHFYQLGRYHEARAKYRKAnryyhylsrqfgwqqlnplkkhlvdedlLKVD 282
Cdd:COG5010   33 GANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA----------------------------LQLD 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442631355 283 GFSVVNNINAAAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLP 351
Cdd:COG5010   85 PNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 231-372 1.92e-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: 48.96  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 231 GNHFYQLGRYHEARAKYRKA-------NRYYHYLSRQFgwqqlnpLKKHLVD------EDLLKVDGFSVVNNINAAAVDL 297
Cdd:COG2956   49 GNLYRRRGEYDRAIRIHQKLlerdpdrAEALLELAQDY-------LKAGLLDraeellEKLLELDPDDAEALRLLAEIYE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 298 KVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN-------KQILNELNSTKQLLAQY 370
Cdd:COG2956  122 QEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCarallllAELYLEQGDYEEAIAAL 201


                 ..
gi 442631355 371 NR 372
Cdd:COG2956  202 ER 203
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
297-360 6.37e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.39  E-value: 6.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442631355 297 LKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAInDLKTAHNLLPENKQILNEL 360
Cdd:COG3063    3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNL 65
PRK10903 PRK10903
peptidylprolyl isomerase A;
28-177 7.15e-06

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 46.37  E-value: 7.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  28 AGRMIIELRKDVVPKTAENF-RALCTGecgigtlgkplHYKGTKFHKIKRVFVVQSGDVVKNdgSSGESIYGPVFDDENF 106
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFvDYVNSG-----------FYNNTTFHRVIPGFMIQGGGFTEQ--MQQKKPNPPIKNEADN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 107 ELsHNEEGVVSMANYGKPNSNNSQFFISAAGCENLNGTN-----VVVGRVLRGLGIVAEMEQNCTD-----EGDPTAPIV 176
Cdd:PRK10903 104 GL-RNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQrdfgyAVFGKVVKGMDVADKISQVPTHdvgpyQNVPSKPVV 182


                 .
gi 442631355 177 I 177
Cdd:PRK10903 183 I 183
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 297-360 1.65e-05

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: 43.84  E-value: 1.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442631355 297 LKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNEL 360
Cdd:COG4235   28 LRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 293-352 2.26e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 45.93  E-value: 2.26e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 293 AAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPE 352
Cdd:PLN03088  43 AQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPG 102
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
234-355 7.45e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 41.31  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 234 FYQLGRYHEARAKYRKAnryyhylsrqfgwqqlnplkkhlvdedlLKVDGFSVVNNINAAAVDLKVGNYTSAREvCNEAI 313
Cdd:COG3063    2 YLKLGDLEEAEEYYEKA----------------------------LELDPDNADALNNLGLLLLEQGRYDEAIA-LEKAL 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 442631355 314 RLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQ 355
Cdd:COG3063   53 KLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPSALR 94
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 228-372 7.96e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.60  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 228 RQSGNHFYQLGRYHEARAKYRKANRYYHYLSRQFGWQQLNPLKKHLVDEDLLKVDGFSVVNNINAAAVDLKVGNYTSARE 307
Cdd:COG3914   20 AAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALA 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442631355 308 VCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQ-------ILNELNSTKQLLAQYNR 372
Cdd:COG3914  100 LYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEaylnlgeALRRLGRLEEAIAALRR 171
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 311-360 2.15e-04

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: 40.76  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 442631355 311 EAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNEL 360
Cdd:COG4235    8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 240-353 4.96e-04

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 42.28  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  240 YHEARAKYRKA---------NRYYHYLSRQFGWQQLNPLKKHlvdEDLLK-VDGFSVVNN--INAAAVDLKVGNYTSARE 307
Cdd:TIGR00990 310 YEEAARAFEKAldlgklgekEAIALNLRGTFKCLKGKHLEAL---ADLSKsIELDPRVTQsyIKRASMNLELGDPDKAEE 386

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 442631355  308 VCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:TIGR00990 387 DFDKALKLNSEDPDIYYHRAQLHFIKGEFAQAGKDYQKSIDLDPDF 432
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
275-360 6.94e-04

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 40.67  E-value: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 275 DEDLLKVDGFSVVNNINAAAVDLKVGNYTSAREVCNEAIR------LDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHN 348
Cdd:COG4785   22 AAILLAALLFAAVLALAIALADLALALAAAALAAAALAAEridralALPDLAQLYYERGVAYDSLGDYDLAIADFDQALE 101

                         90
                 ....*....|..
gi 442631355 349 LLPENKQILNEL 360
Cdd:COG4785  102 LDPDLAEAYNNR 113
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 292-351 7.48e-04

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 41.31  E-value: 7.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 292 AAAVDlkvGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLP 351
Cdd:PLN03088  11 EAFVD---DDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDP 67
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 286-376 1.57e-03

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 40.28  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 286 VVNNINAAAVDLKVGNYTSAREVCNEAIRLDPKCSKAFY-RRAQAQRGLRNYEEAINDLKTAHNLLPENKQILnelnstk 364
Cdd:COG3071   50 LLAYLLAARAAQALGDYERRDEYLAQALELAPEAELAVLlTRAELLLDQGQAEQALATLEALRAGAPRHPQVL------- 122

                         90
                 ....*....|..
gi 442631355 365 QLLAQYNRQQRN 376
Cdd:COG3071  123 RLLLQAYRQLGD 134
TPR_1 pfam00515
Tetratricopeptide repeat;
320-353 2.40e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 2.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 442631355  320 SKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 297-360 3.69e-03

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: 38.94  E-value: 3.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442631355 297 LKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNEL 360
Cdd:COG2956   19 LLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLEL 82
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 297-372 4.19e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.89  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 297 LKVGNYTSAREVCNEAIRLDPKCS---KAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENK----------QILNELNST 363
Cdd:COG1729    4 LKAGDYDEAIAAFKAFLKRYPNSPlapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapdallklgLSYLELGDY 83


                 ....*....
gi 442631355 364 KQLLAQYNR 372
Cdd:COG1729   84 DKARATLEE 92
TPR_19 pfam14559
Tetratricopeptide repeat;
300-369 4.34e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 35.25  E-value: 4.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355  300 GNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQIlnelnstKQLLAQ 369
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRY-------AALLAK 64
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 320-353 6.24e-03

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: 33.96  E-value: 6.24e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 442631355   320 SKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPEN 353
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
313-370 9.13e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 37.29  E-value: 9.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442631355 313 IRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQY 370
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRY 58
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 276-360 9.95e-03

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: 37.40  E-value: 9.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442631355 276 EDLLKVDGFSVVNNINAAAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQ 355
Cdd:COG2956   32 EEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAE 111


                 ....*
gi 442631355 356 ILNEL 360
Cdd:COG2956  112 ALRLL 116
 
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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