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Conserved domains on  [gi|1248495083|ref|NP_001343255|]
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peptidyl-prolyl cis-trans isomerase D isoform 2 [Mus musculus]

Protein Classification

cyclophilin and TPR domain-containing protein( domain architecture ID 11624249)

cyclophilin and TPR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 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 1248495083  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 1248495083 119 LKDVDKILLISED----LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSN 194
Cdd:COG0457    28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQALE----------------LDPDDAEALNNLGLALQALGR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248495083 195 WQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457    92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                  ...
gi 1248495083 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 1248495083  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 1248495083  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 1248495083  11 SRFKNRHHDReGLLSMANAG--PNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:pfam00160  70 IFPLLLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148


                  .
gi 1248495083  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 1248495083  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 1248495083 119 LKDVDKILLISED----LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSN 194
Cdd:COG0457    28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQALE----------------LDPDDAEALNNLGLALQALGR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248495083 195 WQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457    92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                  ...
gi 1248495083 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 1248495083  98 IFPKDGSGDshPDFPEDADIDLKDVDKILLiseDLKNIGNTFFKSQNWEMAIKKYakvlryvdsSKAVIEKADrsrlqPI 177
Cdd:TIGR00990 101 VEPADELPE--IDESSVANLSEEERKKYAA---KLKEKGNKAYRNKDFNKAIKLY---------SKAIECKPD-----PV 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1248495083 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 1248495083 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 1248495083 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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  11 SRFKNRHHDReGLLSMANAG--PNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECG 88
Cdd:pfam00160  70 IFPLLLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148


                  .
gi 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083  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 1248495083 119 LKDVDKILLISED----LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSN 194
Cdd:COG0457    28 IEDYEKALELDPDdaeaLYNLGLAYLRLGRYEEALADYEQALE----------------LDPDDAEALNNLGLALQALGR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248495083 195 WQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKAV 270
Cdd:COG0457    92 YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLgialEKLGRYEEALELLEKLE 171


                  ...
gi 1248495083 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 1248495083 132 LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPS 211
Cdd:COG3914   115 LFNLGNLLLALGRLEEALAALRRALA----------------LNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPD 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1248495083 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 1248495083 132 LKNIGNTFFKSQNWEMAIKKYAKVLryvdsskaviekadrsRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPS 211
Cdd:COG0457    11 YNNLGLAYRRLGRYEEAIEDYEKAL----------------ELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248495083 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 1248495083  98 IFPKDGSGDshPDFPEDADIDLKDVDKILLiseDLKNIGNTFFKSQNWEMAIKKYakvlryvdsSKAVIEKADrsrlqPI 177
Cdd:TIGR00990 101 VEPADELPE--IDESSVANLSEEERKKYAA---KLKEKGNKAYRNKDFNKAIKLY---------SKAIECKPD-----PV 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1248495083 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 1248495083 132 LKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPS 211
Cdd:COG0457    79 LNNLGLALQALGRYEEALEDYDKALE----------------LDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPD 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248495083 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 1248495083 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 1248495083 130 EDLKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMD 209
Cdd:COG4785    74 QLYYERGVAYDSLGDYDLAIADFDQALE----------------LDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248495083 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 1248495083 130 EDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSSKAVIekadrsrlqpialscvLNIGACKLKMSNWQGAIDSCLEALEMD 209
Cdd:COG4235    18 EGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADAL----------------LDLAEALLAAGDTEEAEELLERALALD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1248495083 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 1248495083 132 LKNIGNTFFKSQNWEMAIKKYAKVL-RYVDSSKAVIEKA---------DRS--------RLQPIALSCVLNIGACKLKMS 193
Cdd:COG2956    45 HLALGNLYRRRGEYDRAIRIHQKLLeRDPDRAEALLELAqdylkagllDRAeellekllELDPDDAEALRLLAEIYEQEG 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248495083 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 1248495083 132 LKNIGNTFFKSQNWEMAIKKYAKVLRYV-DSSKAVIEKADRSRLQ-----------------PIALSCVLNIGACKLKMS 193
Cdd:COG2956   113 LRLLAEIYEQEGDWEKAIEVLERLLKLGpENAHAYCELAELYLEQgdydeaiealekalkldPDCARALLLLAELYLEQG 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248495083 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 1248495083 183 LNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVkqMIKA 262
Cdd:COG4783     8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA--LLKA 85

                          90
                  ....*....|..
gi 1248495083 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 1248495083 163 KAVIEKADRSRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEI 242
Cdd:COG4785    57 ALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL 136


                  ....
gi 1248495083 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 1248495083 187 ACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVkqmIKAQKDK 266
Cdd:COG5010    62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAAL---LLSLGQD 138


                  ....
gi 1248495083 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 1248495083 130 EDLKNIGNTFFKSQNWEMAIKKYAKVLryvdsskaviekaDRSRLQPIALscvLNIGACKLKMSNWQGAIDSCLEALEMD 209
Cdd:COG4783     5 EALYALAQALLLAGDYDEAEALLEKAL-------------ELDPDNPEAF---ALLGEILLQLGDLDEAIVLLHEALELD 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1248495083 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 1248495083 113 EDADIDLKDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKM 192
Cdd:COG5010    38 KEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ----------------LDPNNPELYYNLALLYSRS 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1248495083 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 1248495083 139 FFKSQNWEMAIKKYakvlryvdssKAVIEKADRSRLQPIALscvLNIGACKLKMSNWQGAIDSCLEALEMDPSNTK---A 215
Cdd:COG1729     3 LLKAGDYDEAIAAF----------KAFLKRYPNSPLAPDAL---YWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKapdA 69

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1248495083 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 1248495083 186 GACKLKMSNWQ--GAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPgdKAIQAELLKVKQMIKAQ 263
Cdd:TIGR02917 164 GLAQLALAENRfdEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRP--NNIAVLLALATILIEAG 241


                  ....*....
gi 1248495083 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 1248495083 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 1248495083 173 RLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAE 252
Cdd:COG3914   106 ALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN 185


                  .
gi 1248495083 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 1248495083 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 1248495083 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 1248495083  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 1248495083 134 NIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNT 213
Cdd:COG4783    43 LLGEILLQLGDLDEAIVLLHEALE----------------LDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHP 106

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1248495083 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 1248495083 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 1248495083 194 NWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAEL----LKVKQMIKAQKDKEKA 269
Cdd:COG2956    23 QPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELaqdyLKAGLLDRAEELLEKL 102


                  .
gi 1248495083 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 1248495083 134 NIGNTFFKSQNWEMAIKKYAKVLRyvdsskaviekadrsrLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNT 213
Cdd:COG3914   151 NLGEALRRLGRLEEAIAALRRALE----------------LDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNA 214

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1248495083 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 1248495083 190 LKMSNWQGAIDSCLEALEMDPSNT---KALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDK 266
Cdd:COG1729     4 LKAGDYDEAIAAFKAFLKRYPNSPlapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGDY 83


                  ...
gi 1248495083 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 1248495083 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 1248495083  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 1248495083  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 1248495083 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 1248495083 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 1248495083 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 1248495083 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.
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