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Conserved domains on  [gi|2076534481|gb|KAG8497521|]
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hypothetical protein CXB51_008943 [Gossypium anomalum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 112-279 1.01e-101

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: 301.10  E-value: 1.01e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 112 PRCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGEKGIGpntGASLHYKGVRFHRIIRGFMIQGGDISAGDGTGG 191
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 192 ESIYDLKFEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGdYPTQ 271
Cdd:cd01926    78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNG-KPKK 156


                  ....*...
gi 2076534481 272 EVIIADCG 279
Cdd:cd01926   157 KVVIADCG 164
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 406-439 1.88e-07

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: 47.06  E-value: 1.88e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2076534481  406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 380-452 6.03e-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: 6.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076534481 380 ACKLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:COG5010    62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS 134
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 318-476 4.13e-06

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


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 46.34  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 318 EAVDSIKAVGNEQYKKQDYKIALRKYWKALRYSDEcwelegidevkSSKLRKIKSQIFtnssackLKLGDLKGALLDTDF 397
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPD-----------NPEAFALLGEIL-------LQLGDLDEAIVLLHE 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076534481 398 AIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKKvcpssiliAERRDQEKRAYSRMFQ 476
Cdd:COG4783    64 ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA--------LGRPDEAIAALEKALE 134
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 112-279 1.01e-101

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: 301.10  E-value: 1.01e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 112 PRCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGEKGIGpntGASLHYKGVRFHRIIRGFMIQGGDISAGDGTGG 191
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 192 ESIYDLKFEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGdYPTQ 271
Cdd:cd01926    78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNG-KPKK 156


                  ....*...
gi 2076534481 272 EVIIADCG 279
Cdd:cd01926   157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 111-281 7.15e-86

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 261.32  E-value: 7.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 111 NPRCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGEKGIGPntGASLHYKGVRFHRIIRGFMIQGGDISAGDGTG 190
Cdd:PTZ00060   15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSS--GKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 191 GESIYDLKFEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGdYPT 270
Cdd:PTZ00060   93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPK 171

                         170
                  ....*....|.
gi 2076534481 271 QEVIIADCGEI 281
Cdd:PTZ00060  172 KPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 125-280 1.26e-60

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


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 195.17  E-value: 1.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 125 EGRIVIELYKDIVPKTAENFRALCTgeKGigpntgaslHYKGVRFHRIIRGFMIQGGDISaGDGTGGESIYDlkFEDENF 204
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 205 --ELKHERkGMLSMANMG--PNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATdDGDYPTQEVIIADCGE 280
Cdd:pfam00160  72 plLLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT-DGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 126-275 6.35e-59

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 191.15  E-value: 6.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCtgEKGigpntgaslHYKGVRFHRIIRGFMIQGGDISaGDGTGGEsiyDLKFEDENF- 204
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076534481 205 ELKHERkGMLSMAN-MGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEVII 275
Cdd:COG0652    81 GLKHKR-GTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 151
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 406-439 1.88e-07

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: 47.06  E-value: 1.88e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2076534481  406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 405-450 2.43e-07

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 49.62  E-value: 2.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2076534481 405 NVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAAR 450
Cdd:COG4235    16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEAL 61
TPR_1 pfam00515
Tetratricopeptide repeat;
406-439 2.60e-07

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 46.65  E-value: 2.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2076534481 406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 380-452 6.03e-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: 6.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076534481 380 ACKLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:COG5010    62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS 134
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 318-476 4.13e-06

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 46.34  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 318 EAVDSIKAVGNEQYKKQDYKIALRKYWKALRYSDEcwelegidevkSSKLRKIKSQIFtnssackLKLGDLKGALLDTDF 397
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPD-----------NPEAFALLGEIL-------LQLGDLDEAIVLLHE 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076534481 398 AIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKKvcpssiliAERRDQEKRAYSRMFQ 476
Cdd:COG4783    64 ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA--------LGRPDEAIAALEKALE 134
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 405-443 1.48e-03

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


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2076534481 405 NVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIK 443
Cdd:cd24142    33 NVEALELLGEILLELGDVEEAREVLLRAIELDPDGGYEK 71
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 372-451 1.77e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 372 SQIFTNSSACKLKLGDL-KGALLDTDFAIRDGEyNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPN------------ 438
Cdd:TIGR02917 363 PAALSLLGEAYLALGDFeKAAEYLAKATELDPE-NAAARTQLGISKLSQGDPSEAIADLETAAQLDPElgradlllilsy 441

                          90
                  ....*....|....*
gi 2076534481 439 --DGGIKKELAAARK 451
Cdd:TIGR02917 442 lrSGQFDKALAAAKK 456
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 112-279 1.01e-101

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: 301.10  E-value: 1.01e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 112 PRCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGEKGIGpntGASLHYKGVRFHRIIRGFMIQGGDISAGDGTGG 191
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 192 ESIYDLKFEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGdYPTQ 271
Cdd:cd01926    78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNG-KPKK 156


                  ....*...
gi 2076534481 272 EVIIADCG 279
Cdd:cd01926   157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 111-281 7.15e-86

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 261.32  E-value: 7.15e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 111 NPRCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGEKGIGPntGASLHYKGVRFHRIIRGFMIQGGDISAGDGTG 190
Cdd:PTZ00060   15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSS--GKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 191 GESIYDLKFEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGdYPT 270
Cdd:PTZ00060   93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YPK 171

                         170
                  ....*....|.
gi 2076534481 271 QEVIIADCGEI 281
Cdd:PTZ00060  172 KPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 111-281 1.43e-71

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 224.71  E-value: 1.43e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 111 NPRCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGE--KGigpntGASLHYKGVRFHRIIRGFMIQGGDISAGDG 188
Cdd:PLN03149   18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrKA-----GLPQGYKGCQFHRVIKDFMIQGGDFLKGDG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 189 TGGESIYDLKFEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVI-KGMGVVRSIEHVATDDGD 267
Cdd:PLN03149   93 TGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNN 172

                         170
                  ....*....|....
gi 2076534481 268 YPTQEVIIADCGEI 281
Cdd:PLN03149  173 RPKLACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 115-277 2.88e-68

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 214.82  E-value: 2.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 115 YMDISIGgelegRIVIELYKDIVPKTAENFRALCTGEkgigpntgaslHYKGVRFHRIIRGFMIQGGDISAGDGTGGESI 194
Cdd:cd00317     1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLARGG-----------FYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 195 YdlKFEDENFELK-HERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEV 273
Cdd:cd00317    65 Y--KFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPV 142


                  ....
gi 2076534481 274 IIAD 277
Cdd:cd00317   143 TISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 125-280 1.26e-60

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


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 195.17  E-value: 1.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 125 EGRIVIELYKDIVPKTAENFRALCTgeKGigpntgaslHYKGVRFHRIIRGFMIQGGDISaGDGTGGESIYDlkFEDENF 204
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 205 --ELKHERkGMLSMANMG--PNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATdDGDYPTQEVIIADCGE 280
Cdd:pfam00160  72 plLLKHKR-GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT-DGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 126-275 6.35e-59

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 191.15  E-value: 6.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCtgEKGigpntgaslHYKGVRFHRIIRGFMIQGGDISaGDGTGGEsiyDLKFEDENF- 204
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076534481 205 ELKHERkGMLSMAN-MGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEVII 275
Cdd:COG0652    81 GLKHKR-GTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 151
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 126-275 3.59e-56

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: 183.43  E-value: 3.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCtgEKGigpntgaslHYKGVRFHRIIRGFMIQGGDiSAGDGTGGESIYDLKFEDE-NF 204
Cdd:cd01927     7 GDIHIRLFPEEAPKTVENFTTHA--RNG---------YYNNTIFHRVIKGFMIQTGD-PTGDGTGGESIWGKEFEDEfSP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076534481 205 ELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEVII 275
Cdd:cd01927    75 SLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKI 145
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 126-277 6.46e-55

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: 180.32  E-value: 6.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCtgekgigpntgASLHYKGVRFHRIIRGFMIQGGDiSAGDGTGGESIYDLKFEDENFE 205
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALC-----------ASGYYNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFRE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076534481 206 -LKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEVIIAD 277
Cdd:cd01928    78 tLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 126-277 3.30e-52

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: 173.76  E-value: 3.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCtgEKGigpntgaslHYKGVRFHRIIRGFMIQGGDISaGDGTGGESIYDLKFEDE-NF 204
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC--KKG---------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKP 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076534481 205 ELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEVIIAD 277
Cdd:cd01923    77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIED 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 126-275 1.90e-46

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling.


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 158.08  E-value: 1.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCTgeKGigpntgaslHYKGVRFHRIIRGFMIQGGDiSAGDGTGGESIYDLKFEDE-NF 204
Cdd:cd01922     7 GEITLELYWNHAPKTCKNFYELAK--RG---------YYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiHP 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2076534481 205 ELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDgDYPTQEVII 275
Cdd:cd01922    75 ELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKI 144
PTZ00221 PTZ00221
cyclophilin; Provisional
 113-279 5.39e-40

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 144.24  E-value: 5.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 113 RCYMDISIGGELEGRIVIELYKDIVPKTAENFRALCTGEKGIGPNTGASLHYKGVRFHRIIR--GFMIQGGDISAGDGTG 190
Cdd:PTZ00221   54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVDRnnNIIVLGELDSFNVSST 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 191 GESIydlkfEDENFELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPT 270
Cdd:PTZ00221  134 GTPI-----ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPL 208


                  ....*....
gi 2076534481 271 QEVIIADCG 279
Cdd:PTZ00221  209 LPVTVSFCG 217
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 126-269 5.43e-36

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: 130.93  E-value: 5.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCTGEkgigpntgaslHYKGVRFHRIIRGFMIQGGDISaGDGTGGESIYDLKFEDE-NF 204
Cdd:cd01925    15 GDIDIELWSKEAPKACRNFIQLCLEG-----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076534481 205 ELKHERKGMLSMANMGPNTNGSQFFITTTRTPHLDVKHVVFGKVIKG--MGVVRsIEHVATDDGDYP 269
Cdd:cd01925    83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDtiYNLLK-LAEVETDKDERP 148
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 125-275 2.13e-28

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: 110.12  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 125 EGRIVIELYKDIVPKTAENFRALCTgekgigpntgaSLHYKGVRFHRIIRGFMIQGGDISaGDGTGGESIYDLK------ 198
Cdd:cd01921     6 LGDLVIDLFTDECPLACLNFLKLCK-----------LKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqar 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 199 -FEDE-NFELKHERKGMLSMANMGPNTNGSQFFITTTR-TPHLDVKHVVFGKVIKGMGVVRSIEHVATDDGDYPTQEVII 275
Cdd:cd01921    74 fFEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 126-277 5.96e-22

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 92.12  E-value: 5.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCtgEKGigpntgaslHYKGVRFHRIIRGFMIQGGDISAgDGTGGESIYDLKFEDENfE 205
Cdd:cd01920     7 GDIVVELYDDKAPITVENFLAYV--RKG---------FYDNTIFHRVISGFVIQGGGFTP-DLAQKETLKPIKNEAGN-G 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 206 LKHERkGMLSMANMG-PNTNGSQFFITTTRTPHLDVK-----HVVFGKVIKGMGVVRSIEHVATDDG----DYPTQEVII 275
Cdd:cd01920    74 LSNTR-GTIAMARTNaPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPVQDVII 152


                  ..
gi 2076534481 276 AD 277
Cdd:cd01920   153 ES 154
PRK10903 PRK10903
peptidylprolyl isomerase A;
125-282 3.74e-16

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 76.42  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 125 EGRIVIELYKDIVPKTAENFRALCtgekgigpNTGaslHYKGVRFHRIIRGFMIQGGDISAgdgtggesiyDLKFEDENF 204
Cdd:PRK10903   37 AGNIELELNSQKAPVSVKNFVDYV--------NSG---FYNNTTFHRVIPGFMIQGGGFTE----------QMQQKKPNP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 205 ELKHE-------RKGMLSMANMG-PNTNGSQFFITTTRTPHL-----DVKHVVFGKVIKGMGVVRSIEHVATDD-GDY-- 268
Cdd:PRK10903   96 PIKNEadnglrnTRGTIAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKISQVPTHDvGPYqn 175

                         170
                  ....*....|....*
gi 2076534481 269 -PTQEVIIADCGEIP 282
Cdd:PRK10903  176 vPSKPVVILSAKVLP 190
PRK10791 PRK10791
peptidylprolyl isomerase B;
126-275 1.42e-13

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 68.33  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 126 GRIVIELYKDIVPKTAENFRALCTgeKGIGPNTgaslhykgvRFHRIIRGFMIQGGDISAGdgtggesiydLKFEDENFE 205
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYCR--EGFYNNT---------IFHRVINGFMIQGGGFEPG----------MKQKATKEP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 206 LKHE-------RKGMLSMANMG-PNTNGSQFFITTTRTPHLDVK--------HVVFGKVIKGMGVVRSIEHVATDDG--- 266
Cdd:PRK10791   68 IKNEannglknTRGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmh 147

                         170
                  ....*....|
gi 2076534481 267 -DYPTQEVII 275
Cdd:PRK10791  148 qDVPKEDVII 157
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 127-259 1.86e-11

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: 62.46  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 127 RIVIELYKdiVPKTAENFRALCtgEKGIgpntgaslhYKGVRFHRIIRGFMIQGGD-----------------------I 183
Cdd:cd01924    10 TIVLDGYN--APVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGDpqgknpgfpdpetgksrtipleiK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 184 SAGDG--TGGESIYDLKFEDENFELKHERKGMLSMAN--MGPNTNGSQFFI-------TTTRTPHLDVKHVVFGKVIKGM 252
Cdd:cd01924    77 PEGQKqpVYGKTLEEAGRYDEQPVLPFNAFGAIAMARteFDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGL 156


                  ....*..
gi 2076534481 253 GVVRSIE 259
Cdd:cd01924   157 DILRELK 163
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 406-439 1.88e-07

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: 47.06  E-value: 1.88e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2076534481  406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 405-450 2.43e-07

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 49.62  E-value: 2.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2076534481 405 NVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAAR 450
Cdd:COG4235    16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEAL 61
TPR_1 pfam00515
Tetratricopeptide repeat;
406-439 2.60e-07

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 46.65  E-value: 2.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2076534481 406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 380-452 6.03e-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: 6.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076534481 380 ACKLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:COG5010    62 NLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS 134
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 382-449 7.25e-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: 48.65  E-value: 7.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076534481 382 KLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG4783    14 LLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
383-452 1.25e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.62  E-value: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:COG0457    19 RRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
339-449 1.77e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 49.23  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 339 ALRKYWKALRYSDECWELEGIDevkssklrkikSQIFTNSSACKLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMA 418
Cdd:COG0457    20 RLGRYEEAIEDYEKALELDPDD-----------AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2076534481 419 LNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG0457    89 LGRYEEALEDYDKALELDPDDAEALYNLGLA 119
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 406-438 2.24e-06

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


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 44.05  E-value: 2.24e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2076534481 406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPN 438
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
327-452 2.88e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.46  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 327 GNEQYKKQDYKIALRKYWKALRYSDECwelegidevkssklrkikSQIFTNSSACKLKLGDLKGALLDTDFAIRDGEYNV 406
Cdd:COG0457    49 GLAYLRLGRYEEALADYEQALELDPDD------------------AEALNNLGLALQALGRYEEALEDYDKALELDPDDA 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2076534481 407 KAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:COG0457   111 EALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEK 156
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 318-476 4.13e-06

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 46.34  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 318 EAVDSIKAVGNEQYKKQDYKIALRKYWKALRYSDEcwelegidevkSSKLRKIKSQIFtnssackLKLGDLKGALLDTDF 397
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPD-----------NPEAFALLGEIL-------LQLGDLDEAIVLLHE 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076534481 398 AIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKKvcpssiliAERRDQEKRAYSRMFQ 476
Cdd:COG4783    64 ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRA--------LGRPDEAIAALEKALE 134
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
381-440 8.31e-06

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.83  E-value: 8.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 381 CKLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDG 440
Cdd:COG4785    82 AYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYA 141
TPR_8 pfam13181
Tetratricopeptide repeat;
406-438 2.06e-05

Tetratricopeptide repeat;


Pssm-ID: 404131 [Multi-domain]  Cd Length: 33  Bit Score: 41.23  E-value: 2.06e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2076534481 406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPN 438
Cdd:pfam13181   1 AEAYYNLGLIYLKLGDYEEAKEYYEKALELDPD 33
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
383-471 3.47e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.46  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIEsFKKALDLEPNDGGIKKELAAarkkvcpssILIAE 462
Cdd:COG3063     3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAE---------LLLEL 72


                  ....*....
gi 2076534481 463 RRDQEKRAY 471
Cdd:COG3063    73 GDYDEALAY 81
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 383-449 9.21e-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: 42.30  E-value: 9.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2076534481 383 LKLGDLKGALLDTDFAIR-DGEyNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG4235    28 LRLGRYDEALAAYEKALRlDPD-NADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA 94
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 383-447 1.30e-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: 43.56  E-value: 1.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELA 447
Cdd:COG2956   121 EQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLA 185
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 383-449 1.59e-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: 43.56  E-value: 1.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG2956   155 LEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAEL 221
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
304-439 1.62e-04

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 42.98  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 304 ADLDKKSDEISWWMEAVDSIKAVGNEQYKKQDYKIALRKYWKALRYSDEcwelegidevkssklrkiKSQIFTNSSACKL 383
Cdd:COG4785    57 ALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPD------------------LAEAYNNRGLAYL 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2076534481 384 KLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:COG4785   119 LLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPND 174
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 327-449 1.75e-04

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 327 GNEQYKKQDYKIALRKYWKALRYSDEcwelegidevkssklrkiKSQIFTNSSACKLKLGDLKGALLDTDFAIRDGEYNV 406
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPD------------------NADALLDLAEALLAAGDTEEAEELLERALALDPDNP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2076534481 407 KAFFRQGQAYMALNDIDSAIESFKKALDLEPND---GGIKKELAAA 449
Cdd:COG4235    86 EALYLLGLAAFQQGDYAEAIAAWQKLLALLPADapaRLLEASIAEA 131
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 327-454 2.40e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.83  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 327 GNEQYKKQDYKIALRKYWKALRYSDECWElegidevkssklrkiksqIFTNSSACKLKLGDLKGALLDTDFAIRDGEYNV 406
Cdd:COG3914   119 GNLLLALGRLEEALAALRRALALNPDFAE------------------AYLNLGEALRRLGRLEEAIAALRRALELDPDNA 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2076534481 407 KAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKKVC 454
Cdd:COG3914   181 EALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQAC 228
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 383-439 4.00e-04

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: 40.56  E-value: 4.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:COG4783    83 LKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 383-449 4.57e-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: 4.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG2956    87 LKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAEL 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 398-449 6.09e-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: 41.64  E-value: 6.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2076534481 398 AIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG2956    68 LLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEI 119
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 372-437 1.29e-03

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: 39.56  E-value: 1.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2076534481 372 SQIFTNSSACKLKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEP 437
Cdd:COG5010    88 PELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 405-443 1.48e-03

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


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 40.69  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2076534481 405 NVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIK 443
Cdd:cd24142    33 NVEALELLGEILLELGDVEEAREVLLRAIELDPDGGYEK 71
TPR_11 pfam13414
TPR repeat;
413-452 1.53e-03

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 36.30  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2076534481 413 GQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 372-451 1.77e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076534481 372 SQIFTNSSACKLKLGDL-KGALLDTDFAIRDGEyNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPN------------ 438
Cdd:TIGR02917 363 PAALSLLGEAYLALGDFeKAAEYLAKATELDPE-NAAARTQLGISKLSQGDPSEAIADLETAAQLDPElgradlllilsy 441

                          90
                  ....*....|....*
gi 2076534481 439 --DGGIKKELAAARK 451
Cdd:TIGR02917 442 lrSGQFDKALAAAKK 456
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 401-439 2.02e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.05  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2076534481 401 DGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:COG1729    25 NSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDS 63
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 383-449 2.59e-03

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: 38.40  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG5010    31 LAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALL 97
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 383-452 2.84e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 37.66  E-value: 2.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076534481 383 LKLGDLKGALLDTDFAIR---DGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDggikKELAAARKK 452
Cdd:COG1729    41 YALGDYDEAAEAFEKLLKrypDSPKAPDALLKLGLSYLELGDYDKARATLEELIKKYPDS----EAAKEARAR 109
TPR_6 pfam13174
Tetratricopeptide repeat;
408-438 3.47e-03

Tetratricopeptide repeat;


Pssm-ID: 463800 [Multi-domain]  Cd Length: 33  Bit Score: 35.14  E-value: 3.47e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2076534481 408 AFFRQGQAYMALNDIDSAIESFKKALDLEPN 438
Cdd:pfam13174   2 ALLKLALAYLELGDTDEAKEALERLIKKYPD 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
405-452 4.32e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.83  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2076534481 405 NVKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAARKK 452
Cdd:COG0457     7 DAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLR 54
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 383-439 5.46e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.21  E-value: 5.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2076534481 383 LKLGDLKGALLDTDFAIRDGEYNVKAFFRQGQAYMALNDIDSAIESFKKALDLEPND 439
Cdd:COG3914    89 QALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDF 145
TPR_14 pfam13428
Tetratricopeptide repeat;
406-449 8.09e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 34.32  E-value: 8.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2076534481 406 VKAFFRQGQAYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:pfam13428   1 PEALLALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
415-449 8.29e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.92  E-value: 8.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2076534481 415 AYMALNDIDSAIESFKKALDLEPNDGGIKKELAAA 449
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLL 35
 
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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