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Conserved domains on  [gi|311347388|gb|ADP90639|]
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peptidyl-prolyl cis-trans isomerase D [Homo sapiens]

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 ...
 16-182 9.50e-115

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: 330.37  E-value: 9.50e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  16 PRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGhttGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGG 95
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  96 ESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKL 175
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                 ....*..
gi 311347388 176 CVIAECG 182
Cdd:cd01926  158 VVIADCG 164
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
213-367 3.97e-13

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.49  E-value: 3.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 213 LKDVDKILLITED----LKNIGNTFFKSQNWEMAIKKYAEVLryvdsskavietadraKLQPIALSCVLNIGACKLKMSN 288
Cdd:COG0457   28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQAL----------------ELDPDDAEALNNLGLALQALGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 289 WQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAEL----LKVKQKIKAQKDKEKAV 364
Cdd:COG0457   92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                 ...
gi 311347388 365 YAK 367
Cdd:COG0457  172 AAA 174
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 16-182 9.50e-115

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: 330.37  E-value: 9.50e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  16 PRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGhttGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGG 95
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  96 ESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKL 175
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                 ....*..
gi 311347388 176 CVIAECG 182
Cdd:cd01926  158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 7-184 5.44e-94

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 278.65  E-value: 5.44e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388   7 QAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGigHTTGKPLHFKGCPFHRIIKKFMIQGGD 86
Cdd:PTZ00060   7 QSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  87 FSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVE 166
Cdd:PTZ00060  85 ITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEG 164

                        170
                 ....*....|....*...
gi 311347388 167 VKGEKPAKLCVIAECGEL 184
Cdd:PTZ00060 165 TQSGYPKKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 30-183 2.46e-58

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 185.92  E-value: 2.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388   30 GRIVLELFADIVPKTAENFRALCTgeKGighttgkplHFKGCPFHRIIKKFMIQGGDFsnqNGTGGESIYGEKFEDENF- 108
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDP---TGTGGGGKSIFPIPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311347388  109 -HYKHDReGLLSMANAGR--NTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGE 183
Cdd:pfam00160  73 lLLKHKR-GALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-178 1.38e-48

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 161.11  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  13 PSNPRVFFDVDiggerVGRIVLELFADIVPKTAENFRALCtgEKGighttgkplHFKGCPFHRIIKKFMIQGGDFSNqNG 92
Cdd:COG0652    4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDPTG-TG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  93 TGGEsiyGEKFEDENFH-YKHDReGLLSMANA-GRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEV-KG 169
Cdd:COG0652   67 TGGP---GYTIPDEFDPgLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTdPG 142


                 ....*....
gi 311347388 170 EKPAKLCVI 178
Cdd:COG0652  143 DGPLEPVVI 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
213-367 3.97e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.49  E-value: 3.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 213 LKDVDKILLITED----LKNIGNTFFKSQNWEMAIKKYAEVLryvdsskavietadraKLQPIALSCVLNIGACKLKMSN 288
Cdd:COG0457   28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQAL----------------ELDPDDAEALNNLGLALQALGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 289 WQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAEL----LKVKQKIKAQKDKEKAV 364
Cdd:COG0457   92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                 ...
gi 311347388 365 YAK 367
Cdd:COG0457  172 AAA 174
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 192-362 1.30e-10

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: 62.69  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  192 IFPKDGSGDshPDFPEDADIDLKDVDKILLiteDLKNIGNTFFKSQNWEMAIKKYaevlryvdsSKAVIETADraklqPI 271
Cdd:TIGR00990 101 VEPADELPE--IDESSVANLSEEERKKYAA---KLKEKGNKAYRNKDFNKAIKLY---------SKAIECKPD-----PV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  272 ALScvlNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAP-EDKAIQAELLKV 350
Cdd:TIGR00990 162 YYS---NRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTASCIIDGfRNEQSAQAVERL 238

                         170
                  ....*....|..
gi 311347388  351 KQKIKAQKDKEK 362
Cdd:TIGR00990 239 LKKFAESKAKEI 250
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 284-340 4.22e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 45.16  E-value: 4.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311347388 284 LKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:PLN03088  47 IKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPGD 103
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 277-306 3.76e-04

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: 37.43  E-value: 3.76e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 311347388   277 LNIGACKLKMSNWQGAIDSCLEALELDPSN 306
Cdd:smart00028   5 YNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
278-306 6.02e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.02  E-value: 6.02e-04
                          10        20
                  ....*....|....*....|....*....
gi 311347388  278 NIGACKLKMSNWQGAIDSCLEALELDPSN 306
Cdd:pfam00515   6 NLGNAYFKLGKYDEALEYYEKALELNPNN 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 ...
 16-182 9.50e-115

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: 330.37  E-value: 9.50e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  16 PRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGhttGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGG 95
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  96 ESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKL 175
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                 ....*..
gi 311347388 176 CVIAECG 182
Cdd:cd01926  158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 7-184 5.44e-94

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 278.65  E-value: 5.44e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388   7 QAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGigHTTGKPLHFKGCPFHRIIKKFMIQGGD 86
Cdd:PTZ00060   7 QSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKV--GSSGKNLHYKGSIFHRIIPQFMCQGGD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  87 FSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVE 166
Cdd:PTZ00060  85 ITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEG 164

                        170
                 ....*....|....*...
gi 311347388 167 VKGEKPAKLCVIAECGEL 184
Cdd:PTZ00060 165 TQSGYPKKPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 9-184 3.15e-81

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 246.29  E-value: 3.15e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388   9 KPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKgigHTTGKPLHFKGCPFHRIIKKFMIQGGDFS 88
Cdd:PLN03149  12 RPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  89 NQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVI-KGIGVARILENVEV 167
Cdd:PLN03149  89 KGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVAT 168

                        170
                 ....*....|....*...
gi 311347388 168 -KGEKPAKLCVIAECGEL 184
Cdd:PLN03149 169 gPNNRPKLACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 29-178 4.02e-62

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: 195.56  E-value: 4.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  29 VGRIVLELFADIVPKTAENFRALCTGEkgighttgkplHFKGCPFHRIIKKFMIQGGDFsnQNGTGGESIYGEKFEDENF 108
Cdd:cd00317    6 KGRIVIELYGDEAPKTVENFLSLARGG-----------FYDGTTFHRVIPGFMIQGGDP--TGTGGGGSGPGYKFPDENF 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311347388 109 HYK-HDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEV-KGEKPAKLCVI 178
Cdd:cd00317   73 PLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTdENGRPIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 30-183 2.46e-58

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 185.92  E-value: 2.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388   30 GRIVLELFADIVPKTAENFRALCTgeKGighttgkplHFKGCPFHRIIKKFMIQGGDFsnqNGTGGESIYGEKFEDENF- 108
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDP---TGTGGGGKSIFPIPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311347388  109 -HYKHDReGLLSMANAGR--NTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGE 183
Cdd:pfam00160  73 lLLKHKR-GALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 30-172 2.26e-51

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: 168.02  E-value: 2.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  30 GRIVLELFADIVPKTAENFRALCtgekgighttgKPLHFKGCPFHRIIKKFMIQGGDFSNQnGTGGESIYGEKFEDEnFH 109
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA-----------RNGYYNNTIFHRVIKGFMIQTGDPTGD-GTGGESIWGKEFEDE-FS 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311347388 110 --YKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEV-KGEKP 172
Cdd:cd01927   74 psLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTdKNDRP 139
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 29-172 1.24e-50

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: 166.46  E-value: 1.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  29 VGRIVLELFADIVPKTAENFRALCTGEkgighttgkplHFKGCPFHRIIKKFMIQGGDFSNqNGTGGESIYGEKFEDENF 108
Cdd:cd01928    9 LGDIKIELFCDDCPKACENFLALCASG-----------YYNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFR 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311347388 109 -HYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEV-KGEKP 172
Cdd:cd01928   77 eTLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVdKKYRP 142
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-178 1.38e-48

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 161.11  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  13 PSNPRVFFDVDiggerVGRIVLELFADIVPKTAENFRALCtgEKGighttgkplHFKGCPFHRIIKKFMIQGGDFSNqNG 92
Cdd:COG0652    4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDPTG-TG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  93 TGGEsiyGEKFEDENFH-YKHDReGLLSMANA-GRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEV-KG 169
Cdd:COG0652   67 TGGP---GYTIPDEFDPgLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTdPG 142


                 ....*....
gi 311347388 170 EKPAKLCVI 178
Cdd:COG0652  143 DGPLEPVVI 151
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 30-178 3.40e-48

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: 160.27  E-value: 3.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  30 GRIVLELFADIVPKTAENFRALCtgEKGighttgkplHFKGCPFHRIIKKFMIQGGDFSNqNGTGGESIYGEKFEDE-NF 108
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC--KKG---------YYDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKP 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311347388 109 HYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKG-EKPAKLCVI 178
Cdd:cd01923   77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGtDRPKEEIKI 147
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 29-172 6.46e-46

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: 153.84  E-value: 6.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  29 VGRIVLELFADIVPKTAENFRALCTgeKGighttgkplHFKGCPFHRIIKKFMIQGGDfSNQNGTGGESIYGEKFEDE-N 107
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELAK--RG---------YYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiH 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311347388 108 FHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKP 172
Cdd:cd01922   74 PELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRP 138
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 29-172 4.92e-37

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 131.71  E-value: 4.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  29 VGRIVLELFADIVPKTAENFRALCTGEkgighttgkplHFKGCPFHRIIKKFMIQGGDFSNqNGTGGESIYGEKFEDEnF 108
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEG-----------YYDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDE-F 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311347388 109 H--YKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKG--IGVARILENVEVKGEKP 172
Cdd:cd01925   81 HsrLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDtiYNLLKLAEVETDKDERP 148
PTZ00221 PTZ00221
cyclophilin; Provisional
 2-201 3.68e-34

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 126.52  E-value: 3.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388   2 SHPSPQAKPSNpsnpRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKF- 80
Cdd:PTZ00221  43 SHRMKEEQNSC----RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVDRNNn 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  81 MIQGGDFSNQNgtggESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVAR 160
Cdd:PTZ00221 119 IIVLGELDSFN----VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLE 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 311347388 161 ILENVEVKG-EKPAKLCVIAECGELKEGDDGGIF----PKDGSGDS 201
Cdd:PTZ00221 195 KLESLPLDDvGRPLLPVTVSFCGALTGEKPPGRQqllaAADDSASS 240
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 29-158 8.39e-26

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: 101.65  E-value: 8.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  29 VGRIVLELFADIVPKTAENFRALCtgekgighttgKPLHFKGCPFHRIIKKFMIQGGDfSNQNGTGGESIYGEK------ 102
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQLygrqar 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 311347388 103 -FEDENFH-YKHDREGLLSMANAGRNTNGSQFFITTVP-TPHLDGKHVVFGQVIKGIGV 158
Cdd:cd01921   74 fFEPEILPlLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDV 132
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 30-167 2.62e-15

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: 72.48  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  30 GRIVLELFADIVPKTAENFRALCtgEKGighttgkplHFKGCPFHRIIKKFMIQGGDFS---NQNGTG----GESIYGEK 102
Cdd:cd01920    7 GDIVVELYDDKAPITVENFLAYV--RKG---------FYDNTIFHRVISGFVIQGGGFTpdlAQKETLkpikNEAGNGLS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311347388 103 fedenfhykhDREGLLSMA-NAGRNTNGSQFFITTVPTPHLD-----GKHVVFGQVIKGIGVARILENVEV 167
Cdd:cd01920   76 ----------NTRGTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVET 136
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
213-367 3.97e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.49  E-value: 3.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 213 LKDVDKILLITED----LKNIGNTFFKSQNWEMAIKKYAEVLryvdsskavietadraKLQPIALSCVLNIGACKLKMSN 288
Cdd:COG0457   28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQAL----------------ELDPDDAEALNNLGLALQALGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 289 WQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAEL----LKVKQKIKAQKDKEKAV 364
Cdd:COG0457   92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                 ...
gi 311347388 365 YAK 367
Cdd:COG0457  172 AAA 174
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-364 8.74e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.34  E-value: 8.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 226 LKNIGNTFFKSQNWEMAIKKYAEVLryvdsskavietadraKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPS 305
Cdd:COG0457   11 YNNLGLAYRRLGRYEEAIEDYEKAL----------------ELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311347388 306 NTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAEL----LKVKQKIKAQKDKEKAV 364
Cdd:COG0457   75 DAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLglalLELGRYDEAIEAYERAL 137
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 226-364 3.62e-11

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: 63.21  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 226 LKNIGNTFFKSQNWEMAIKKYAEVL-RYVDSSKAVIETA---------DRA--------KLQPIALSCVLNIGACKLKMS 287
Cdd:COG2956   45 HLALGNLYRRRGEYDRAIRIHQKLLeRDPDRAEALLELAqdylkagllDRAeellekllELDPDDAEALRLLAEIYEQEG 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311347388 288 NWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKikaQKDKEKAV 364
Cdd:COG2956  125 DWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLE---QGDYEEAI 198
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 226-348 5.05e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 64.24  E-value: 5.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 226 LKNIGNTFFKSQNWEMAIKKYAEVLRyvdsskavietadrakLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPS 305
Cdd:COG3914  115 LFNLGNLLLALGRLEEALAALRRALA----------------LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPD 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 311347388 306 NTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELL 348
Cdd:COG3914  179 NAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLL 221
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
226-366 5.26e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.33  E-value: 5.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 226 LKNIGNTFFKSQNWEMAIKKYAEVLRyvdsskavietadrakLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPS 305
Cdd:COG0457   79 LNNLGLALQALGRYEEALEDYDKALE----------------LDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPD 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311347388 306 NTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYA 366
Cdd:COG0457  143 DADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLAL 203
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
224-340 8.32e-11

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 61.08  E-value: 8.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 224 EDLKNIGNTFFKSQNWEMAIKKYAEVLRyvdsskavietadrakLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELD 303
Cdd:COG4785   74 QLYYERGVAYDSLGDYDLAIADFDQALE----------------LDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD 137

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 311347388 304 PSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:COG4785  138 PDYAYAYLNRGIALYYLGRYELAIADLEKALELDPND 174
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 192-362 1.30e-10

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: 62.69  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  192 IFPKDGSGDshPDFPEDADIDLKDVDKILLiteDLKNIGNTFFKSQNWEMAIKKYaevlryvdsSKAVIETADraklqPI 271
Cdd:TIGR00990 101 VEPADELPE--IDESSVANLSEEERKKYAA---KLKEKGNKAYRNKDFNKAIKLY---------SKAIECKPD-----PV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  272 ALScvlNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAP-EDKAIQAELLKV 350
Cdd:TIGR00990 162 YYS---NRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTASCIIDGfRNEQSAQAVERL 238

                         170
                  ....*....|..
gi 311347388  351 KQKIKAQKDKEK 362
Cdd:TIGR00990 239 LKKFAESKAKEI 250
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
267-340 4.45e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.64  E-value: 4.45e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311347388 267 KLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:COG0457    2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD 75
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 223-347 1.06e-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: 56.17  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 223 TEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIetadraklqpialscvLNIGACKLKMSNWQGAIDSCLEALEL 302
Cdd:COG4235   17 AEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADAL----------------LDLAEALLAAGDTEEAEELLERALAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 311347388 303 DPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED---KAIQAEL 347
Cdd:COG4235   81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADapaRLLEASI 128
PRK10903 PRK10903
peptidylprolyl isomerase A;
29-172 3.18e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 56.00  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  29 VGRIVLELFADIVPKTAENFralctgekgIGHTTGKplHFKGCPFHRIIKKFMIQGGDFSN--QNGTGGESIygeKFEDE 106
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNF---------VDYVNSG--FYNNTTFHRVIPGFMIQGGGFTEqmQQKKPNPPI---KNEAD 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311347388 107 NfhYKHDREGLLSMA-NAGRNTNGSQFFITTVPTPHLD-GK----HVVFGQVIKGIGVARILENVEVKGEKP 172
Cdd:PRK10903 103 N--GLRNTRGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHDVGP 172
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 226-364 4.22e-09

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: 57.05  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 226 LKNIGNTFFKSQNWEMAIKKYAEVLRYVDSS-----------------KAVIETADRA-KLQPIALSCVLNIGACKLKMS 287
Cdd:COG2956  113 LRLLAEIYEQEGDWEKAIEVLERLLKLGPENahaycelaelyleqgdyDEAIEALEKAlKLDPDCARALLLLAELYLEQG 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311347388 288 NWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDkaiqAELLKVKQKIKAQKDKEKAV 364
Cdd:COG2956  193 DYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSD----DLLLALADLLERKEGLEAAL 265
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 224-370 2.21e-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: 52.50  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 224 EDLKNIGNTFFKSQNWEMAIKKYAEVLryvdsskavietaDRAKLQPIALscvLNIGACKLKMSNWQGAIDSCLEALELD 303
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKAL-------------ELDPDNPEAF---ALLGEILLQLGDLDEAIVLLHEALELD 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311347388 304 PSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKaQKDKEKAVYAKMFA 370
Cdd:COG4783   69 PDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG-RPDEAIAALEKALE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 281-364 3.09e-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: 52.66  E-value: 3.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 281 ACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVkqkIKAQKDK 360
Cdd:COG5010   62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAAL---LLSLGQD 138


                 ....
gi 311347388 361 EKAV 364
Cdd:COG5010  139 DEAK 142
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 207-338 4.40e-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: 51.88  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 207 EDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLryvdsskavietadraKLQPIALSCVLNIGACKLKM 286
Cdd:COG5010   38 KEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQAL----------------QLDPNNPELYYNLALLYSRS 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 311347388 287 SNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAP 338
Cdd:COG5010  102 GDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
209-364 1.02e-07

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 52.22  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 209 ADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLqpialscVLNIGACKLKMSN 288
Cdd:COG4785   16 AAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQL-------YYERGVAYDSLGD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 289 WQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAE----LLKVKQKIKAQKDKEKAV 364
Cdd:COG4785   89 YDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNrgiaLYYLGRYELAIADLEKAL 168
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 31-163 2.60e-07

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: 50.13  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  31 RIVLELFAdiVPKTAENFRALCtgEKGIghttgkplhFKGCPFHRIIKKFMIQGGD-FSNQNG-----TG---------- 94
Cdd:cd01924   10 TIVLDGYN--APVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleik 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  95 ----GESIYGEKFE-----DENFHYKHDREGLLSMANA--GRNTNGSQFFI-------TTVPTPHLDGKHVVFGQVIKGI 156
Cdd:cd01924   77 pegqKQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGL 156


                 ....*..
gi 311347388 157 GVARILE 163
Cdd:cd01924  157 DILRELK 163
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
284-364 2.72e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.24  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 284 LKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALAdLKKAQGIAPEDKAIQAEL----LKVKQKIKAQKD 359
Cdd:COG3063    3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLaellLELGDYDEALAY 81


                 ....*
gi 311347388 360 KEKAV 364
Cdd:COG3063   82 LERAL 86
PRK10791 PRK10791
peptidylprolyl isomerase B;
30-165 5.52e-07

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 49.07  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  30 GRIVLELFADIVPKTAENFRALCTGEkgighttgkplHFKGCPFHRIIKKFMIQGGDFsnQNGTGGESIYGEKFEDENFH 109
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREG-----------FYNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNG 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311347388 110 YKHDReGLLSMANAGR-NTNGSQFFITTVPTPHLDGK--------HVVFGQVIKGIGVARILENV 165
Cdd:PRK10791  76 LKNTR-GTLAMARTQApHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGV 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 230-364 8.29e-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: 49.73  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 230 GNTFFKSQNWEMAIKKYAEVLRyVDSskaviETADraklqpiALscvLNIGACKLKMSNWQGAIDSCLEALELDPSNTKA 309
Cdd:COG2956   15 GLNYLLNGQPDKAIDLLEEALE-LDP-----ETVE-------AH---LALGNLYRRRGEYDRAIRIHQKLLERDPDRAEA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 311347388 310 LYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKikaQKDKEKAV 364
Cdd:COG2956   79 LLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQ---EGDWEKAI 130
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
260-339 1.26e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.32  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 260 IETADRA-KLQPIALSCVLNIGACKLKMSNWQGAIDsCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAP 338
Cdd:COG3063   12 EEYYEKAlELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90


                 .
gi 311347388 339 E 339
Cdd:COG3063   91 S 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 228-340 2.19e-06

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: 46.72  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 228 NIGNTFFKSQNWEMAIKKYAEVLRyvdsskavietadRAKLQPIALscvLNIGACKLKMSNWQGAIDSCLEALELDPSNT 307
Cdd:COG4783   43 LLGEILLQLGDLDEAIVLLHEALE-------------LDPDEPEAR---LNLGLALLKAGDYDEALALLEKALKLDPEHP 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 311347388 308 KALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:COG4783  107 EAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 250-366 5.14e-06

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: 48.54  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  250 LRYVDSSKAVIETAdrAKLQPIALSCVLniGACKLKMSNWQ--GAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQAL 327
Cdd:TIGR02917 138 LGQLELAQKSYEQA--LAIDPRSLYAKL--GLAQLALAENRfdEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELAL 213

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 311347388  328 ADLKKAQGIAPedKAIQAELLKVKQKIKAQKDKEKAVYA 366
Cdd:TIGR02917 214 AAYRKAIALRP--NNIAVLLALATILIEAGEFEEAEKHA 250
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 267-347 5.91e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.07  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 267 KLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAE 346
Cdd:COG3914  106 ALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185


                 .
gi 311347388 347 L 347
Cdd:COG3914  186 L 186
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 233-346 9.70e-06

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: 44.21  E-value: 9.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 233 FFKSQNWEMAIKKYaevlryvdssKAVIETADRAKLQPIALscvLNIGACKLKMSNWQGAIDSCLEALELDPSNTK---A 309
Cdd:COG1729    3 LLKAGDYDEAIAAF----------KAFLKRYPNSPLAPDAL---YWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKapdA 69

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 311347388 310 LYRRAQGWQGLKEYDQALADLKKAQGIAPE-DKAIQAE 346
Cdd:COG1729   70 LLKLGLSYLELGDYDKARATLEELIKKYPDsEAAKEAR 107
LcrH_SycD TIGR02552
type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in ...
 277-359 1.15e-05

type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in type III secretion operons. LcrH, from Yersinia is believed to have a regulatory function in the low-calcium response of the secretion system. The same protein is also known as SycD (SYC = Specific Yop Chaperone) for its chaperone role. In Pseudomonas, where the homolog is known as PcrH, the chaperone role has been demonstrated and the regulatory role appears to be absent. ScyD/LcrH contains three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array.


Pssm-ID: 274197 [Multi-domain]  Cd Length: 135  Bit Score: 44.59  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  277 LNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDkaiqAELLKVKQKIKA 356
Cdd:TIGR02552  55 LGLAACCQMLKEYEEAIDAYALAAALDPDDPRPYFHAAECLLALGEPESALKALDLAIEICGEN----PEYSELKERAEA 130


                  ...
gi 311347388  357 QKD 359
Cdd:TIGR02552 131 MLE 133
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 292-347 2.30e-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: 43.46  E-value: 2.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 311347388 292 AIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAEL 347
Cdd:COG4235    2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 284-340 4.22e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 45.16  E-value: 4.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311347388 284 LKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:PLN03088  47 IKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPGD 103
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 277-306 3.76e-04

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: 37.43  E-value: 3.76e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 311347388   277 LNIGACKLKMSNWQGAIDSCLEALELDPSN 306
Cdd:smart00028   5 YNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
278-306 6.02e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.02  E-value: 6.02e-04
                          10        20
                  ....*....|....*....|....*....
gi 311347388  278 NIGACKLKMSNWQGAIDSCLEALELDPSN 306
Cdd:pfam00515   6 NLGNAYFKLGKYDEALEYYEKALELNPNN 34
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 284-363 9.89e-04

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: 38.43  E-value: 9.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388 284 LKMSNWQGAIDSCLEALELDPSNT---KALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDK 360
Cdd:COG1729    4 LKAGDYDEAIAAFKAFLKRYPNSPlapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGDY 83


                 ...
gi 311347388 361 EKA 363
Cdd:COG1729   84 DKA 86
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 284-340 1.10e-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: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311347388 284 LKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:COG3914   89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDF 145
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
300-340 1.84e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.60  E-value: 1.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 311347388 300 LELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD 41
TPR_1 pfam00515
Tetratricopeptide repeat;
308-340 2.85e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 2.85e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 311347388  308 KALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:pfam00515   2 KALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 252-364 2.92e-03

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: 39.58  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  252 YVDSSKAVIETADRAKLQP-IALSCVLNiGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADL 330
Cdd:TIGR00990 310 YEEAARAFEKALDLGKLGEkEAIALNLR-GTFKCLKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDF 388

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 311347388  331 KKAQGIAPEDKAI---QAELLKVKQKI-KAQKDKEKAV 364
Cdd:TIGR00990 389 DKALKLNSEDPDIyyhRAQLHFIKGEFaQAGKDYQKSI 426
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 308-340 3.03e-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: 34.73  E-value: 3.03e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 311347388   308 KALYRRAQGWQGLKEYDQALADLKKAQGIAPED 340
Cdd:smart00028   2 EALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_19 pfam14559
Tetratricopeptide repeat;
288-345 6.33e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 34.87  E-value: 6.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 311347388  288 NWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQA 345
Cdd:pfam14559   3 DYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAA 60
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 257-366 7.17e-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: 38.53  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311347388  257 KAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGI 336
Cdd:TIGR02917 585 KALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALEL 664

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 311347388  337 AP---EDKAIQAELL----------KVKQKIKAQKDKEKAVYA 366
Cdd:TIGR02917 665 KPdntEAQIGLAQLLlaakrtesakKIAKSLQKQHPKAALGFE 707
 
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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