NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568923769|ref|XP_006502006|]
View 

peptidyl-prolyl cis-trans isomerase D isoform X1 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 17-88 3.05e-41

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: 139.70  E-value: 3.05e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923769  17 HHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:cd01926   93 KHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
119-273 4.89e-13

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 4.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 119 LKDVDKILLISED----LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSN 194
Cdd:COG0457   28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQALE----------------LDPDDAEALNNLGLALQALGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 195 WQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457   92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                 ...
gi 568923769 271 YAK 273
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 ...
 17-88 3.05e-41

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: 139.70  E-value: 3.05e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923769  17 HHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:cd01926   93 KHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 15-90 6.82e-33

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 118.79  E-value: 6.82e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568923769  15 NRHHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECGEL 90
Cdd:PTZ00060 107 KLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 11-89 6.60e-29

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: 107.34  E-value: 6.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769   11 SRFKNRHHDReGLLSMANAG--PNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:pfam00160  70 IFPLLLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148


                  .
gi 568923769   89 E 89
Cdd:pfam00160 149 V 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-84 4.39e-25

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 97.55  E-value: 4.39e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568923769  13 FKNRHHDREGLLSMANA-GPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEV-NGEKPAKLCVI 84
Cdd:COG0652   78 FDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTdPGDGPLEPVVI 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
119-273 4.89e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 4.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 119 LKDVDKILLISED----LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSN 194
Cdd:COG0457   28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQALE----------------LDPDDAEALNNLGLALQALGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 195 WQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457   92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                 ...
gi 568923769 271 YAK 273
Cdd:COG0457  172 AAA 174
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 98-236 9.24e-11

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: 61.92  E-value: 9.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769   98 IFPKDGSGDshPDFPEDADIDLKDVDKILLiseDLKNIGNTFFKSQNWEMAIKKYakvlryvdsSKAVIEKADrsrlqPI 177
Cdd:TIGR00990 101 VEPADELPE--IDESSVANLSEEERKKYAA---KLKEKGNKAYRNKDFNKAIKLY---------SKAIECKPD-----PV 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568923769  178 ALScvlNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADL 236
Cdd:TIGR00990 162 YYS---NRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDL 217
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 190-246 2.21e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 45.16  E-value: 2.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769 190 LKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:PLN03088  47 IKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPGD 103
TPR_1 pfam00515
Tetratricopeptide repeat;
214-246 9.80e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.86  E-value: 9.80e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568923769  214 KALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:pfam00515   2 KALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 214-246 1.69e-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: 35.11  E-value: 1.69e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568923769   214 KALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:smart00028   2 EALYNLGNAYLKLGDYDEALEYYEKALELDPNN 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 ...
 17-88 3.05e-41

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: 139.70  E-value: 3.05e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923769  17 HHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:cd01926   93 KHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 15-90 6.82e-33

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 118.79  E-value: 6.82e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568923769  15 NRHHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECGEL 90
Cdd:PTZ00060 107 KLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 13-84 7.34e-30

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: 109.66  E-value: 7.34e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568923769  13 FKNRHHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEV-NGEKPAKLCVI 84
Cdd:cd00317   72 FPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTdENGRPIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 11-89 6.60e-29

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: 107.34  E-value: 6.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769   11 SRFKNRHHDReGLLSMANAG--PNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:pfam00160  70 IFPLLLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148


                  .
gi 568923769   89 E 89
Cdd:pfam00160 149 V 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 14-78 2.77e-28

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: 105.62  E-value: 2.77e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568923769  14 KNRHHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVN-GEKP 78
Cdd:cd01927   74 PSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDkNDRP 139
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 18-90 2.10e-25

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 99.14  E-value: 2.10e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568923769  18 HDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVI-KGLGVARTLENVEVNGEKPAKL-CVIAECGEL 90
Cdd:PLN03149 112 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLaCVISECGEM 186
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-84 4.39e-25

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 97.55  E-value: 4.39e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568923769  13 FKNRHHDREGLLSMANA-GPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEV-NGEKPAKLCVI 84
Cdd:COG0652   78 FDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTdPGDGPLEPVVI 151
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 17-73 1.54e-24

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: 95.97  E-value: 1.54e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769  17 HHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEV 73
Cdd:cd01928   80 KHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV 136
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 18-84 1.67e-24

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: 95.95  E-value: 1.67e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568923769  18 HDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNG-EKPAKLCVI 84
Cdd:cd01923   80 HDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGtDRPKEEIKI 147
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 10-78 4.09e-22

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: 89.52  E-value: 4.09e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568923769  10 HSRFKnrhHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKP 78
Cdd:cd01922   73 HPELK---HTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRP 138
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 10-58 1.11e-14

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: 70.07  E-value: 1.11e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568923769  10 HSRFKnrhHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQV 58
Cdd:cd01925   81 HSRLR---FNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 18-68 2.07e-13

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: 66.60  E-value: 2.07e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568923769  18 HDREGLLSMANAGPNTNGSQFFITTVP-TPHLDGKHVVFGQVIKGLGVARTL 68
Cdd:cd01921   85 HSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKI 136
PTZ00221 PTZ00221
cyclophilin; Provisional
 13-90 2.41e-13

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 67.97  E-value: 2.41e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568923769  13 FKNRHHDReGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNG-EKPAKLCVIAECGEL 90
Cdd:PTZ00221 142 YRHRHTER-GLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDvGRPLLPVTVSFCGAL 219
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
119-273 4.89e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 4.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 119 LKDVDKILLISED----LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSN 194
Cdd:COG0457   28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQALE----------------LDPDDAEALNNLGLALQALGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 195 WQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457   92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                 ...
gi 568923769 271 YAK 273
Cdd:COG0457  172 AAA 174
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 132-254 9.25e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.01  E-value: 9.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 132 LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPS 211
Cdd:COG3914  115 LFNLGNLLLALGRLEEALAALRRALA----------------LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPD 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568923769 212 NTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELL 254
Cdd:COG3914  179 NAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLL 221
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
132-270 9.89e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.49  E-value: 9.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 132 LKNIGNTFFKSQNWEMAIKKYAKVLryvdsskaviekadrsRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPS 211
Cdd:COG0457   11 YNNLGLAYRRLGRYEEAIEDYEKAL----------------ELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568923769 212 NTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457   75 DAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLglalLELGRYDEAIEAYERAL 137
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 98-236 9.24e-11

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: 61.92  E-value: 9.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769   98 IFPKDGSGDshPDFPEDADIDLKDVDKILLiseDLKNIGNTFFKSQNWEMAIKKYakvlryvdsSKAVIEKADrsrlqPI 177
Cdd:TIGR00990 101 VEPADELPE--IDESSVANLSEEERKKYAA---KLKEKGNKAYRNKDFNKAIKLY---------SKAIECKPD-----PV 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568923769  178 ALScvlNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADL 236
Cdd:TIGR00990 162 YYS---NRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDL 217
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
132-272 2.35e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.25  E-value: 2.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 132 LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPS 211
Cdd:COG0457   79 LNNLGLALQALGRYEEALEDYDKALE----------------LDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPD 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568923769 212 NTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDKEKAVYA 272
Cdd:COG0457  143 DADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLAL 203
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
173-246 8.95e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.71  E-value: 8.95e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568923769 173 RLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:COG0457    2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD 75
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
130-269 9.22e-10

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 57.23  E-value: 9.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 130 EDLKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMD 209
Cdd:COG4785   74 QLYYERGVAYDSLGDYDLAIADFDQALE----------------LDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 210 PSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDkaiqAELLKVKQMIKAQKDKEKA 269
Cdd:COG4785  138 PDYAYAYLNRGIALYYLGRYELAIADLEKALELDPND----PERALWLYLAERKLDPEKA 193
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 130-262 1.60e-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: 55.01  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 130 EDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSSKAVIekadrsrlqpialscvLNIGACKLKMSNWQGAIDSCLEALEMD 209
Cdd:COG4235   18 EGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADAL----------------LDLAEALLAAGDTEEAEELLERALALD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568923769 210 PSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDkaiqAELLKVKQMIKA 262
Cdd:COG4235   82 PDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD----APARLLEASIAE 130
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 132-270 2.18e-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: 56.66  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 132 LKNIGNTFFKSQNWEMAIKKYAKVL-RYVDSSKAVIEKA---------DRS--------RLQPIALSCVLNIGACKLKMS 193
Cdd:COG2956   45 HLALGNLYRRRGEYDRAIRIHQKLLeRDPDRAEALLELAqdylkagllDRAeellekllELDPDDAEALRLLAEIYEQEG 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769 194 NWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQmikAQKDKEKAV 270
Cdd:COG2956  125 DWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYL---EQGDYEEAI 198
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 132-270 2.61e-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: 53.58  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 132 LKNIGNTFFKSQNWEMAIKKYAKVLRYV-DSSKAVIEKADRSRLQ-----------------PIALSCVLNIGACKLKMS 193
Cdd:COG2956  113 LRLLAEIYEQEGDWEKAIEVLERLLKLGpENAHAYCELAELYLEQgdydeaiealekalkldPDCARALLLLAELYLEQG 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769 194 NWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDkaiqAELLKVKQMIKAQKDKEKAV 270
Cdd:COG2956  193 DYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSD----DLLLALADLLERKEGLEAAL 265
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 183-273 9.22e-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: 50.19  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 183 LNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVkqMIKA 262
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA--LLKA 85

                         90
                 ....*....|..
gi 568923769 263 QK-DKEKAVYAK 273
Cdd:COG4783   86 GDyDEALALLEK 97
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
163-246 2.72e-07

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 50.30  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 163 KAVIEKADRSRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEI 242
Cdd:COG4785   57 ALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL 136


                 ....
gi 568923769 243 APGD 246
Cdd:COG4785  137 DPDY 140
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 187-270 2.78e-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: 49.19  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 187 ACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVkqmIKAQKDK 266
Cdd:COG5010   62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAAL---LLSLGQD 138


                 ....
gi 568923769 267 EKAV 270
Cdd:COG5010  139 DEAK 142
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 130-270 5.38e-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: 47.88  E-value: 5.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 130 EDLKNIGNTFFKSQNWEMAIKKYAKVLryvdsskaviekaDRSRLQPIALscvLNIGACKLKMSNWQGAIDSCLEALEMD 209
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKAL-------------ELDPDNPEAF---ALLGEILLQLGDLDEAIVLLHEALELD 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568923769 210 PSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG4783   69 PDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLarayRALGRPDEAIAALEKAL 133
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 113-244 5.97e-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: 48.03  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 113 EDADIDLKDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKM 192
Cdd:COG5010   38 KEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ----------------LDPNNPELYYNLALLYSRS 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568923769 193 SNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAP 244
Cdd:COG5010  102 GDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 139-252 1.67e-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: 45.75  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 139 FFKSQNWEMAIKKYakvlryvdssKAVIEKADRSRLQPIALscvLNIGACKLKMSNWQGAIDSCLEALEMDPSNTK---A 215
Cdd:COG1729    3 LLKAGDYDEAIAAF----------KAFLKRYPNSPLAPDAL---YWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKapdA 69

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568923769 216 LYRKAQGWQGLKEYDQALADLKKAQEIAPG-DKAIQAE 252
Cdd:COG1729   70 LLKLGLSYLELGDYDKARATLEELIKKYPDsEAAKEAR 107
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 186-272 6.92e-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: 47.00  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769  186 GACKLKMSNWQ--GAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPgdKAIQAELLKVKQMIKAQ 263
Cdd:TIGR02917 164 GLAQLALAENRfdEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRP--NNIAVLLALATILIEAG 241


                  ....*....
gi 568923769  264 KDKEKAVYA 272
Cdd:TIGR02917 242 EFEEAEKHA 250
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
183-244 8.87e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 43.24  E-value: 8.87e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568923769 183 LNIGACKLKMSNWQGAIDsCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAP 244
Cdd:COG3063   30 NNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 173-253 1.06e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.52  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 173 RLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAE 252
Cdd:COG3914  106 ALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185


                 .
gi 568923769 253 L 253
Cdd:COG3914  186 L 186
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 190-246 2.21e-05

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 45.16  E-value: 2.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769 190 LKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:PLN03088  47 IKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQTAKAALEKGASLAPGD 103
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 198-253 2.90e-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: 42.69  E-value: 2.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568923769 198 AIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL 253
Cdd:COG4235    2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 22-69 5.82e-05

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: 42.82  E-value: 5.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769  22 GLLSMANA--GPNTNGSQFFI-------TTVPTPHLDGKHVVFGQVIKGLGVARTLE 69
Cdd:cd01924  107 GAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 134-246 5.92e-05

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: 42.10  E-value: 5.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 134 NIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNT 213
Cdd:COG4783   43 LLGEILLQLGDLDEAIVLLHEALE----------------LDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHP 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568923769 214 KALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:COG4783  107 EAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
LcrH_SycD TIGR02552
type III secretion low calcium response chaperone LcrH/SycD; Genes in this family are found in ...
 183-262 1.20e-04

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: 41.13  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769  183 LNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKA 262
Cdd:TIGR02552  55 LGLAACCQMLKEYEEAIDAYALAAALDPDDPRPYFHAAECLLALGEPESALKALDLAIEICGENPEYSELKERAEAMLES 134
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 194-270 1.79e-04

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 194 NWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKA 269
Cdd:COG2956   23 QPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaqdyLKAGLLDRAEELLEKL 102


                 .
gi 568923769 270 V 270
Cdd:COG2956  103 L 103
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 134-241 1.95e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 134 NIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNT 213
Cdd:COG3914  151 NLGEALRRLGRLEEAIAALRRALE----------------LDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214

                         90       100       110
                 ....*....|....*....|....*....|....
gi 568923769 214 KA------LYRKAQGWQGLKEYDQALADLKKAQE 241
Cdd:COG3914  215 DAhsnllfALRQACDWEVYDRFEELLAALARGPS 248
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 190-269 2.27e-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: 39.97  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568923769 190 LKMSNWQGAIDSCLEALEMDPSNT---KALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDK 266
Cdd:COG1729    4 LKAGDYDEAIAAFKAFLKRYPNSPlapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGDY 83


                 ...
gi 568923769 267 EKA 269
Cdd:COG1729   84 DKA 86
TPR_1 pfam00515
Tetratricopeptide repeat;
214-246 9.80e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.86  E-value: 9.80e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568923769  214 KALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:pfam00515   2 KALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 214-246 1.69e-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: 35.11  E-value: 1.69e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568923769   214 KALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:smart00028   2 EALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 183-212 1.74e-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: 35.11  E-value: 1.74e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568923769   183 LNIGACKLKMSNWQGAIDSCLEALEMDPSN 212
Cdd:smart00028   5 YNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
206-246 2.03e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.83  E-value: 2.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568923769 206 LEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD 41
TPR_19 pfam14559
Tetratricopeptide repeat;
194-251 3.03e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 35.25  E-value: 3.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568923769  194 NWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQA 251
Cdd:pfam14559   3 DYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAA 60
TPR_1 pfam00515
Tetratricopeptide repeat;
184-212 3.67e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 34.32  E-value: 3.67e-03
                          10        20
                  ....*....|....*....|....*....
gi 568923769  184 NIGACKLKMSNWQGAIDSCLEALEMDPSN 212
Cdd:pfam00515   6 NLGNAYFKLGKYDEALEYYEKALELNPNN 34
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 190-246 5.96e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.05  E-value: 5.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568923769 190 LKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGD 246
Cdd:COG3914   89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDF 145
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH