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Conserved domains on  [gi|542176767|ref|XP_005468167|]
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aspartyl/asparaginyl beta-hydroxylase isoform X9 [Oreochromis niloticus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 586-740 4.58e-75

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


:

Pssm-ID: 461552  Cd Length: 157  Bit Score: 239.47  E-value: 4.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  586 ERNWKTIRDEALAVLDQNTGHFVPEEENLREKGD--WGQYTLWQQGRKVGNACQGVPKTCALLERFP-EATGCKRGQIKF 662
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542176767  663 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKrGCKIRCTNETREWEEGKVLIFDDSFEHEVWQEAESYRLIFIVDVWHP 740
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 86-156 4.61e-23

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


:

Pssm-ID: 428406  Cd Length: 66  Bit Score: 92.98  E-value: 4.61e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767   86 SVFTWFVVLGLLGVWSSVAVVYFNIVDYDTVIarakefrmnfsevlqGKLTAYDTDGDGDFDVEDAKVLLG 156
Cdd:pfam05279  11 SFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 334-543 1.37e-19

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: 89.40  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 334 KTIKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAELPDVTSDL 413
Cdd:COG2956   40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQD-------YLKAGLLDRAEELLEKLLELDPDDAEA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 414 LRatlkRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFIL 493
Cdd:COG2956  113 LR----LLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 542176767 494 KSENKIAESIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGDN-SAYDWYE 543
Cdd:COG2956  189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDPeEALELLR 236
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
182-314 5.93e-05

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14949:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 944  Bit Score: 46.64  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 182 KPAAE----TPNQQAAvpravepteAAPSVTPPRESESAAVPLPPPAEDFVPDDPQESISPYGDEANTIDTTGVLLAE-- 255
Cdd:PRK14949 638 KSSADrkpkTPPSRAP---------PASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPyd 708

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767 256 --PQTEESAGESAEYLTSSKLTQEAELVIEAEKQPEAADVDPQSETPKQTEAEGTSEKQAE 314
Cdd:PRK14949 709 rpPWEEAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTT 769
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 586-740 4.58e-75

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 239.47  E-value: 4.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  586 ERNWKTIRDEALAVLDQNTGHFVPEEENLREKGD--WGQYTLWQQGRKVGNACQGVPKTCALLERFP-EATGCKRGQIKF 662
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542176767  663 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKrGCKIRCTNETREWEEGKVLIFDDSFEHEVWQEAESYRLIFIVDVWHP 740
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 582-743 8.64e-57

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.17  E-value: 8.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 582 VKVLERNWKTIRDEALAVLDQNTG----H-FVPEEENLREKGDWGQYTLWQQGRKVGNACQGVPKTCALLERFPeatgck 656
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEAlppyHdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 657 rgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKR-GCKIRCTNETREWEEGKVLIFDDSFEHEVWQEAESYRLI 732
Cdd:COG3555   94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|.
gi 542176767 733 FIVDVWHPELT 743
Cdd:COG3555  172 LFCDVWRPMLS 182
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 86-156 4.61e-23

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 92.98  E-value: 4.61e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767   86 SVFTWFVVLGLLGVWSSVAVVYFNIVDYDTVIarakefrmnfsevlqGKLTAYDTDGDGDFDVEDAKVLLG 156
Cdd:pfam05279  11 SFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 334-543 1.37e-19

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: 89.40  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 334 KTIKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAELPDVTSDL 413
Cdd:COG2956   40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQD-------YLKAGLLDRAEELLEKLLELDPDDAEA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 414 LRatlkRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFIL 493
Cdd:COG2956  113 LR----LLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 542176767 494 KSENKIAESIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGDN-SAYDWYE 543
Cdd:COG2956  189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDPeEALELLR 236
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 333-516 2.52e-07

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: 54.32  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  333 DKTIKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaeKLRSNDMLQrAINTYREAAEL----PD 408
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKI------YLALGDYAA-AEKELRKALSLgypkNQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  409 VTSDLLRATLKRRaerqQFlgrmrgslatlERLVQLFPEDIGLKND--------LGVAHLLLGDNKGAKKIYEEVLGVAP 480
Cdd:TIGR02917  92 VLPLLARAYLLQG----KF-----------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDP 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 542176767  481 DNGFAKVHYGFILKSENKIAESIPYLKEGLeSGEPG 516
Cdd:TIGR02917 157 RSLYAKLGLAQLALAENRFDEARALIDEVL-TADPG 191
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 182-314 5.93e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 46.64  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 182 KPAAE----TPNQQAAvpravepteAAPSVTPPRESESAAVPLPPPAEDFVPDDPQESISPYGDEANTIDTTGVLLAE-- 255
Cdd:PRK14949 638 KSSADrkpkTPPSRAP---------PASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPyd 708

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767 256 --PQTEESAGESAEYLTSSKLTQEAELVIEAEKQPEAADVDPQSETPKQTEAEGTSEKQAE 314
Cdd:PRK14949 709 rpPWEEAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTT 769
TPR_9 pfam13371
Tetratricopeptide repeat;
418-481 8.54e-05

Tetratricopeptide repeat;


Pssm-ID: 463860 [Multi-domain]  Cd Length: 73  Bit Score: 41.44  E-value: 8.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542176767  418 LKRRAERQQFLGRMrgsLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPD 481
Cdd:pfam13371   1 LKAIYLREEDWERA---LAVVERLLLLAPDDPEERRDRGLLYAQLGCFQAALEDLEAYLELAPD 61
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
 343-486 9.10e-04

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 42.76  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  343 AEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRA---INTYREAAELPDVTSdllratLK 419
Cdd:PRK11447  502 AQDLRQAGQRSQADALMRRLAQQKPNDPEQVYAYGLY-------LSGSDRDRAAlahLNTLPRAQWNSNIQE------LA 568

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542176767  420 RRAERQQFL---GRMR--GSLATLERLVQLFPEDIglKNDLGVAH--LLLGDNKGAKKIYEEVLGVAPDNGFAK 486
Cdd:PRK11447  569 QRLQSDQVLetaNRLRdsGKEAEAEALLRQQPPST--RIDLTLADwaQQRGDYAAARAAYQRVLTREPGNADAR 640
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 586-740 4.58e-75

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 239.47  E-value: 4.58e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  586 ERNWKTIRDEALAVLDQNTGHFVPEEENLREKGD--WGQYTLWQQGRKVGNACQGVPKTCALLERFP-EATGCKRGQIKF 662
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542176767  663 SVMQPGTHVWPHTGPTNCRLRMHLGLVIPKrGCKIRCTNETREWEEGKVLIFDDSFEHEVWQEAESYRLIFIVDVWHP 740
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVPP-GCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 582-743 8.64e-57

Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442776  Cd Length: 220  Bit Score: 193.17  E-value: 8.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 582 VKVLERNWKTIRDEALAVLDQNTG----H-FVPEEENLREKGDWGQYTLWQQGRKVGNACQGVPKTCALLERFPeatgck 656
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEAlppyHdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 657 rgQIK---FSVMQPGTHVWPHTGPTNCRLRMHLGLVIPKR-GCKIRCTNETREWEEGKVLIFDDSFEHEVWQEAESYRLI 732
Cdd:COG3555   94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPNDdRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|.
gi 542176767 733 FIVDVWHPELT 743
Cdd:COG3555  172 LFCDVWRPMLS 182
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 86-156 4.61e-23

Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of the junctin, junctate and aspartyl beta-hydroxylase proteins. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin. Aspartyl beta-hydroxylase catalyzes the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins.


Pssm-ID: 428406  Cd Length: 66  Bit Score: 92.98  E-value: 4.61e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767   86 SVFTWFVVLGLLGVWSSVAVVYFNIVDYDTVIarakefrmnfsevlqGKLTAYDTDGDGDFDVEDAKVLLG 156
Cdd:pfam05279  11 SFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 334-543 1.37e-19

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: 89.40  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 334 KTIKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAELPDVTSDL 413
Cdd:COG2956   40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQD-------YLKAGLLDRAEELLEKLLELDPDDAEA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 414 LRatlkRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFIL 493
Cdd:COG2956  113 LR----LLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 542176767 494 KSENKIAESIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGDN-SAYDWYE 543
Cdd:COG2956  189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDPeEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
346-511 2.18e-16

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 79.28  E-value: 2.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 346 LRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAEL-PDVTsdllrATLKRRAER 424
Cdd:COG0457   18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA-------YLRLGRYEEALADYEQALELdPDDA-----EALNNLGLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 425 QQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIP 504
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                 ....*..
gi 542176767 505 YLKEGLE 511
Cdd:COG0457  166 LLEKLEA 172
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 336-525 8.93e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 71.56  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 336 IKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYgkaqaedDMAEKLRSNDMLQRAINTYREAAELPdvtSDLLR 415
Cdd:COG3914   78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALN---PDFAE 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 416 AtLKRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKS 495
Cdd:COG3914  148 A-YLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQ 226

                        170       180       190
                 ....*....|....*....|....*....|
gi 542176767 496 ENKIAESIPYLKEGLESGEPGTDDGRFYFH 525
Cdd:COG3914  227 ACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
363-598 2.69e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 67.34  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 363 VQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAEL-PDVTSdllraTLKRRAERQQFLGRMRGSLATLERL 441
Cdd:COG0457    1 LELDPDDAEAYNNLGLA-------YRRLGRYEEAIEDYEKALELdPDDAE-----ALYNLGLAYLRLGRYEEALADYEQA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 442 VQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLKEGLESgEPgtDDGR 521
Cdd:COG0457   69 LELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDAD 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 522 FYFHLGDALQRVGDN----SAYDWYELGHKRGHFASLWQRSLYNVNGLKAQPWWTAKETGYTDLVKVLERNWKTIRDEAL 597
Cdd:COG0457  146 ALYNLGIALEKLGRYeealELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLL 225


                 .
gi 542176767 598 A 598
Cdd:COG0457  226 A 226
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 342-535 3.17e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 70.02  E-value: 3.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 342 AAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAEDDMAEKLRSNDMLQRAINTYREAAELPDvtsdLLRATLKRR 421
Cdd:COG3914    9 LAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALL----LLAALLELA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 422 AERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAE 501
Cdd:COG3914   85 ALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEE 164

                        170       180       190
                 ....*....|....*....|....*....|....
gi 542176767 502 SIPYLKEGLESgEPgtDDGRFYFHLGDALQRVGD 535
Cdd:COG3914  165 AIAALRRALEL-DP--DNAEALNNLGNALQDLGR 195
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 338-482 3.74e-12

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: 64.44  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 338 AEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAELP--DVTSDLLR 415
Cdd:COG4783    6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI-------LLQLGDLDEAIVLLHEALELDpdEPEARLNL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542176767 416 ATLKRRAerqqflGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDN 482
Cdd:COG4783   79 GLALLKA------GDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 420-535 2.51e-11

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: 62.13  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 420 RRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKI 499
Cdd:COG4783    9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDY 88

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 542176767 500 AESIPYLKEGLESGEpgtDDGRFYFHLGDALQRVGD 535
Cdd:COG4783   89 DEALALLEKALKLDP---EHPEAYLRLARAYRALGR 121
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 362-512 1.02e-10

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: 60.74  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 362 LVQQYPQSPRARYGKAQAEDDMAEKLRSNDMLQRAINTYREAAELPDVTSDLLRATLKRRAERQQFLGRMRGSLATLERL 441
Cdd:COG5010    1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767 442 VQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLKEGLES 512
Cdd:COG5010   81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 354-543 1.90e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 61.16  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 354 EALKAFERLVQQYPQSPRARYGKAQAEDDMAEKLRSNDMLQRAINTYREAAEL-PDvtsdlLRATLKRRAERQQFLGRMR 432
Cdd:COG3914   55 AAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALnPD-----NAEALFNLGNLLLALGRLE 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 433 GSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLKEGLES 512
Cdd:COG3914  130 EALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209

                        170       180       190
                 ....*....|....*....|....*....|.
gi 542176767 513 gEPgtDDGRFYFHLGDALQRVGDNSAYDWYE 543
Cdd:COG3914  210 -DP--DNADAHSNLLFALRQACDWEVYDRFE 237
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 343-476 4.55e-09

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 58.20  E-value: 4.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 343 AEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAEL-PDVTSdllraTLKRR 421
Cdd:COG2956  151 AELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL-------YLEQGDYEEAIAALERALEQdPDYLP-----ALPRL 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 542176767 422 AERQQFLGRMRGSLATLERLVQLFPEDIgLKNDLGVAHLLLGDNKGAKKIYEEVL 476
Cdd:COG2956  219 AELYEKLGDPEEALELLRKALELDPSDD-LLLALADLLERKEGLEAALALLERQL 272
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 345-447 5.52e-09

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: 54.61  E-value: 5.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 345 KLRKKGKPDEALKAFERLVQQYPQS---PRARYGKAQAeddmaekLRSNDMLQRAINTYREAAEL-PDvtSDLLRATLKR 420
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEA-------YYALGDYDEAAEAFEKLLKRyPD--SPKAPDALLK 72

                         90       100
                 ....*....|....*....|....*..
gi 542176767 421 RAERQQFLGRMRGSLATLERLVQLFPE 447
Cdd:COG1729   73 LGLSYLELGDYDKARATLEELIKKYPD 99
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 428-518 6.57e-09

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 54.63  E-value: 6.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 428 LGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLK 507
Cdd:COG4235   30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                         90
                 ....*....|.
gi 542176767 508 EGLESGEPGTD 518
Cdd:COG4235  110 KLLALLPADAP 120
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 354-482 4.49e-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: 52.32  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 354 EALKAFERLVQQYPQSPRARYGKAQAEddmaekLRSNDmLQRAINTYREAAEL-PDVTSDLLRatlkrRAERQQFLGRMR 432
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAY------LRLGR-YDEALAAYEKALRLdPDNADALLD-----LAEALLAAGDTE 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 542176767 433 GSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDN 482
Cdd:COG4235   69 EAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 435-543 1.46e-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: 50.77  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 435 LATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLKEGLESgE 514
Cdd:COG4235    3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 542176767 515 PgtDDGRFYFHLGDALQRVGDNS-AYDWYE 543
Cdd:COG4235   82 P--DNPEALYLLGLAAFQQGDYAeAIAAWQ 109
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 333-516 2.52e-07

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: 54.32  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  333 DKTIKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaeKLRSNDMLQrAINTYREAAEL----PD 408
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKI------YLALGDYAA-AEKELRKALSLgypkNQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  409 VTSDLLRATLKRRaerqQFlgrmrgslatlERLVQLFPEDIGLKND--------LGVAHLLLGDNKGAKKIYEEVLGVAP 480
Cdd:TIGR02917  92 VLPLLARAYLLQG----KF-----------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAIDP 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 542176767  481 DNGFAKVHYGFILKSENKIAESIPYLKEGLeSGEPG 516
Cdd:TIGR02917 157 RSLYAKLGLAQLALAENRFDEARALIDEVL-TADPG 191
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
333-485 6.57e-07

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 51.07  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 333 DKTIKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAEDDMAEKLRsndmlqrAINTYREAAELPDVTSD 412
Cdd:COG4785    3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAAL-------AAERIDRALALPDLAQL 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542176767 413 LLRatlkrRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFA 485
Cdd:COG4785   76 YYE-----RGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
428-511 7.91e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.86  E-value: 7.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 428 LGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKiYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLK 507
Cdd:COG3063    5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                 ....
gi 542176767 508 EGLE 511
Cdd:COG3063   84 RALE 87
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 342-510 3.43e-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: 50.47  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  342 AAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaeKLRSNDMlQRAINTYREAAELpdvTSDLLRAtlkRR 421
Cdd:TIGR02917 369 LGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGIS------KLSQGDP-SEAIADLETAAQL---DPELGRA---DL 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  422 AERQQFL--GRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKI 499
Cdd:TIGR02917 436 LLILSYLrsGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQEGNP 515

                         170
                  ....*....|.
gi 542176767  500 AESIPYLKEGL 510
Cdd:TIGR02917 516 DDAIQRFEKVL 526
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 343-448 4.03e-06

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: 46.92  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 343 AEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAAELpdvTSDLLRAtLKRRA 422
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA-------LLAAGDTEEAEELLERALAL---DPDNPEA-LYLLG 92

                         90       100
                 ....*....|....*....|....*.
gi 542176767 423 ERQQFLGRMRGSLATLERLVQLFPED 448
Cdd:COG4235   93 LAAFQQGDYAEAIAAWQKLLALLPAD 118
SirB1 COG2912
Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal ...
 380-487 8.69e-06

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


Pssm-ID: 442156 [Multi-domain]  Cd Length: 264  Bit Score: 47.90  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 380 EDDMAEKLRSN-DMLQRAINTYREAAELPDVTSDLLRaTLKRRAERQQflgRMRGSLATLERLVQLFPEDIGLKNDLGVA 458
Cdd:COG2912  147 EEELEELLKGLlGPPAELEPEFLAPASNREILARMLR-NLKAAYLREK---DWERALRVVERLLLLDPDDPYEIRDRGLL 222

                         90       100
                 ....*....|....*....|....*....
gi 542176767 459 HLLLGDNKGAKKIYEEVLGVAPDNGFAKV 487
Cdd:COG2912  223 YAQLGCYQAALEDLEYFLEQCPEDPDAEL 251
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 347-511 1.18e-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: 48.93  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  347 RKKGKPDEALKAFERLVQQYPQSPRARYGKAqaedDMAEKLRSNDMlqrAINTYREAAELpDVTSDLLRATLKRRAERQq 426
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALA----GLYLRTGNEEE---AVAWLEKAAEL-NPQEIEPALALAQYYLGK- 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  427 flGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYL 506
Cdd:TIGR02917 581 --GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSL 658


                  ....*
gi 542176767  507 KEGLE 511
Cdd:TIGR02917 659 KRALE 663
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
458-543 1.45e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.01  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 458 AHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYlKEGLESgEPgtDDGRFYFHLGDALQRVGDNS 537
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDYD 76


                 ....*..
gi 542176767 538 -AYDWYE 543
Cdd:COG3063   77 eALAYLE 83
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 336-503 1.50e-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: 48.54  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  336 IKAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQ----------AEDDMAEKLRSND----------MLQR 395
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALvdfqkknyedARETLQDALKSAPeylpalllagASEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  396 AINTYREAAELPDVTsdLLRATLKRRAER-----QQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKK 470
Cdd:TIGR02917 307 QLGNLEQAYQYLNQI--LKYAPNSHQARRllasiQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAE 384

                         170       180       190
                  ....*....|....*....|....*....|...
gi 542176767  471 IYEEVLGVAPDNGFAKVHYGFILKSENKIAESI 503
Cdd:TIGR02917 385 YLAKATELDPENAAARTQLGISKLSQGDPSEAI 417
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 342-480 1.82e-05

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: 45.34  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 342 AAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAEDDMAEKLRSNDMLQR---AINTYREAAEL-PDVTsdllrAT 417
Cdd:COG5010   16 LLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDfeeSLALLEQALQLdPNNP-----EL 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542176767 418 LKRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAP 480
Cdd:COG5010   91 YYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 343-400 3.82e-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: 43.44  E-value: 3.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767 343 AEKLRKKGKPDEALKAFERLVQQYPQS---PRARYGKAQAEDDMAEKLRSNDMLQRAINTY 400
Cdd:COG1729   37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY 97
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 182-314 5.93e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 46.64  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 182 KPAAE----TPNQQAAvpravepteAAPSVTPPRESESAAVPLPPPAEDFVPDDPQESISPYGDEANTIDTTGVLLAE-- 255
Cdd:PRK14949 638 KSSADrkpkTPPSRAP---------PASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPyd 708

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767 256 --PQTEESAGESAEYLTSSKLTQEAELVIEAEKQPEAADVDPQSETPKQTEAEGTSEKQAE 314
Cdd:PRK14949 709 rpPWEEAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTT 769
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 337-447 7.25e-05

tol-pal system protein YbgF; Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction.


Pssm-ID: 188247 [Multi-domain]  Cd Length: 117  Bit Score: 42.65  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  337 KAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPR---ARY--GKAQ-AEDDMAEKLRSndmLQRAINTYREAAELPDvt 410
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAYyAQGDYADAAKA---FLAVVKKYPKSPKAPD-- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 542176767  411 sdllrATLKrRAERQQFLGRMRGSLATLERLVQLFPE 447
Cdd:TIGR02795  76 -----ALLK-LGMSLQELGDKEKAKATLQQVIKRYPG 106
TPR_9 pfam13371
Tetratricopeptide repeat;
418-481 8.54e-05

Tetratricopeptide repeat;


Pssm-ID: 463860 [Multi-domain]  Cd Length: 73  Bit Score: 41.44  E-value: 8.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542176767  418 LKRRAERQQFLGRMrgsLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPD 481
Cdd:pfam13371   1 LKAIYLREEDWERA---LAVVERLLLLAPDDPEERRDRGLLYAQLGCFQAALEDLEAYLELAPD 61
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
332-474 2.02e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.84  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 332 FDKTIKAEIDAAEKL-------RKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRAINTYREAA 404
Cdd:COG0457   65 YEQALELDPDDAEALnnlglalQALGRYEEALEDYDKALELDPDDAEALYNLGLA-------LLELGRYDEAIEAYERAL 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767 405 EL-PDVTsdllrATLKRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEE 474
Cdd:COG0457  138 ELdPDDA-----DALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLAL 203
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 340-420 3.28e-04

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.14  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 340 IDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAEddmaekLRSNDMlQRAINTYREAAEL--PDVTSDLLRAT 417
Cdd:COG4235   55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAA------FQQGDY-AEAIAAWQKLLALlpADAPARLLEAS 127


                 ...
gi 542176767 418 LKR 420
Cdd:COG4235  128 IAE 130
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 337-482 6.61e-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: 43.15  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  337 KAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPrarYGKAQaEDDMAekLRSNDmLQRAINTYREAAELPDvtsdlLRA 416
Cdd:TIGR02917 670 EAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAA---LGFEL-EGDLY--LRQKD-YPAAIQAYRKALKRAP-----SSQ 737

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542176767  417 TLKRRAERQQFLGRMRGSLATLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDN 482
Cdd:TIGR02917 738 NAIKLHRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPDN 803
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
 343-486 9.10e-04

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 42.76  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  343 AEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAeddmaekLRSNDMLQRA---INTYREAAELPDVTSdllratLK 419
Cdd:PRK11447  502 AQDLRQAGQRSQADALMRRLAQQKPNDPEQVYAYGLY-------LSGSDRDRAAlahLNTLPRAQWNSNIQE------LA 568

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542176767  420 RRAERQQFL---GRMR--GSLATLERLVQLFPEDIglKNDLGVAH--LLLGDNKGAKKIYEEVLGVAPDNGFAK 486
Cdd:PRK11447  569 QRLQSDQVLetaNRLRdsGKEAEAEALLRQQPPST--RIDLTLADwaQQRGDYAAARAAYQRVLTREPGNADAR 640
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
183-300 1.10e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 183 PAAETPNQQAAVPRAVEPTEAAPSVTPPRESESAA-------VPLPPPAEDFVPDD-------PQESISPYGDEANTIDT 248
Cdd:PRK07003 405 AAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGddaadgdAPVPAKANARASADsrcderdAQPPADSGSASAPASDA 484

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 542176767 249 TGVLLAEPQT------EESAGESAEYLTSSKLTQEAELVIEAEKQPEAADVDPQSETP 300
Cdd:PRK07003 485 PPDAAFEPAPraaapsAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAP 542
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 151-309 1.99e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 151 AKVLLG---LKEAKRLHVGDTPERQTVLKAEETikPAAETPNQQAAVPRAVEPTEAAPSVTPPRESESAAVPLPPPAEDF 227
Cdd:PRK07764 360 ARMLLPsasDDERGLLARLERLERRLGVAGGAG--APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAP 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 228 VPDDPQESISPYGDEANTIDTTGVLLAEPQTEESAGESAeyltsskltqeaelviEAEKQPEAADVDPQSETPKQTEAEG 307
Cdd:PRK07764 438 APAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP----------------TAAPAPAPPAAPAPAAAPAAPAAPA 501


                 ..
gi 542176767 308 TS 309
Cdd:PRK07764 502 AP 503
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
346-481 2.27e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.84  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 346 LRKKGKPDEALKAFERLVQQYPQSPRARYGKAqaeddmaeklrsndMLQRAINTYREAAElpdvtsdllratlkrraerq 425
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLG--------------LLLLEQGRYDEAIA-------------------- 47

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 542176767 426 qflgrmrgslatLERLVQLFPEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPD 481
Cdd:COG3063   48 ------------LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 337-402 2.38e-03

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 40.25  E-value: 2.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542176767 337 KAEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPR---ARYGKAQA---EDDMAEklRSNDMLQRAINTYRE 402
Cdd:COG4105   70 QAQLMLAYAYYKQGDYEEAIAAADRFIKLYPNSPNadyAYYLRGLSyyeQSPDSD--RDQTSTRKAIEAFQE 139
PTZ00121 PTZ00121
MAEBL; Provisional
 257-426 3.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  257 QTEESAGESAEYLTSSKLTQEAElviEAEKQPEAADVDPQsETPKQTEAEGTSEKQAEDKLKEKAKKKKPKLLNKFDKTI 336
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAE---EAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  337 KAEiDAAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAED--DMAEKLRSNDMLQRAINTYREAAELPDVTSDLL 414
Cdd:PTZ00121 1379 KAD-AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1457

                         170
                  ....*....|...
gi 542176767  415 RA-TLKRRAERQQ 426
Cdd:PTZ00121 1458 KAeEAKKKAEEAK 1470
TPR_14 pfam13428
Tetratricopeptide repeat;
346-379 3.36e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 35.86  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 542176767  346 LRKKGKPDEALKAFERLVQQYPQSPRARYGKAQA 379
Cdd:pfam13428  11 LLALGDPDEALALLERALALDPDDPEAWLALAQL 44
rne PRK10811
ribonuclease E; Reviewed
 167-314 4.13e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767  167 DTPERQTVLKAEETIKPAAETPnQQAAVPRAVEPTEA-APSVTPPRESESAAVPLPPPAEDFVPDDPQESISPYGDEANT 245
Cdd:PRK10811  852 DVQVEEQREAEEVQVQPVVAEV-PVAAAVEPVVSAPVvEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQV 930

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542176767  246 IDTTGVLLAEPQTEES--AGESAEYLTSSKLTQEAELVIEAEKQPEAADVDPQSETPKQTEAEGTSEKQAE 314
Cdd:PRK10811  931 ITESDVAVAQEVAEHAepVVEPQDETADIEEAAETAEVVVAEPEVVAQPAAPVVAEVAAEVETVTAVEPEV 1001
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 342-380 4.15e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 37.66  E-value: 4.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 542176767 342 AAEKLRKKGKPDEALKAFERLVQQYPQSPRARYGKAQAE 380
Cdd:COG1729   73 LGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLA 111
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
366-591 4.20e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 39.51  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 366 YPQSPRARYGKAQAEDDMAEKLRSNDMLQRAINTYREAAELPDvtsdLLRATLKRRAERQqflgrmrgslatleRLVQLF 445
Cdd:COG4785    8 LLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAA----AALAAAALAAERI--------------DRALAL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 446 PEDIGLKNDLGVAHLLLGDNKGAKKIYEEVLGVAPDNGFAKVHYGFILKSENKIAESIPYLKEGLESgEPgtDDGRFYFH 525
Cdd:COG4785   70 PDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAYLN 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542176767 526 LGDALQRVGD-NSAYDWYElghkrgHFASLWQRSLYNVNGLkaqpWWTAKETGYTDLVKVLERNWKT 591
Cdd:COG4785  147 RGIALYYLGRyELAIADLE------KALELDPNDPERALWL----YLAERKLDPEKALALLLEDWAT 203
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 338-483 5.31e-03

Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];


Pssm-ID: 442215 [Multi-domain]  Cd Length: 207  Bit Score: 39.07  E-value: 5.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 338 AEIDAAEKLRKKGKPDEALKAFERLVQQYPQSPrarYGkAQAEDDMAEKLRSNDMLQRAINTYREAAElpDVTSDLLRAT 417
Cdd:COG2976   55 ALYEQLLEALAAGDAAAAAAAAEKLIDDYGGTA---YA-ALAALLLAKAAVDAGDLDKAAAQLQWVLD--NAKDPALKAL 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542176767 418 LKRRAERQQF-LGRMRGSLATLErlvQLFPEDI-GLKNDL-GVAHLLLGDNKGAKKIYEEVLGVAPDNG 483
Cdd:COG2976  129 ARLRLARVLLaQKKYDEALATLD---AVKPEAFaALYAELrGDILLAQGDKAEARAAYQKALAALPEDA 194
TPR_6 pfam13174
Tetratricopeptide repeat;
346-369 5.86e-03

Tetratricopeptide repeat;


Pssm-ID: 463800 [Multi-domain]  Cd Length: 33  Bit Score: 34.75  E-value: 5.86e-03
                          10        20
                  ....*....|....*....|....
gi 542176767  346 LRKKGKPDEALKAFERLVQQYPQS 369
Cdd:pfam13174  10 YLELGDTDEAKEALERLIKKYPDS 33
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
346-405 7.34e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.30  E-value: 7.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 346 LRKKGKPDEALkAFERLVQQYPQSPRARYGKAQAEDDMAEKLRSNDMLQRAINTYREAAE 405
Cdd:COG3063   36 LLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPSALR 94
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
183-309 7.75e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 183 PAAETPNQQAAVPRAVEPTEAAPSVTPPRESESAAVPLPPPAEDFVPDDPqeSISPYGDEANTIDTTGVLLAEPQTEESA 262
Cdd:PRK12323 458 PAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA--SPAPAQPDAAPAGWVAESIPDPATADPD 535

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 542176767 263 GESAeyltssklTQEAELVIEAEKQPEAADVDPQSETPKQTEAEGTS 309
Cdd:PRK12323 536 DAFE--------TLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLP 574
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 354-447 7.76e-03

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 38.71  E-value: 7.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542176767 354 EALKAFERLVQQYPQSPRARYGKA---QAEDDMAEKlrsnDM------LQR-----AINTYREAAEL-PDvtSDLLRATL 418
Cdd:COG4105  132 KAIEAFQELINRYPDSEYAEDAKKridELRDKLARK----ELevaryyLKRgayvaAINRFQNVLEDyPD--TPAVEEAL 205

                         90       100
                 ....*....|....*....|....*....
gi 542176767 419 KRRAERQQFLGRMRGSLATLERLVQLFPE 447
Cdd:COG4105  206 YLLVEAYYALGRYDEAQDAAAVLGKNYPD 234
 
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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