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Conserved domains on  [gi|2157295121|ref|WP_230467707|]
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tetratricopeptide repeat protein [Lujinxingia vulgaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 63-337 1.01e-12

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: 68.99  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  63 VAYLL-GDFPRASVLFVAVVDNKQvrqfdSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFYqpAIVRLLEIAGE 141
Cdd:COG2956    16 LNYLLnGQPDKAIDLLEEALELDP-----ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAE--ALLELAQDYLK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 142 IGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFT 221
Cdd:COG2956    89 AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 222 GLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLIS 301
Cdd:COG2956   169 KALKLDPDCAR-------ALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALEL 241

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2157295121 302 DPDprfvPEAKLLMADLSMRLRQYDQARLWFNDIIA 337
Cdd:COG2956   242 DPS----DDLLLALADLLERKEGLEAALALLERQLR 273
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 390-683 2.11e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 2.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  390 MADARQLVADgslTQADIDEAQKALAEVEQMLSYGSN---------IEAFPVLSEGWKRGIALEAELISLEERL------ 454
Cdd:TIGR02168  679 IEELEEKIEE---LEEKIAELEKALAELRKELEELEEeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIaqlske 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  455 ----------VGAELEGAREVLGPSERQRlATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELERVAFDIE 524
Cdd:TIGR02168  756 lteleaeieeLEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  525 SLQVNLDGIDTYLRQNpvesfsAEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQFGARDATLVQQREAREVYHR 604
Cdd:TIGR02168  835 ATERRLEDLEEQIEEL------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2157295121  605 RLMELGELIDEQRARLASSSRgdALAIAEQRRRlpELKARLNTYFQGIDQVIEERVVDIRATVEVERQELATYQRELDA 683
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLEL--RLEGLEVRID--NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 63-337 1.01e-12

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: 68.99  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  63 VAYLL-GDFPRASVLFVAVVDNKQvrqfdSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFYqpAIVRLLEIAGE 141
Cdd:COG2956    16 LNYLLnGQPDKAIDLLEEALELDP-----ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAE--ALLELAQDYLK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 142 IGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFT 221
Cdd:COG2956    89 AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 222 GLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLIS 301
Cdd:COG2956   169 KALKLDPDCAR-------ALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALEL 241

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2157295121 302 DPDprfvPEAKLLMADLSMRLRQYDQARLWFNDIIA 337
Cdd:COG2956   242 DPS----DDLLLALADLLERKEGLEAALALLERQLR 273
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 390-683 2.11e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 2.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  390 MADARQLVADgslTQADIDEAQKALAEVEQMLSYGSN---------IEAFPVLSEGWKRGIALEAELISLEERL------ 454
Cdd:TIGR02168  679 IEELEEKIEE---LEEKIAELEKALAELRKELEELEEeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIaqlske 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  455 ----------VGAELEGAREVLGPSERQRlATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELERVAFDIE 524
Cdd:TIGR02168  756 lteleaeieeLEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  525 SLQVNLDGIDTYLRQNpvesfsAEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQFGARDATLVQQREAREVYHR 604
Cdd:TIGR02168  835 ATERRLEDLEEQIEEL------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2157295121  605 RLMELGELIDEQRARLASSSRgdALAIAEQRRRlpELKARLNTYFQGIDQVIEERVVDIRATVEVERQELATYQRELDA 683
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLEL--RLEGLEVRID--NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 31-338 1.47e-06

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 52.01  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  31 LDAQIDELEERYLVPAVLESRFRLETRFNDAKVAYLLGDFPRASVLFVAVVdnkqvRQFDSYGEALYLLGDSLYQMRSFR 110
Cdd:TIGR02917 238 IEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDAL-----KSAPEYLPALLLAGASEYQLGNLE 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 111 AARTFFRRVVELGPggfYQPAIVRLLE-IAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRA 189
Cdd:TIGR02917 313 QAYQYLNQILKYAP---NSHQARRLLAsIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 190 A-RDSEYAlIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEDSRVVDLGHLALGRL--------AYEEQQFDLAIDH 260
Cdd:TIGR02917 390 TeLDPENA-AARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFdkalaaakKLEKKQPDNASLH 468

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2157295121 261 YLqlpRTSPYFERSLYEltwslVSKESYQAAlrnldilLISDPDprFVPEAKLLmADLSMRLRQYDQARLWFNDIIAT 338
Cdd:TIGR02917 469 NL---LGAIYLGKGDLA-----KAREAFEKA-------LSIEPD--FFPAAANL-ARIDIQEGNPDDAIQRFEKVLTI 528
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 441-697 4.68e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 441 IALEAELISLEERLVGAELEGAREVLGpSERQRLATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELERVA 520
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 521 FDIESLQVNLDGIDT-YLRQNPVESFSAEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQfgaRDATLVQQREAR 599
Cdd:COG1196   330 EELEELEEELEELEEeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA---AAELAAQLEELE 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 600 EVYHRRLMELGELIDEQRARLASSSRGDALAIAEQRRRLPELKARLNtyfqgidqvIEERVVDIRATVEVERQELATYQR 679
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---------LEEEEEALLELLAELLEEAALLEA 477

                         250
                  ....*....|....*...
gi 2157295121 680 ELDAWRSETERAVSSIAL 697
Cdd:COG1196   478 ALAELLEELAEAAARLLL 495
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 442-691 2.08e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  442 ALEAELISLEERLVGAELEGAREVlgpSERQ-RLATLEAEVETLRVQHQsgpQTLDELQSRNSAIREDFGRLNSELERVa 520
Cdd:pfam12128  255 SAELRLSHLHFGYKSDETLIASRQ---EERQeTSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDRSELEAL- 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  521 fDIESLQVNLDGIDTYlrqnpvesfsAEDRQKVRQIRQDLREEVRRleeeHAGLSQEIVAVQRQFGARDAtLVQQREARE 600
Cdd:pfam12128  328 -EDQHGAFLDADIETA----------AADQEQLPSWQSELENLEER----LKALTGKHQDVTAKYNRRRS-KIKEQNNRD 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  601 VyhRRLMELGELIDEQRARLASSSRGDALAI-AEQRRRLPELKARLNTYFQGIDQVIEE---RVVDIRATVEvERQELAT 676
Cdd:pfam12128  392 I--AGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGElklRLNQATATPE-LLLQLEN 468

                          250
                   ....*....|....*
gi 2157295121  677 YQRELDAWRSETERA 691
Cdd:pfam12128  469 FDERIERAREEQEAA 483
 
Name Accession Description Interval E-value
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 63-337 1.01e-12

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: 68.99  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  63 VAYLL-GDFPRASVLFVAVVDNKQvrqfdSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFYqpAIVRLLEIAGE 141
Cdd:COG2956    16 LNYLLnGQPDKAIDLLEEALELDP-----ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAE--ALLELAQDYLK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 142 IGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFT 221
Cdd:COG2956    89 AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 222 GLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLIS 301
Cdd:COG2956   169 KALKLDPDCAR-------ALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALEL 241

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2157295121 302 DPDprfvPEAKLLMADLSMRLRQYDQARLWFNDIIA 337
Cdd:COG2956   242 DPS----DDLLLALADLLERKEGLEAALALLERQLR 273
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 29-293 8.60e-11

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 63.21  E-value: 8.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  29 EQLDAQIDELEErylvpAVLESRFRLETRFNDAKVAYLLGDFPRASVLFVAVVDNKQVRQfdsygEALYLLGDSLYQMRS 108
Cdd:COG2956    22 GQPDKAIDLLEE-----ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRA-----EALLELAQDYLKAGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 109 FRAARTFFRRVVELGPggFYQPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQR 188
Cdd:COG2956    92 LDRAEELLEKLLELDP--DDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 189 AARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTS 268
Cdd:COG2956   170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP-------ALPRLAELYEKLGDPEEALELLRKALELD 242

                         250       260
                  ....*....|....*....|....*
gi 2157295121 269 PYfERSLYELTWSLVSKESYQAALR 293
Cdd:COG2956   243 PS-DDLLLALADLLERKEGLEAALA 266
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
55-266 1.02e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.64  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  55 ETRFNDAKVAYLLGDFPRASVLFvavvdNKQVRQFDSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGgfYQPAIVR 134
Cdd:COG0457     9 EAYNNLGLAYRRLGRYEEAIEDY-----EKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD--DAEALNN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 135 LLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIA 214
Cdd:COG0457    82 LGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2157295121 215 EAREVFTGLVAQNPTTPEDSRVVDLGHLALGRLAYEEQQFDLAIDHYLQLPR 266
Cdd:COG0457   162 EALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAI 213
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
163-337 2.70e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 163 PALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHL 242
Cdd:COG0457     8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAE-------ALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 243 ALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLISDPDprfVPEAKLLMADLSMRL 322
Cdd:COG0457    81 NLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPD---DADALYNLGIALEKL 157

                         170
                  ....*....|....*
gi 2157295121 323 RQYDQARLWFNDIIA 337
Cdd:COG0457   158 GRYEEALELLEKLEA 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 390-683 2.11e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 2.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  390 MADARQLVADgslTQADIDEAQKALAEVEQMLSYGSN---------IEAFPVLSEGWKRGIALEAELISLEERL------ 454
Cdd:TIGR02168  679 IEELEEKIEE---LEEKIAELEKALAELRKELEELEEeleqlrkelEELSRQISALRKDLARLEAEVEQLEERIaqlske 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  455 ----------VGAELEGAREVLGPSERQRlATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELERVAFDIE 524
Cdd:TIGR02168  756 lteleaeieeLEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  525 SLQVNLDGIDTYLRQNpvesfsAEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQFGARDATLVQQREAREVYHR 604
Cdd:TIGR02168  835 ATERRLEDLEEQIEEL------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2157295121  605 RLMELGELIDEQRARLASSSRgdALAIAEQRRRlpELKARLNTYFQGIDQVIEERVVDIRATVEVERQELATYQRELDA 683
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLEL--RLEGLEVRID--NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 438-710 3.52e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  438 KRGIALEAELISLEERLVGAELEGAREVLGPSERQ-------------RLATLEAEVETLRVQHQSGPQTLDELQSRNSA 504
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLRLEELREELEELQEElkeaeeeleeltaELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  505 IREDFGRLNSELERVAFDIESLQVNLDGIDTYLRQNPvesfsaEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQ 584
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELE------SKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  585 FGARDATLVQQREAREVYHRRLMELGELIDEQRARLAS---------------SSRGDALAIAEQRRRLPELKARLNTYF 649
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERlearlerledrrerlQQEIEELLKKLEEAELKELQAELEELE 446

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2157295121  650 QGIDQViEERVVDIRATVEVERQELATYQRELDAWRSETERAVSSIALWN--FTRVDGEFDAL 710
Cdd:TIGR02168  447 EELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlQENLEGFSEGV 508
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 129-269 4.16e-08

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.89  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 129 QPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLA 208
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2157295121 209 ADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSP 269
Cdd:COG4783    84 KAGDYDEALALLEKALKLDPEHPE-------AYLRLARAYRALGRPDEAIAALEKALELDP 137
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
92-299 4.60e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.63  E-value: 4.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  92 YGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGgfYQPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGK 171
Cdd:COG0457     7 DAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPD--DAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 172 TLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYEE 251
Cdd:COG0457    85 ALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDAD-------ALYNLGIALEKL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2157295121 252 QQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILL 299
Cdd:COG0457   158 GRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQ 205
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 2-189 6.69e-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: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121   2 LLGALWLSAPQAHAQEAIAASTARERVEQLDAQIDELEERYLVPAVLESRFRLETRFNDAKVAYLLGDFPRASVLFvavv 81
Cdd:COG3914    26 LALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALY---- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  82 dNKQVRQFDSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGgfYQPAIVRLLEIAGEIGDYSGVDALYARLDNLEEV 161
Cdd:COG3914   102 -RRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPD--FAEAYLNLGEALRRLGRLEEAIAALRRALELDPD 178

                         170       180
                  ....*....|....*....|....*...
gi 2157295121 162 TPALHYTRGKTLYQEGRYRAARPWFQRA 189
Cdd:COG3914   179 NAEALNNLGNALQDLGRLEEAIAAYRRA 206
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 246-339 6.91e-08

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: 51.15  E-value: 6.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 246 RLAYEEQQFDLAIDHYLQLPRT---SPYFERSLYELTWSLVSKESYQAALRNLDILLISDPDPRFVPEAKLLMADLSMRL 322
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKRypnSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLEL 80

                          90
                  ....*....|....*..
gi 2157295121 323 RQYDQARLWFNDIIATF 339
Cdd:COG1729    81 GDYDKARATLEELIKKY 97
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 171-269 1.45e-07

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: 50.38  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 171 KTLYQEGRYRAARPWFQRAAR---DSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPttpeDSRVVDLGHLALGRL 247
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKrypNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYP----DSPKAPDALLKLGLS 76

                          90       100
                  ....*....|....*....|..
gi 2157295121 248 AYEEQQFDLAIDHYLQLPRTSP 269
Cdd:COG1729    77 YLELGDYDKARATLEELIKKYP 98
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 207-318 1.62e-07

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: 50.38  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 207 LAADGDIAEAREVFTGLVAQNPttpeDSRVVDLGHLALGRLAYEEQQFDLAIDHYLQLPRT---SPYFERSLYELTWSLV 283
Cdd:COG1729     3 LLKAGDYDEAIAAFKAFLKRYP----NSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRypdSPKAPDALLKLGLSYL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2157295121 284 SKESYQAALRNLDILLISDPDPRFVPEAKLLMADL 318
Cdd:COG1729    79 ELGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 167-337 1.65e-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: 53.58  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 167 YTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGR 246
Cdd:COG2956    12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAE-------ALLELAQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 247 LAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLISDPDPrfvPEAKLLMADLSMRLRQYD 326
Cdd:COG2956    85 DYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPEN---AHAYCELAELYLEQGDYD 161

                         170
                  ....*....|.
gi 2157295121 327 QARLWFNDIIA 337
Cdd:COG2956   162 EAIEALEKALK 172
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 195-419 1.94e-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: 53.19  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 195 YALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERS 274
Cdd:COG2956     6 AAALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVE-------AHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 275 LYELTWSLVSKESYQAALRNLDILLISDPDprfVPEAKLLMADLSMRLRQYDQARLWFNDIiatftpvrtelvsfIESQP 354
Cdd:COG2956    79 LLELAQDYLKAGLLDRAEELLEKLLELDPD---DAEALRLLAEIYEQEGDWEKAIEVLERL--------------LKLGP 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2157295121 355 DLQSFFVELVRQDLEGLRPDYMPEMVSEWVEGEPLMADARQLVADGSLTQADIDEAQKALAEVEQ 419
Cdd:COG2956   142 ENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALE 206
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 164-304 6.18e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 53.07  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 164 ALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLA 243
Cdd:COG3914    79 ALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAE-------AYLN 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2157295121 244 LGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLISDPD 304
Cdd:COG3914   152 LGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPD 212
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 101-232 1.26e-06

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 47.68  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 101 DSLYQMRSFRAARTFFRRVVELGPGGFYQPaivrlleiageigdysgvDALYArldnleevtpalhytRGKTLYQEGRYR 180
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKRYPNSPLAP------------------DALYW---------------LGEAYYALGDYD 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2157295121 181 AARPWFQRAAR---DSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPE 232
Cdd:COG1729    48 EAAEAFEKLLKrypDSPKAPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEA 102
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 31-338 1.47e-06

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 52.01  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  31 LDAQIDELEERYLVPAVLESRFRLETRFNDAKVAYLLGDFPRASVLFVAVVdnkqvRQFDSYGEALYLLGDSLYQMRSFR 110
Cdd:TIGR02917 238 IEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDAL-----KSAPEYLPALLLAGASEYQLGNLE 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 111 AARTFFRRVVELGPggfYQPAIVRLLE-IAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRA 189
Cdd:TIGR02917 313 QAYQYLNQILKYAP---NSHQARRLLAsIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 190 A-RDSEYAlIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEDSRVVDLGHLALGRL--------AYEEQQFDLAIDH 260
Cdd:TIGR02917 390 TeLDPENA-AARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFdkalaaakKLEKKQPDNASLH 468

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2157295121 261 YLqlpRTSPYFERSLYEltwslVSKESYQAAlrnldilLISDPDprFVPEAKLLmADLSMRLRQYDQARLWFNDIIAT 338
Cdd:TIGR02917 469 NL---LGAIYLGKGDLA-----KAREAFEKA-------LSIEPD--FFPAAANL-ARIDIQEGNPDDAIQRFEKVLTI 528
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 164-304 1.49e-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: 48.26  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 164 ALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLA 243
Cdd:COG4783     5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE-------ARLN 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2157295121 244 LGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLISDPD 304
Cdd:COG4783    78 LGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 163-269 1.37e-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: 45.38  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 163 PALHYTRGKTLYQEGRYRAARPWFQRAAR---DSEYALIARyfeGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdl 239
Cdd:COG4235    17 AEGWLLLGRAYLRLGRYDEALAAYEKALRldpDNADALLDL---AEALLAAGDTEEAEELLERALALDPDNPE------- 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 2157295121 240 GHLALGRLAYEEQQFDLAIDHYLQLPRTSP 269
Cdd:COG4235    87 ALYLLGLAAFQQGDYAEAIAAWQKLLALLP 116
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 92-331 1.39e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.45  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  92 YGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFYQPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGK 171
Cdd:COG3914    41 LGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 172 TLYQEGRYRAARPWFQRA-ARDSEYALiARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYE 250
Cdd:COG3914   121 LLLALGRLEEALAALRRAlALNPDFAE-AYLNLGEALRRLGRLEEAIAALRRALELDPDNAE-------ALNNLGNALQD 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 251 EQQFDLAIDHY---LQLPRTSPYFeRSLYeLTWSLVSKESYQAALRNLDILLISDPDPRFVPEAKLLMADLSmRLRQYDQ 327
Cdd:COG3914   193 LGRLEEAIAAYrraLELDPDNADA-HSNL-LFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDDD-PAELLAL 269


                  ....
gi 2157295121 328 ARLW 331
Cdd:COG3914   270 ARAW 273
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 86-329 2.83e-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: 47.77  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  86 VRQFDSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGpggfYQPAIVRLL--EIAGEIGDYSGVDALYARLDNL-EEVT 162
Cdd:TIGR02917  49 LQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLG----YPKNQVLPLlaRAYLLQGKFQQVLDELPGKTLLdDEGA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 163 PALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPtTPEDSrvvdlgHL 242
Cdd:TIGR02917 125 AELLALRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADP-GNVDA------LL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 243 ALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLISDPDPrfvPEAKLLMADLSMRL 322
Cdd:TIGR02917 198 LKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNS---PLAHYLKALVDFQK 274


                  ....*..
gi 2157295121 323 RQYDQAR 329
Cdd:TIGR02917 275 KNYEDAR 281
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 64-155 5.38e-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: 43.06  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  64 AYLLGDFPRASVLFVAVVDNKQvrQFDSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFYQP-AIVRLLEIAGEI 142
Cdd:COG1729     3 LLKAGDYDEAIAAFKAFLKRYP--NSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPdALLKLGLSYLEL 80

                          90
                  ....*....|...
gi 2157295121 143 GDYSGVDALYARL 155
Cdd:COG1729    81 GDYDKARATLEEL 93
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 84-200 5.44e-05

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 43.46  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  84 KQVRQFDSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGgfYQPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTP 163
Cdd:COG4235     8 QALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPD--NADALLDLAEALLAAGDTEEAEELLERALALDPDNP 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2157295121 164 ALHYTRGKTLYQEGRYRAARPWFQRAAR----DSEYALIAR 200
Cdd:COG4235    86 EALYLLGLAAFQQGDYAEAIAAWQKLLAllpaDAPARLLEA 126
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 93-280 2.19e-04

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: 44.69  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  93 GEALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFyqPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKT 172
Cdd:TIGR02917 635 ALALLLLADAYAVMKNYAKAITSLKRALELKPDNT--EAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDL 712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 173 LYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAAdGDIAEAREVFTGLVAQNPttpEDSRVvdlgHLALGRLAYEEQ 252
Cdd:TIGR02917 713 YLRQKDYPAAIQAYRKALKRAPSSQNAIKLHRALLAS-GNTAEAVKTLEAWLKTHP---NDAVL----RTALAELYLAQK 784

                         170       180
                  ....*....|....*....|....*...
gi 2157295121 253 QFDLAIDHYLQLPRTSPYFERSLYELTW 280
Cdd:TIGR02917 785 DYDKAIKHYQTVVKKAPDNAVVLNNLAW 812
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 199-337 2.27e-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: 42.10  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 199 ARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYEL 278
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPE-------AFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2157295121 279 TWSLVSKESYQAALRNLDILLISDPDPrfvPEAKLLMADLSMRLRQYDQARLWFNDIIA 337
Cdd:COG4783    79 GLALLKAGDYDEALALLEKALKLDPEH---PEAYLRLARAYRALGRPDEAIAALEKALE 134
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 156-329 3.06e-04

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 43.33  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 156 DNLEEVTPALHYTRGKTLYQEGRYRAARPWFQ---RAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTP- 231
Cdd:COG4105    25 KALKSWDAEELYEEAKEALEKGDYEKAIKLFEelePRYPGSPYAEQAQLMLAYAYYKQGDYEEAIAAADRFIKLYPNSPn 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 232 -------------EDSRVVDLGHlALGRLAYEE-QQFdlaIDHYlqlPrTSPYFERS---LYELTWSLVSKE-------- 286
Cdd:COG4105   105 adyayylrglsyyEQSPDSDRDQ-TSTRKAIEAfQEL---INRY---P-DSEYAEDAkkrIDELRDKLARKElevaryyl 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2157295121 287 ---SYQAALRNLDILLISDPDPRFVPEAKLLMADLSMRLRQYDQAR 329
Cdd:COG4105   177 krgAYVAAINRFQNVLEDYPDTPAVEEALYLLVEAYYALGRYDEAQ 222
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 441-697 4.68e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 441 IALEAELISLEERLVGAELEGAREVLGpSERQRLATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELERVA 520
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 521 FDIESLQVNLDGIDT-YLRQNPVESFSAEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQfgaRDATLVQQREAR 599
Cdd:COG1196   330 EELEELEEELEELEEeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA---AAELAAQLEELE 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 600 EVYHRRLMELGELIDEQRARLASSSRGDALAIAEQRRRLPELKARLNtyfqgidqvIEERVVDIRATVEVERQELATYQR 679
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---------LEEEEEALLELLAELLEEAALLEA 477

                         250
                  ....*....|....*...
gi 2157295121 680 ELDAWRSETERAVSSIAL 697
Cdd:COG1196   478 ALAELLEELAEAAARLLL 495
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 224-338 1.00e-03

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: 39.99  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 224 VAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLDILLISDP 303
Cdd:COG4235    10 LAANPNDAE-------GWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDP 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2157295121 304 DPrfvPEAKLLMADLSMRLRQYDQARLWFNDIIAT 338
Cdd:COG4235    83 DN---PEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
137-338 1.00e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 41.44  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 137 EIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIArYFEGVTLAADGDIAEA 216
Cdd:COG4785    14 LAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLY-YERGVAYDSLGDYDLA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 217 REVFTGLVAQNPTTPEdsrvvdlGHLALGRLAYEEQQFDLAIDHYLQLPRTSPYFERSLYELTWSLVSKESYQAALRNLD 296
Cdd:COG4785    93 IADFDQALELDPDLAE-------AYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLE 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2157295121 297 ILLISDPDPRFVpeakLLMADLSMRLRQYDQARLWFNDIIAT 338
Cdd:COG4785   166 KALELDPNDPER----ALWLYLAERKLDPEKALALLLEDWAT 203
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 160-337 1.07e-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: 42.38  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 160 EVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNP----TTP---- 231
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGYpknqVLPllar 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 232 ------EDSRVVD---------------------LGHLALGrlayeeqQFDLAIDHYLQLPRTSPYFERSLYELTWSLVS 284
Cdd:TIGR02917  99 ayllqgKFQQVLDelpgktllddegaaellalrgLAYLGLG-------QLELAQKSYEQALAIDPRSLYAKLGLAQLALA 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2157295121 285 KESYQAALRNLDILLISDPDPRfvpEAKLLMADLSMRLRQYDQARLWFNDIIA 337
Cdd:TIGR02917 172 ENRFDEARALIDEVLTADPGNV---DALLLKGDLLLSLGNIELALAAYRKAIA 221
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 94-246 1.46e-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: 41.99  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  94 EALYLLGDSLYQMRSFRAARTFFRRVVELGPggFYQPAIVRLLEIAGEIGDYSG----VDALYARLDNleevTPALHYTR 169
Cdd:TIGR02917 194 DALLLKGDLLLSLGNIELALAAYRKAIALRP--NNIAVLLALATILIEAGEFEEaekhADALLKKAPN----SPLAHYLK 267

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2157295121 170 GKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNPTTPEDSRVVDLGHLALGR 246
Cdd:TIGR02917 268 ALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGR 344
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
55-264 1.81e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.76  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  55 ETRFNDAKVAYLLGDFPRASVLFvavvdNKQVRQFDSYGEALYLLGDSLYQMRSFRAARTFFRRVVELGPGgfYQPAIVR 134
Cdd:COG0457    43 EALYNLGLAYLRLGRYEEALADY-----EQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPD--DAEALYN 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 135 LLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTLYQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIA 214
Cdd:COG0457   116 LGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEV 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2157295121 215 EAREVFTGLVAQNPTTPEDSRVVDLGHLALGRLAYEEQQFDLAIDHYLQL 264
Cdd:COG0457   196 LLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYRA 245
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 94-228 2.00e-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: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  94 EALYLLGDSLYQMRSFRAARTFFRRVVELGPGGFYQPAIVRLLEIAGEIGDYSGVDALYARLDNLEEVTPALHYTRGKTL 173
Cdd:COG5010    19 KLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLY 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2157295121 174 YQEGRYRAARPWFQRAARDSEYALIARYFEGVTLAADGDIAEAREVFTGLVAQNP 228
Cdd:COG5010    99 SRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 442-691 2.08e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  442 ALEAELISLEERLVGAELEGAREVlgpSERQ-RLATLEAEVETLRVQHQsgpQTLDELQSRNSAIREDFGRLNSELERVa 520
Cdd:pfam12128  255 SAELRLSHLHFGYKSDETLIASRQ---EERQeTSAELNQLLRTLDDQWK---EKRDELNGELSAADAAVAKDRSELEAL- 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  521 fDIESLQVNLDGIDTYlrqnpvesfsAEDRQKVRQIRQDLREEVRRleeeHAGLSQEIVAVQRQFGARDAtLVQQREARE 600
Cdd:pfam12128  328 -EDQHGAFLDADIETA----------AADQEQLPSWQSELENLEER----LKALTGKHQDVTAKYNRRRS-KIKEQNNRD 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  601 VyhRRLMELGELIDEQRARLASSSRGDALAI-AEQRRRLPELKARLNTYFQGIDQVIEE---RVVDIRATVEvERQELAT 676
Cdd:pfam12128  392 I--AGIKDKLAKIREARDRQLAVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSRLGElklRLNQATATPE-LLLQLEN 468

                          250
                   ....*....|....*
gi 2157295121  677 YQRELDAWRSETERA 691
Cdd:pfam12128  469 FDERIERAREEQEAA 483
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
394-755 2.15e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 394 RQLVADGSLTQADIDEAQKALAEVEQMLsygSNIEAFPVLSEGWKRGIALEAELISLEERL------------------- 454
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREEL---EKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreleeelee 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 455 -------VGAELEGAREVLGPSERQRLATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELE---------- 517
Cdd:COG4717   168 leaelaeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaaaleerlke 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 518 -RVAFDIESLQVNLDGID-------------------------TYLRQNPVESFSAEDRQKVRQIRQDLREEVRRLEEEH 571
Cdd:COG4717   248 aRLLLLIAAALLALLGLGgsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAA 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 572 AGLSQEIVAVQRQFGARDATLVQQREAREVYHRRLMELGELIDEQRARLAS---SSRGDALAIAEQRRRLPELKARLNTY 648
Cdd:COG4717   328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEELEEL 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121 649 FQGIDQVIEERVVDIRATVEVE-RQELATYQRELDAWRSETERAVSSIAlwnftRVDGEFDALIRRGHVGLLDvgwQRKE 727
Cdd:COG4717   408 EEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELA-----ELEAELEQLEEDGELAELL---QELE 479

                         410       420
                  ....*....|....*....|....*...
gi 2157295121 728 DATRDINQLFEDRSTeINVLREAFREVR 755
Cdd:COG4717   480 ELKAELRELAEEWAA-LKLALELLEEAR 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
442-633 5.47e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  442 ALEAELISLEERLvgAELEGAREVLgpseRQRLATLEAEVETLRVQH-QSGPQTLDELQSRNSAIREDFGRLNSELERVA 520
Cdd:COG4913    292 LLEAELEELRAEL--ARLEAELERL----EARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  521 FDIESLQVNLDGIDtylrqnpvESFsAEDRQKVRQIRQDLREEVRRLEEEHAGLSQEIVAVQRQFGARDATLVQQREARE 600
Cdd:COG4913    366 ALLAALGLPLPASA--------EEF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2157295121  601 VYHRRLMELgelideqRARLAsssrgDALAIAE 633
Cdd:COG4913    437 NIPARLLAL-------RDALA-----EALGLDE 457
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 384-719 8.49e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 8.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  384 VEGEPLMADARQLVADGSLTQADIDEAQKALAEVEQMLSygsnieafpvlsEGWKRGIALEAELISLEERLVGAELEGAR 463
Cdd:TIGR02169  223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS------------ELEKRLEEIEQLLEELNKKIKDLGEEEQL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  464 EVlgpseRQRLATLEAEVETLRVQHQSGPQTLDELQSRNSAIREDFGRLNSELERVAFDIESLQVNLDGIDTYL------ 537
Cdd:TIGR02169  291 RV-----KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkee 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  538 ------RQNPVESFSAEDRQKVRQIRQdlreEVRRleeehagLSQEIVAVQRQFGARDATLVQQREAREVYHRRLmelgE 611
Cdd:TIGR02169  366 ledlraELEEVDKEFAETRDELKDYRE----KLEK-------LKREINELKRELDRLQEELQRLSEELADLNAAI----A 430

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157295121  612 LIDEQRARLASSSRGDALAIAEQRRRLPELKARLNTYfqgidqviEERVVDIRATVEVERQELATYQRELDawRSETERA 691
Cdd:TIGR02169  431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY--------EQELYDLKEEYDRVEKELSKLQRELA--EAEAQAR 500

                          330       340
                   ....*....|....*....|....*...
gi 2157295121  692 VSSIALWNFTRVDGEFDALIrRGHVGLL 719
Cdd:TIGR02169  501 ASEERVRGGRAVEEVLKASI-QGVHGTV 527
 
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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