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Conserved domains on  [gi|1191857485|ref|XP_020939137|]
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peptidyl-prolyl cis-trans isomerase FKBP8 isoform X1 [Sus scrofa]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446594)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0000413|GO:0061077
PubMed:  27664121
SCOP:  4001062

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
114-203 2.63e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 87.64  E-value: 2.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 114 GSSRPTKGQVVTVQLQTSLENGTRVQ----EEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGSRSPY 189
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDssydRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGPV 80

                          90
                  ....*....|....
gi 1191857485 190 IPPHAALCLEVTLK 203
Cdd:pfam00254  81 IPPNATLVFEVELL 94
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 216-348 2.48e-11

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


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.40  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 216 GQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLK---VKCLNNLAASQLKLDHYRA 292
Cdd:COG3914    64 AGEAAAAAAALLLLAALLELAALLLQALGRYEEALALY-------------RRALALNpdnAEALFNLGNLLLALGRLEE 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1191857485 293 ALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG3914   131 ALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
114-203 2.63e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 87.64  E-value: 2.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 114 GSSRPTKGQVVTVQLQTSLENGTRVQ----EEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGSRSPY 189
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDssydRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGPV 80

                          90
                  ....*....|....
gi 1191857485 190 IPPHAALCLEVTLK 203
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 103-202 2.29e-12

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 62.89  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 103 LRKKTLVPGppGSSRPTKGQVVTVQLQTSLENGT----RVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKY 178
Cdd:COG0545     1 LQYKVLKEG--TGAKPKAGDTVTVHYTGTLLDGTvfdsSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPEL 78

                          90       100
                  ....*....|....*....|....
gi 1191857485 179 CYGPQGSrSPYIPPHAALCLEVTL 202
Cdd:COG0545    79 AYGERGA-GGVIPPNSTLVFEVEL 101
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 216-348 2.48e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.40  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 216 GQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLK---VKCLNNLAASQLKLDHYRA 292
Cdd:COG3914    64 AGEAAAAAAALLLLAALLELAALLLQALGRYEEALALY-------------RRALALNpdnAEALFNLGNLLLALGRLEE 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1191857485 293 ALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG3914   131 ALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 230-379 3.40e-05

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: 46.23  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 230 GNAHYQRADFVLAANSYDLAIK-------AITSSAKVDMTFEEEEQLLQL----------KVKCLNNLAASQLKLDHYRA 292
Cdd:TIGR02917 132 GLAYLGLGQLELAQKSYEQALAidprslyAKLGLAQLALAENRFDEARALidevltadpgNVDALLLKGDLLLSLGNIEL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 293 ALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKL---EPSNKTIHAELSKLVKKHAAQRSTETALYRKm 369
Cdd:TIGR02917 212 ALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKapnSPLAHYLKALVDFQKKNYEDARETLQDALKS- 290

                         170
                  ....*....|
gi 1191857485 370 lgNPSRLPAK 379
Cdd:TIGR02917 291 --APEYLPAL 298
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 279-341 6.84e-05

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: 44.54  E-value: 6.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191857485 279 NLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:cd24142     5 EKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDG 67
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 308-341 9.73e-05

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: 39.35  E-value: 9.73e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1191857485  308 IKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
308-341 1.07e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 38.94  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1191857485 308 IKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
114-203 2.63e-21

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 87.64  E-value: 2.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 114 GSSRPTKGQVVTVQLQTSLENGTRVQ----EEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGSRSPY 189
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDssydRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGPV 80

                          90
                  ....*....|....
gi 1191857485 190 IPPHAALCLEVTLK 203
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 103-202 2.29e-12

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 62.89  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 103 LRKKTLVPGppGSSRPTKGQVVTVQLQTSLENGT----RVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKY 178
Cdd:COG0545     1 LQYKVLKEG--TGAKPKAGDTVTVHYTGTLLDGTvfdsSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPEL 78

                          90       100
                  ....*....|....*....|....
gi 1191857485 179 CYGPQGSrSPYIPPHAALCLEVTL 202
Cdd:COG0545    79 AYGERGA-GGVIPPNSTLVFEVEL 101
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 216-348 2.48e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.40  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 216 GQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLK---VKCLNNLAASQLKLDHYRA 292
Cdd:COG3914    64 AGEAAAAAAALLLLAALLELAALLLQALGRYEEALALY-------------RRALALNpdnAEALFNLGNLLLALGRLEE 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1191857485 293 ALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG3914   131 ALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
221-348 7.02e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.95  E-value: 7.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 221 ALANRkrecGNAHYQRADFVLAANSYDLAIKAITSSAKVdmtfeeeeqllqlkvkcLNNLAASQLKLDHYRAALRSCSLV 300
Cdd:COG0457    10 AYNNL----GLAYRRLGRYEEAIEDYEKALELDPDDAEA-----------------LYNLGLAYLRLGRYEEALADYEQA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1191857485 301 LEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG0457    69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNL 116
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
231-348 1.08e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.56  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 231 NAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEeeqllqlkvkCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKA 310
Cdd:COG0457    43 EALYNLGLAYLRLGRYEEALADYEQALELDPDDAE----------ALNNLGLALQALGRYEEALEDYDKALELDPDDAEA 112

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1191857485 311 LFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG0457   113 LYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 221-348 1.82e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 62.70  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 221 ALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMT----------FEEEEQLLQ--LKVK-----CLNNLAAS 283
Cdd:COG3914    76 LLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNlgnlllalgrLEEALAALRraLALNpdfaeAYLNLGEA 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191857485 284 QLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG3914   156 LRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL 220
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 277-348 6.49e-09

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: 54.04  E-value: 6.49e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191857485 277 LNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG4783     7 LYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
180-341 1.73e-08

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 54.54  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 180 YGPQGSRSPYIPPHAALCLevTLKAAVDGPDLEMLTGQERVALANRkrecGNAHYQRADFVLAANSYDLAIKAITSSAKV 259
Cdd:COG4785    36 ALAIALADLALALAAAALA--AAALAAERIDRALALPDLAQLYYER----GVAYDSLGDYDLAIADFDQALELDPDLAEA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 260 dmtfeeeeqllqlkvkcLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEP 339
Cdd:COG4785   110 -----------------YNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDP 172


                  ..
gi 1191857485 340 SN 341
Cdd:COG4785   173 ND 174
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 232-378 2.02e-08

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.15  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 232 AHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEEQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKAL 311
Cdd:COG3914    36 ALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEAL 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 312 FRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLvkkHAAQRSTETAL--YRKMLG-NPSRLPA 378
Cdd:COG3914   116 FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEA---LRRLGRLEEAIaaLRRALElDPDNAEA 182
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 230-341 3.26e-08

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: 51.93  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 230 GNAHYQRADFVLAANSYDLAIKAITSSAKVdmtfeeeeqllqlkvkcLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIK 309
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADA-----------------LLDLAEALLAAGDTEEAEELLERALALDPDNPE 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1191857485 310 ALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:COG4235    87 ALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 232-373 5.15e-08

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 51.88  E-value: 5.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 232 AHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEEQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKAL 311
Cdd:COG5010    12 LYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELY 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191857485 312 FRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNP 373
Cdd:COG5010    92 YNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 222-370 9.27e-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: 53.19  E-value: 9.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 222 LANRKRECGNAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLKVKCLN---NLAASQLKLDHYRAALRSCS 298
Cdd:COG2956   136 LLKLGPENAHAYCELAELYLEQGDYDEAIEAL-------------EKALKLDPDCARallLLAELYLEQGDYEEAIAALE 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191857485 299 LVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNktihAELSKLVKKHAAQRSTETA--LYRKML 370
Cdd:COG2956   203 RALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSD----DLLLALADLLERKEGLEAAlaLLERQL 272
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 231-374 9.62e-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: 53.19  E-value: 9.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 231 NAHYQRADFVLAANSYDLAIKaitssakvdmTFEEEEQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKA 310
Cdd:COG2956   111 EALRLLAEIYEQEGDWEKAIE----------VLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARA 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191857485 311 LFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNPS 374
Cdd:COG2956   181 LLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPS 244
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 228-373 1.16e-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: 50.58  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 228 ECGNAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLK---VKCLNNLAASQLKLDHYRAALRSCSLVLEHQ 304
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALL-------------EKALELDpdnPEAFALLGEILLQLGDLDEAIVLLHEALELD 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191857485 305 PDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNP 373
Cdd:COG4783    69 PDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 279-348 1.47e-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: 50.00  E-value: 1.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 279 NLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG4235    22 LLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLL 91
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
284-351 1.70e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.01  E-value: 1.70e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191857485 284 QLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPiLRAALKLEPSNKTIHAELSKL 351
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAEL 68
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 234-370 5.83e-07

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 50.50  E-value: 5.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 234 YQRADFVLAANSYDLAIKAITSSAKVDmtfEEEEQLlqlkvkcLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFR 313
Cdd:COG2956    12 YFKGLNYLLNGQPDKAIDLLEEALELD---PETVEA-------HLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1191857485 314 KGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLvkkHAAQRSTETAL--YRKML 370
Cdd:COG2956    82 LAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEI---YEQEGDWEKAIevLERLL 137
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 232-378 7.52e-07

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 50.11  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 232 AHYQRADFVLAANSYDLAIKAITSSAKVDmtfEEEEQLLQlkvkclnNLAASQLKLDHYRAALRSCSLVLEHQPDNIKAL 311
Cdd:COG2956    44 AHLALGNLYRRRGEYDRAIRIHQKLLERD---PDRAEALL-------ELAQDYLKAGLLDRAEELLEKLLELDPDDAEAL 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 312 FRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLvkkHAAQRSTETAL--YRKMLG-NPSRLPA 378
Cdd:COG2956   114 RLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAEL---YLEQGDYDEAIeaLEKALKlDPDCARA 180
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
231-366 2.38e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.46  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 231 NAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLK---VKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDN 307
Cdd:COG0457    77 EALNNLGLALQALGRYEEALEDY-------------DKALELDpddAEALYNLGLALLELGRYDEAIEAYERALELDPDD 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1191857485 308 IKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALY 366
Cdd:COG0457   144 ADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLA 202
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 222-378 2.80e-06

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.57  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 222 LANRKRECGNAHYQRADFVLAANSYDLAIKAItssakvdmtfeeeEQLLQLK---VKCLNNLAASQLKLDHYRAALRSCS 298
Cdd:COG2956    68 LLERDPDRAEALLELAQDYLKAGLLDRAEELL-------------EKLLELDpddAEALRLLAEIYEQEGDWEKAIEVLE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 299 LVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLvkkHAAQRSTETAL--YRKMLG-NPSR 375
Cdd:COG2956   135 RLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL---YLEQGDYEEAIaaLERALEqDPDY 211


                  ...
gi 1191857485 376 LPA 378
Cdd:COG2956   212 LPA 214
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
277-340 3.94e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.16  E-value: 3.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191857485 277 LNNLAASQLKLDHYRAALRsCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPS 340
Cdd:COG3063    29 LNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 232-341 4.19e-06

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 45.95  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 232 AHYQRADFVLAANSYDLAIKAITSSAKVDmtfEEEEQLLqlkvkclNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKAL 311
Cdd:COG4783    40 AFALLGEILLQLGDLDEAIVLLHEALELD---PDEPEAR-------LNLGLALLKAGDYDEALALLEKALKLDPEHPEAY 109

                          90       100       110
                  ....*....|....*....|....*....|
gi 1191857485 312 FRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:COG4783   110 LRLARAYRALGRPDEAIAALEKALELDPDD 139
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 232-350 1.04e-05

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 44.21  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 232 AHYQRADFVLAANSYDLAIKAITSSAKVDmtfeeeeqllqlkvKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIK-- 309
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPLAP--------------DALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKap 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1191857485 310 -ALFRKGKVLAQQGEYSEAIPILRAALKLEPsnKTIHAELSK 350
Cdd:COG1729    68 dALLKLGLSYLELGDYDKARATLEELIKKYP--DSEAAKEAR 107
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 230-379 3.40e-05

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: 46.23  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 230 GNAHYQRADFVLAANSYDLAIK-------AITSSAKVDMTFEEEEQLLQL----------KVKCLNNLAASQLKLDHYRA 292
Cdd:TIGR02917 132 GLAYLGLGQLELAQKSYEQALAidprslyAKLGLAQLALAENRFDEARALidevltadpgNVDALLLKGDLLLSLGNIEL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 293 ALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKL---EPSNKTIHAELSKLVKKHAAQRSTETALYRKm 369
Cdd:TIGR02917 212 ALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKapnSPLAHYLKALVDFQKKNYEDARETLQDALKS- 290

                         170
                  ....*....|
gi 1191857485 370 lgNPSRLPAK 379
Cdd:TIGR02917 291 --APEYLPAL 298
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 292-348 4.02e-05

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 43.07  E-value: 4.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1191857485 292 AALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL 57
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 237-354 4.04e-05

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: 45.84  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 237 ADFVLAANSYDLAIKAitssakvdmtFEEEEQLLQLKVKCLNNLAASQLKLDHYRA---ALRScslvLEHQPDNIKALFR 313
Cdd:TIGR02917 777 AELYLAQKDYDKAIKH----------YQTVVKKAPDNAVVLNNLAWLYLELKDPRAleyAERA----LKLAPNIPAILDT 842

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1191857485 314 KGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKK 354
Cdd:TIGR02917 843 LGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHLALALLA 883
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 279-341 6.84e-05

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: 44.54  E-value: 6.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191857485 279 NLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:cd24142     5 EKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDG 67
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 214-378 9.63e-05

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: 44.59  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 214 LTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAitssaKVDMTFeeeeqllqlkvkcLNNLAASQLKLDHYRAA 293
Cdd:TIGR00990 118 LSEEERKKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIEC-----KPDPVY-------------YSNRAACHNALGDWEKV 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 294 LRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRA-ALKLEPSNKTIHAELSKLVKKHAaqrstETALYRKMLGN 372
Cdd:TIGR00990 180 VEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTAsCIIDGFRNEQSAQAVERLLKKFA-----ESKAKEILETK 254


                  ....*.
gi 1191857485 373 PSRLPA 378
Cdd:TIGR00990 255 PENLPS 260
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 308-341 9.73e-05

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: 39.35  E-value: 9.73e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1191857485  308 IKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
308-341 1.07e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 38.94  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1191857485 308 IKALFRKGKVLAQQGEYSEAIPILRAALKLEPSN 341
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
301-348 2.25e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.69  E-value: 2.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1191857485 301 LEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAEL 348
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNL 48
TPR_11 pfam13414
TPR repeat;
315-354 2.98e-04

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 38.22  E-value: 2.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1191857485 315 GKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKK 354
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
TPR_19 pfam14559
Tetratricopeptide repeat;
290-351 4.31e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 38.33  E-value: 4.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191857485 290 YRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKL 351
Cdd:pfam14559   4 YAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAKL 65
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 309-339 6.72e-04

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: 36.73  E-value: 6.72e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1191857485 309 KALFRKGKVLAQQGEYSEAIPILRAALKLEP 339
Cdd:pfam07719   2 EALYNLGLAYYKLGDYEEALEAYEKALELDP 32
TPR_8 pfam13181
Tetratricopeptide repeat;
308-340 3.47e-03

Tetratricopeptide repeat;


Pssm-ID: 404131 [Multi-domain]  Cd Length: 33  Bit Score: 34.68  E-value: 3.47e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1191857485 308 IKALFRKGKVLAQQGEYSEAIPILRAALKLEPS 340
Cdd:pfam13181   1 AEAYYNLGLIYLKLGDYEEAKEYYEKALELDPD 33
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 283-365 4.20e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.89  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 283 SQLKLDHYRAALRSCSLVLEHQPDNI---KALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQR 359
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPlapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELG 81


                  ....*.
gi 1191857485 360 STETAL 365
Cdd:COG1729    82 DYDKAR 87
SirB1 COG2912
Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal ...
 277-358 6.28e-03

Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal transduction mechanisms];


Pssm-ID: 442156 [Multi-domain]  Cd Length: 264  Bit Score: 38.27  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191857485 277 LNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSnktihAELSKLVKKHA 356
Cdd:COG2912   182 LRNLKAAYLREKDWERALRVVERLLLLDPDDPYEIRDRGLLYAQLGCYQAALEDLEYFLEQCPE-----DPDAELIKEQL 256


                  ..
gi 1191857485 357 AQ 358
Cdd:COG2912   257 EE 258
 
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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