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Conserved domains on  [gi|742084752|ref|XP_010828609|]
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PREDICTED: aspartyl/asparaginyl beta-hydroxylase isoform X1 [Bison bison bison]

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 ...
 672-826 3.56e-74

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: 238.70  E-value: 3.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  672 ERNWKLIRDEGLAAMDRTHGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCSLLDKFP-ETTGCRRGQIKY 748
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742084752  749 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 826
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 88-168 7.87e-24

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: 95.29  E-value: 7.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752   88 NGRKGGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 167
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 742084752  168 G 168
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 420-629 2.90e-18

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: 85.94  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 420 KTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQceDDLAEKRrsneiLRRAIETYQEAASL-PDAPTd 498
Cdd:COG2956   40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELdPDDAE- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 499 lvklSLKRRSDRQQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFI 578
Cdd:COG2956  112 ----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742084752 579 LKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG2956  188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 672-826 3.56e-74

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: 238.70  E-value: 3.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  672 ERNWKLIRDEGLAAMDRTHGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCSLLDKFP-ETTGCRRGQIKY 748
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742084752  749 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 826
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 668-833 5.19e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 189.32  E-value: 5.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 668 VKSLERNWKLIRDEGLAAMDRTHGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCSLLDKFPettgcr 742
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 743 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLI 818
Cdd:COG3555   94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|....*
gi 742084752 819 FIVDVWHPELTPHQR 833
Cdd:COG3555  172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 88-168 7.87e-24

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: 95.29  E-value: 7.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752   88 NGRKGGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 167
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 742084752  168 G 168
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 420-629 2.90e-18

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: 85.94  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 420 KTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQceDDLAEKRrsneiLRRAIETYQEAASL-PDAPTd 498
Cdd:COG2956   40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELdPDDAE- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 499 lvklSLKRRSDRQQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFI 578
Cdd:COG2956  112 ----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742084752 579 LKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG2956  188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 422-608 7.93e-08

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: 56.25  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  422 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAqceddLAEKRRSNeiLRRAIETYQEAASL-PDAPTD-- 498
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  499 LVKLSLKRRSDRQQFLGHMRGSLL---------------------------TLQKLVQLFPDDTALKNDLGVGYLLIGDN 551
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 742084752  552 DSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRF 608
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 426-496 2.60e-04

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 40.01  E-value: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742084752  426 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPG---ARYGKAQCeddLAEKRRsneiLRRAIETYQEAASL-PDAP 496
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPDaaaALLLLGLA---ALRQGR----LAEAAAAYRAALRAaPGDP 68
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 672-826 3.56e-74

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: 238.70  E-value: 3.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  672 ERNWKLIRDEGLAAMDRTHGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCSLLDKFP-ETTGCRRGQIKY 748
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742084752  749 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 826
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 668-833 5.19e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 189.32  E-value: 5.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 668 VKSLERNWKLIRDEGLAAMDRTHGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCSLLDKFPettgcr 742
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 743 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLI 818
Cdd:COG3555   94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|....*
gi 742084752 819 FIVDVWHPELTPHQR 833
Cdd:COG3555  172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 88-168 7.87e-24

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: 95.29  E-value: 7.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752   88 NGRKGGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 167
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 742084752  168 G 168
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 420-629 2.90e-18

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: 85.94  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 420 KTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQceDDLAEKRrsneiLRRAIETYQEAASL-PDAPTd 498
Cdd:COG2956   40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELdPDDAE- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 499 lvklSLKRRSDRQQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFI 578
Cdd:COG2956  112 ----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 742084752 579 LKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG2956  188 YLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
432-597 1.80e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 71.19  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 432 LRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRsneiLRRAIETYQEAASL-PDAPTdlvklSLKRRSDR 510
Cdd:COG0457   18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGR----YEEALADYEQALELdPDDAE-----ALNNLGLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 511 QQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIP 590
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                 ....*..
gi 742084752 591 YLKEGIE 597
Cdd:COG0457  166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 424-597 1.21e-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: 62.90  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 424 AELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRSNEilrrAIETYQEAaslpdaptdlvkls 503
Cdd:COG4783    6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI---LLQLGDLDE----AIVLLHEA-------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 504 lkrrsdrqqflghmrgslltlqklVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 583
Cdd:COG4783   65 ------------------------LELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                        170
                 ....*....|....
gi 742084752 584 KIAESIPYLKEGIE 597
Cdd:COG4783  121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 424-629 3.19e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 66.94  E-value: 3.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 424 AELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCEDDLAEKRRSNEILRRAIETYQEAAslpdAPTDLVKLS 503
Cdd:COG3914    5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAA----AALLLLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 504 LKRRSDRQQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 583
Cdd:COG3914   81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 742084752 584 KIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG3914  161 RLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
514-629 3.41e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 514 LGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 593
Cdd:COG0457   21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 742084752 594 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG0457  101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 422-611 5.44e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 63.09  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 422 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYgkaqcedDLAEKRRSNEILRRAIETYQEAASL-PDAPTDLV 500
Cdd:COG3914   78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 501 KLSLKRRSdrqqfLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILK 580
Cdd:COG3914  151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                        170       180       190
                 ....*....|....*....|....*....|.
gi 742084752 581 AQNKIAESIPYLKEGIESGDPGTDDGRFYFH 611
Cdd:COG3914  226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 514-598 1.23e-09

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: 57.66  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 514 LGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 593
Cdd:COG5010   67 LGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQ 146


                 ....*
gi 742084752 594 EGIES 598
Cdd:COG5010  147 RALGT 151
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
528-629 9.41e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.94  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 528 VQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGR 607
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                         90       100
                 ....*....|....*....|...
gi 742084752 608 FYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG0457   78 ALNNLGLALQALGRyEEALEDYD 100
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 431-536 4.16e-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: 51.92  E-value: 4.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 431 KLRKRGKIEEAVNAFEELVRKYPQS---PGARYGKAQCEDDLAEKRRSNEILRRAIETYQEAASLPDAptdLVKLSLkrr 507
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA---LLKLGL--- 75

                         90       100
                 ....*....|....*....|....*....
gi 742084752 508 sdRQQFLGHMRGSLLTLQKLVQLFPDDTA 536
Cdd:COG1729   76 --SYLELGDYDKARATLEELIKKYPDSEA 102
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 422-608 7.93e-08

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: 56.25  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  422 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAqceddLAEKRRSNeiLRRAIETYQEAASL-PDAPTD-- 498
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  499 LVKLSLKRRSDRQQFLGHMRGSLL---------------------------TLQKLVQLFPDDTALKNDLGVGYLLIGDN 551
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 742084752  552 DSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRF 608
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 419-602 1.09e-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: 55.86  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  419 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARY--GKAQCED-DL--AEKRrsneiLRRAIET-YQEAASL 492
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEKE-----LRKALSLgYPKNQVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  493 PDaptdLVKLSLKRRSDrqqflghmrgslltlQKLVQLFPDDTALKND--------LGVGYLLIGDNDSAKKVYEEVLSV 564
Cdd:TIGR02917  94 PL----LARAYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 742084752  565 TPNDGFAKVHYGFILKAQNKIAESIPYLKEgIESGDPG 602
Cdd:TIGR02917 155 DPRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 481-604 1.16e-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: 51.16  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 481 RAIETYQEAASL-PDAPTDLVKLSLKRRSdrqqfLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYE 559
Cdd:COG4235    1 EAIARLRQALAAnPNDAEGWLLLGRAYLR-----LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 742084752 560 EVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTD 604
Cdd:COG4235   76 RALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
545-629 2.75e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.01  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 545 YLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 623
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                 ....*.
gi 742084752 624 AYRWYE 629
Cdd:COG3063   78 ALAYLE 83
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
514-597 3.22e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.32  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 514 LGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKvYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 593
Cdd:COG3063    5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                 ....
gi 742084752 594 EGIE 597
Cdd:COG3063   84 RALE 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 545-629 3.40e-06

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: 47.65  E-value: 3.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 545 YLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 623
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGQdDE 140


                 ....*.
gi 742084752 624 AYRWYE 629
Cdd:COG5010  141 AKAALQ 146
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 429-502 5.33e-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: 46.14  E-value: 5.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742084752 429 AEKLRKRGKIEEAVNAFEELVRKYPQS---PGARYGKAQCEDDLAEKRRSNEILRRAIETYQEAASLPDAPTDLVKL 502
Cdd:COG1729   37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 433-597 7.25e-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: 49.70  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  433 RKRGKIEEAVNAFEELVRKYPQSPGARYGKAqcedDLAEKRRSNEilrRAIETYQEAASL-PDAPTDLVKLSLKRRSDrq 511
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALA----GLYLRTGNEE---EAVAWLEKAAELnPQEIEPALALAQYYLGK-- 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  512 qflGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPY 591
Cdd:TIGR02917 581 ---GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITS 657


                  ....*.
gi 742084752  592 LKEGIE 597
Cdd:TIGR02917 658 LKRALE 663
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 420-597 1.01e-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: 49.31  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  420 KTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQ--SPG---ARYGKAQCEDDLAE---------KRRSNEIL------ 479
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQeiEPAlalAQYYLGKGQLKKALailneaadaAPDSPEAWlmlgra 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  480 -------RRAIETYQEAASL-PDAPTDLVKLSlkrrsDRQQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDN 551
Cdd:TIGR02917 611 qlaagdlNKAVSSFKKLLALqPDSALALLLLA-----DAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRT 685

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 742084752  552 DSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIE 597
Cdd:TIGR02917 686 ESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
419-571 5.33e-05

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.29  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 419 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCEDDLAEKRRSNEILRRAIETYQEAASLpdaptd 498
Cdd:COG4785    3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQLY------ 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742084752 499 lvkLSLKRRSDRQQFLGhmrGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFA 571
Cdd:COG4785   77 ---YERGVAYDSLGDYD---LAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 432-534 6.69e-05

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 43.64  E-value: 6.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 432 LRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRSNEilrrAIETYQEAASL-PDAPTdlvklSLKRRSDR 510
Cdd:COG4783   48 LLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLdPEHPE-----AYLRLARA 115

                         90       100
                 ....*....|....*....|....
gi 742084752 511 QQFLGHMRGSLLTLQKLVQLFPDD 534
Cdd:COG4783  116 YRALGRPDEAIAALEKALELDPDD 139
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 523-629 7.33e-05

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: 45.49  E-value: 7.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 523 TLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDpg 602
Cdd:COG2956   30 LLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDP-- 107

                         90       100
                 ....*....|....*....|....*...
gi 742084752 603 tDDGRFYFHLGDAMQRVGN-KEAYRWYE 629
Cdd:COG2956  108 -DDAEALRLLAEIYEQEGDwEKAIEVLE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 432-566 2.11e-04

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: 42.64  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 432 LRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRsneiLRRAIETYQEAaslpdaptdlvklslkrrsdrq 511
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYEKA---------------------- 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 742084752 512 qflghmrgslltlqklVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTP 566
Cdd:COG5010  115 ----------------LALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 426-496 2.60e-04

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 40.01  E-value: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742084752  426 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPG---ARYGKAQCeddLAEKRRsneiLRRAIETYQEAASL-PDAP 496
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPDaaaALLLLGLA---ALRQGR----LAEAAAAYRAALRAaPGDP 68
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 424-488 3.21e-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: 41.72  E-value: 3.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742084752 424 AELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCEDDLAEKRRSNEILRRAIETYQE 488
Cdd:COG4783   74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
type_IV_pilW TIGR02521
type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF ...
 515-598 3.33e-04

type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF and PilW. This outer membrane protein is required both for pilus stability and for pilus function such as adherence to human cells. Members of this family contain copies of the TPR (tetratricopeptide repeat) domain.


Pssm-ID: 131573 [Multi-domain]  Cd Length: 234  Bit Score: 43.09  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  515 GHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKE 594
Cdd:TIGR02521  45 GDLEVAKENLDKALEHDPDDYLAYLALALYYQQLGELEKAEDSFRRALTLNPNNGDVLNNYGTFLCQQGKYEQAMQQFEQ 124


                  ....
gi 742084752  595 GIES 598
Cdd:TIGR02521 125 AIED 128
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 429-536 3.51e-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: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 429 AEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRSNEilrrAIETYQEAASLpdAPTDLVKLSLKRRS 508
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEE----AEELLERALAL--DPDNPEALYLLGLA 94

                         90       100
                 ....*....|....*....|....*...
gi 742084752 509 DRQQflGHMRGSLLTLQKLVQLFPDDTA 536
Cdd:COG4235   95 AFQQ--GDYAEAIAAWQKLLALLPADAP 120
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
466-629 8.33e-04

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 41.82  E-value: 8.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 466 EDDLAEKRRSNEILRRAIETYQEAASLPDAPTDLVKLSLKRRSDRQQFLGhmrgsLLTLQKLVQLFPDDTALKNDLGVGY 545
Cdd:COG4785    9 LLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAAL-----AAERIDRALALPDLAQLYYERGVAY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 546 LLIGDNDSAKKVYEEVLSVTPndGFAKVHY--GFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-K 622
Cdd:COG4785   84 DSLGDYDLAIADFDQALELDP--DLAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAYLNRGIALYYLGRyE 158


                 ....*..
gi 742084752 623 EAYRWYE 629
Cdd:COG4785  159 LAIADLE 165
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 439-538 1.57e-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: 41.02  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 439 EEAVNAFEELVRKYPQSPGARYGKA---QCEDDLAEK---------RRSNEI-----LRRAIETYQEAASLPDAPTDLVK 501
Cdd:COG4105  131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 742084752 502 --LSLKRRSDRQQflghmrgsllTLQKLVQLFPDDTALK 538
Cdd:COG4105  211 ayYALGRYDEAQD----------AAAVLGKNYPDSPYLK 239
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 436-617 1.60e-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: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  436 GKIEEAVNAFEELVRKYPQSPGARYGKAQ---CEDDLAEKRrsnEILRRAIETYQEAAslpDAptdlvkLSLKrrSDRQQ 512
Cdd:TIGR02917 139 GQLELAQKSYEQALAIDPRSLYAKLGLAQlalAENRFDEAR---ALIDEVLTADPGNV---DA------LLLK--GDLLL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  513 FLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAkvHYgfiLKA-----QNKIAE 587
Cdd:TIGR02917 205 SLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLA--HY---LKAlvdfqKKNYED 279

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 742084752  588 SIPYLKEGIESgDPGTDDGRFY-----FHLGDAMQ 617
Cdd:TIGR02917 280 ARETLQDALKS-APEYLPALLLagaseYQLGNLEQ 313
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 426-506 3.51e-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: 38.45  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 426 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRsneiLRRAIETYQEAASL--PDAPTDLVKLS 503
Cdd:COG4235   55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                 ...
gi 742084752 504 LKR 506
Cdd:COG4235  128 IAE 130
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
432-567 4.58e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.07  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752 432 LRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCeddLAEKRRsneilrraietYQEAaslpdaptdlvklslkrrsdrq 511
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLL---LLEQGR-----------YDEA---------------------- 45

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 742084752 512 qflghmrgslLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPN 567
Cdd:COG3063   46 ----------IALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 428-594 4.60e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.84  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  428 AAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQceddlaEKRRSNEIlRRAIETYQEAASLPDAPTdlvklslkrR 507
Cdd:TIGR02917 369 LGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGI------SKLSQGDP-SEAIADLETAAQLDPELG---------R 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  508 SDRQQFLGHMRG-----SLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQ 582
Cdd:TIGR02917 433 ADLLLILSYLRSgqfdkALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQE 512

                         170
                  ....*....|..
gi 742084752  583 NKIAESIPYLKE 594
Cdd:TIGR02917 513 GNPDDAIQRFEK 524
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 438-516 8.14e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 38.69  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742084752  438 IEEAVNAFEELVRKYPQSPGARYGKAQ---CEDDLAEK---------RRSNEI-----LRRAIETYQEAASLPDAPTDLV 500
Cdd:TIGR03302 131 AREAFEAFQELIRRYPNSEYAPDAKKRmdyLRNRLAGKelyvarfylKRGAYVaainrFQTVVENYPDTPATEEALARLV 210

                          90       100
                  ....*....|....*....|.
gi 742084752  501 ----KLSLKRRSDR-QQFLGH 516
Cdd:TIGR03302 211 eaylKLGLTDLAQDaAAVLGA 231
 
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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