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Conserved domains on  [gi|295390525|ref|NP_001171320|]
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aspartyl/asparaginyl beta-hydroxylase isoform 3 [Mus musculus]

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 ...
 558-712 1.76e-73

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: 234.85  E-value: 1.76e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  558 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCALLEKFS-ETTGCRRGQIKY 634
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295390525  635 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 712
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 ...
 52-117 7.90e-39

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: 137.67  E-value: 7.90e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295390525   52 NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 117
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 300-515 2.00e-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: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 300 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL- 378
Cdd:COG2956   34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 379 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAK 458
Cdd:COG2956  107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295390525 459 VHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 515
Cdd:COG2956  182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 131-289 1.79e-05

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 48.24  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  131 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 208
Cdd:PTZ00341  972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  209 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 287
Cdd:PTZ00341 1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122


                  ..
gi 295390525  288 QD 289
Cdd:PTZ00341 1123 DD 1124
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 558-712 1.76e-73

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: 234.85  E-value: 1.76e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  558 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCALLEKFS-ETTGCRRGQIKY 634
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295390525  635 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 712
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 554-719 2.13e-54

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 186.24  E-value: 2.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 554 VKSLERNWKLIRDEGLMVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCALLEKFsettgcr 628
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 629 rGQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLI 704
Cdd:COG3555   93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|....*
gi 295390525 705 FIVDVWHPELTPQQR 719
Cdd:COG3555  172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 52-117 7.90e-39

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: 137.67  E-value: 7.90e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295390525   52 NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 117
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 300-515 2.00e-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: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 300 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL- 378
Cdd:COG2956   34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 379 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAK 458
Cdd:COG2956  107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295390525 459 VHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 515
Cdd:COG2956  182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 308-494 1.98e-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: 54.70  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  308 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAqceddLAEKQRSNevLRRAIETYQEAADL-PDAPTD-- 384
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  385 LVKLSLKRRSERQQFLGHMRGSLL---------------------------TLQRLVQLFPSDTTLKNDLGVGYLLLGDN 437
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295390525  438 DSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTDDGRF 494
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 312-382 7.27e-06

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: 44.25  E-value: 7.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295390525  312 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSP---RARYGKAQCeddLAEKQRsnevLRRAIETYQEAADL-PDAP 382
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAALRAaPGDP 68
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 131-289 1.79e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 48.24  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  131 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 208
Cdd:PTZ00341  972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  209 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 287
Cdd:PTZ00341 1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122


                  ..
gi 295390525  288 QD 289
Cdd:PTZ00341 1123 DD 1124
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 558-712 1.76e-73

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: 234.85  E-value: 1.76e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  558 ERNWKLIRDEGLMVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCALLEKFS-ETTGCRRGQIKY 634
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 295390525  635 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 712
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 554-719 2.13e-54

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 186.24  E-value: 2.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 554 VKSLERNWKLIRDEGLMVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCALLEKFsettgcr 628
Cdd:COG3555   20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQI------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 629 rGQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDASSFRLI 704
Cdd:COG3555   93 -PGVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                        170
                 ....*....|....*
gi 295390525 705 FIVDVWHPELTPQQR 719
Cdd:COG3555  172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 52-117 7.90e-39

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: 137.67  E-value: 7.90e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295390525   52 NGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 117
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 300-515 2.00e-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: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 300 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL- 378
Cdd:COG2956   34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLE-------LAQDYLKAGLLDRAEELLEKLLELd 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 379 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAK 458
Cdd:COG2956  107 PDDAE-----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARAL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295390525 459 VHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 515
Cdd:COG2956  182 LLLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
318-483 2.39e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.42  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 318 LRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAADL-PDAPTdlvklSLKRRSER 396
Cdd:COG0457   18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGRYEE----ALADYEQALELdPDDAE-----ALNNLGLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 397 QQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIP 476
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                 ....*..
gi 295390525 477 YLKEGIE 483
Cdd:COG0457  166 LLEKLEA 172
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 310-483 5.42e-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: 60.98  E-value: 5.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 310 AELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddlaekqrsnevlrraietYQEAADLPDAptdlvkls 389
Cdd:COG4783    6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI--------------------LLQLGDLDEA-------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 390 lkrrserqqflghmrgsLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQN 469
Cdd:COG4783   58 -----------------IVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                        170
                 ....*....|....
gi 295390525 470 KISESIPYLKEGIE 483
Cdd:COG4783  121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 308-497 3.99e-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: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 308 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYgkaqcedDLAEKQRSNEVLRRAIETYQEAADL-PDAPTDLV 386
Cdd:COG3914   78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 387 KLSLKRRSerqqfLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILK 466
Cdd:COG3914  151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                        170       180       190
                 ....*....|....*....|....*....|.
gi 295390525 467 AQNKISESIPYLKEGIESGDPGTDDGRFYFH 497
Cdd:COG3914  226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
400-515 6.32e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.41  E-value: 6.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 400 LGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLK 479
Cdd:COG0457   21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 295390525 480 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 515
Cdd:COG0457  101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
339-533 9.78e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 59.64  E-value: 9.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 339 PQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADlpdaptdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFP 418
Cdd:COG0457    5 PDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAE-----------ALYNLGLAYLRLGRYEEALADYEQALELDP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 419 SDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESgDPgtDDGRFYFHL 498
Cdd:COG0457   74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL-DP--DDADALYNL 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 295390525 499 GDAMQRVGN-KEAYKWYELGHKRGHFASVWQRSLYN 533
Cdd:COG0457  151 GIALEKLGRyEEALELLEKLEAAALAALLAAALGEA 186
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 334-484 4.07e-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: 56.12  E-value: 4.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 334 LVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAPTDLVKLSLKRRSERQQFLGHMRGSLLTLQRL 413
Cdd:COG5010    1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295390525 414 VQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIES 484
Cdd:COG5010   81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 317-419 2.14e-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: 52.69  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 317 KLRKRGKIEEAVNAFEELVRKYPQS---PRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAptdLVKLslkrr 393
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDA---LLKL----- 73

                         90       100
                 ....*....|....*....|....*.
gi 295390525 394 SERQQFLGHMRGSLLTLQRLVQLFPS 419
Cdd:COG1729   74 GLSYLELGDYDKARATLEELIKKYPD 99
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
414-515 6.44e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 54.24  E-value: 6.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 414 VQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESgDPgtDDGR 493
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                         90       100
                 ....*....|....*....|...
gi 295390525 494 FYFHLGDAMQRVGN-KEAYKWYE 515
Cdd:COG0457   78 ALNNLGLALQALGRyEEALEDYD 100
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 308-494 1.98e-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: 54.70  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  308 IKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAqceddLAEKQRSNevLRRAIETYQEAADL-PDAPTD-- 384
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEYLPAll 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  385 LVKLSLKRRSERQQFLGHMRGSLL---------------------------TLQRLVQLFPSDTTLKNDLGVGYLLLGDN 437
Cdd:TIGR02917 300 LAGASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295390525  438 DSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTDDGRF 494
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
431-515 3.48e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.63  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 431 YLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 509
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                 ....*.
gi 295390525 510 AYKWYE 515
Cdd:COG3063   78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 367-490 8.84e-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: 48.46  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 367 RAIETYQEAadLPDAPTDLVKLSLKRRSERQQflGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEE 446
Cdd:COG4235    1 EAIARLRQA--LAANPNDAEGWLLLGRAYLRL--GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLER 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 295390525 447 VLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDPGTD 490
Cdd:COG4235   77 ALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAP 120
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 305-488 1.36e-06

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 52.01  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  305 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARY--GKAQCED-DL--AEKQrsnevLRRAIET-YQEAADL 378
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEKE-----LRKALSLgYPKNQVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  379 PDaptdLVKLSLKRRSerqqflghmrgslltLQRLVQLFPSDTTLKND--------LGVGYLLLGDNDSAKKVYEEVLNV 450
Cdd:TIGR02917  94 PL----LARAYLLQGK---------------FQQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 295390525  451 TPNDGFAKVHYGFILKAQNKISESIPYLKEgIESGDPG 488
Cdd:TIGR02917 155 DPRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 315-388 1.63e-06

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 47.29  E-value: 1.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295390525 315 AEKLRKRGKIEEAVNAFEELVRKYPQS---PRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADLPDAPTDLVKL 388
Cdd:COG1729   37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARARLARL 113
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 326-454 3.72e-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: 3.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 326 EAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL-PDAPTDLVKLslkrrSERQQFLGHMR 404
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLL-------LGRAYLRLGRYDEALAAYEKALRLdPDNADALLDL-----AEALLAAGDTE 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 295390525 405 GSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPND 454
Cdd:COG4235   69 EAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 312-382 7.27e-06

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: 44.25  E-value: 7.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 295390525  312 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSP---RARYGKAQCeddLAEKQRsnevLRRAIETYQEAADL-PDAP 382
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAALRAaPGDP 68
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
400-483 1.49e-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: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 400 LGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKvYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLK 479
Cdd:COG3063    5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                 ....
gi 295390525 480 EGIE 483
Cdd:COG3063   84 RALE 87
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 131-289 1.79e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 48.24  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  131 EEEAETHAE--LEEQAPEGADiQNVEDEVKEQIQSLLQESVHTDHDLEADGLAGEPQPEVEDFLTVTDSDDRFEdlepgt 208
Cdd:PTZ00341  972 EENVEENVEenVEENVEENVE-ENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEE------ 1044

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  209 VHEEIEDtyHVEDTASQN-HPNDMEEMTNEQENSEEVRHQDYDEPVYEPSEHEGVAISDNTIDDSSIISEEINVASVEEQ 287
Cdd:PTZ00341 1045 IEENAEE--NVEENIEENiEEYDEENVEEIEENIEENIEENVEENVEENVEEIEENVEENVEENAEENAEENAEENAEEY 1122


                  ..
gi 295390525  288 QD 289
Cdd:PTZ00341 1123 DD 1124
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 306-483 1.01e-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: 45.84  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  306 KTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGkaqceddLAEKQRSNEVLRRAIETYQEAADL-PDAPTD 384
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALA-------LAQYYLGKGQLKKALAILNEAADAaPDSPEA 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  385 LVKL---------------SLKRRSERQ--QFLGHMR------------GSLLTLQRLVQLFPSDTTLKNDLGVGYLLLG 435
Cdd:TIGR02917 604 WLMLgraqlaagdlnkavsSFKKLLALQpdSALALLLladayavmknyaKAITSLKRALELKPDNTEAQIGLAQLLLAAK 683

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 295390525  436 DNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIE 483
Cdd:TIGR02917 684 RTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 300-420 1.20e-04

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.49  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 300 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAADL- 378
Cdd:COG4783   30 ALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLd 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 295390525 379 PDAPTdlvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSD 420
Cdd:COG4783  103 PEHPE-----AYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 318-452 1.35e-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: 43.03  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 318 LRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAadlpdaptdlvklslkrrserq 397
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYEKA---------------------- 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295390525 398 qflghmrgslltlqrlVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTP 452
Cdd:COG5010  115 ----------------LALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 319-483 1.45e-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: 45.46  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  319 RKRGKIEEAVNAFEELVRKYPQSPRARYGKAqcedDLAEKQRSNEvlrRAIETYQEAADLpdAPTDL-VKLSLKRRSERQ 397
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALA----GLYLRTGNEE---EAVAWLEKAAEL--NPQEIePALALAQYYLGK 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  398 qflGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPY 477
Cdd:TIGR02917 581 ---GQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITS 657


                  ....*.
gi 295390525  478 LKEGIE 483
Cdd:TIGR02917 658 LKRALE 663
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 312-392 1.70e-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: 41.92  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 312 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRsnevLRRAIETYQEAADL--PDAPTDLVKLS 389
Cdd:COG4235   55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                 ...
gi 295390525 390 LKR 392
Cdd:COG4235  128 IAE 130
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 315-420 1.92e-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: 41.92  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 315 AEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRSNEvlrrAIETYQEAADLpdAPTDLVKLSLKRRS 394
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEE----AEELLERALAL--DPDNPEALYLLGLA 94

                         90       100
                 ....*....|....*....|....*.
gi 295390525 395 ERQQflGHMRGSLLTLQRLVQLFPSD 420
Cdd:COG4235   95 AFQQ--GDYAEAIAAWQKLLALLPAD 118
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
305-457 2.39e-04

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 43.37  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 305 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAAdlpdaptd 384
Cdd:COG4785    3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAERIDRALALPDLAQ-------- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295390525 385 lvklSLKRRSERQQFLGHMRGSLLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFA 457
Cdd:COG4785   75 ----LYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 300-381 5.37e-04

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 42.18  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 300 LLNKFDKTIKAElDAAEKLR------------------KRGKIEEAVNAFEELVRKYPQSP---RARYGKAQCEDDLAEK 358
Cdd:COG4105  140 LINRYPDSEYAE-DAKKRIDelrdklarkelevaryylKRGAYVAAINRFQNVLEDYPDTPaveEALYLLVEAYYALGRY 218

                         90       100
                 ....*....|....*....|...
gi 295390525 359 QRSNEVLRRAIETYQEAADLPDA 381
Cdd:COG4105  219 DEAQDAAAVLGKNYPDSPYLKDA 241
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 409-515 8.78e-04

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 8.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 409 TLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPNDGFAKVHYGFILKAQNKISESIPYLKEGIESGDpg 488
Cdd:COG2956   30 LLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDP-- 107

                         90       100
                 ....*....|....*....|....*...
gi 295390525 489 tDDGRFYFHLGDAMQRVGN-KEAYKWYE 515
Cdd:COG2956  108 -DDAEALRLLAEIYEQEGDwEKAIEVLE 134
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 325-400 1.17e-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: 41.40  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 325 EEAVNAFEELVRKYPQSPRARYGKA---QCEDDLAEK---------QRSNEV-----LRRAIETYQEAADLPDAPTDLVK 387
Cdd:COG4105  131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                         90
                 ....*....|....*
gi 295390525 388 --LSLKRRSERQQFL 400
Cdd:COG4105  211 ayYALGRYDEAQDAA 225
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
318-453 2.90e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 318 LRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCeddLAEKQRsnevlrraietYQEAadlpdaptdlvklslkrrserq 397
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLL---LLEQGR-----------YDEA---------------------- 45

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 295390525 398 qflghmrgslLTLQRLVQLFPSDTTLKNDLGVGYLLLGDNDSAKKVYEEVLNVTPN 453
Cdd:COG3063   46 ----------IALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 300-350 3.07e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.05  E-value: 3.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 295390525 300 LLNKFDKTIKAE---LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQ 350
Cdd:COG1729   56 LLKRYPDSPKAPdalLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 300-378 4.20e-03

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: 39.71  E-value: 4.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 295390525 300 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADL 378
Cdd:COG2956  170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLL 248
TPR_19 pfam14559
Tetratricopeptide repeat;
322-378 4.36e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 36.02  E-value: 4.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 295390525  322 GKIEEAVNAFEELVRKYPQSPRARYGKAQCEDDLAEKQRSNEVLRRAIETYQEAADL 378
Cdd:pfam14559   2 GDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRY 58
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 324-398 4.83e-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: 39.46  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  324 IEEAVNAFEELVRKYPQSPRARYGKAQ---CEDDLAEK---------QRSNEV-----LRRAIETYQEAADLPDAPTDLV 386
Cdd:TIGR03302 131 AREAFEAFQELIRRYPNSEYAPDAKKRmdyLRNRLAGKelyvarfylKRGAYVaainrFQTVVENYPDTPATEEALARLV 210

                          90
                  ....*....|....
gi 295390525  387 K--LSLKRRSERQQ 398
Cdd:TIGR03302 211 EayLKLGLTDLAQD 224
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 313-418 5.38e-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: 39.07  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525  313 DAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARygKAQCedDLAEKQRSNEVLRRAIETYQEAADL----PDAPTDLVKL 388
Cdd:TIGR03302  38 EEAKEALDSGDYTEAIKYFEALESRYPFSPYAE--QAQL--DLAYAYYKSGDYAEAIAAADRFIRLhpnhPDADYAYYLR 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 295390525  389 SL---KR--RSERQQflGHMRGSLLTLQRLVQLFP 418
Cdd:TIGR03302 114 GLsnyNQidRVDRDQ--TAAREAFEAFQELIRRYP 146
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 305-418 6.26e-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: 39.09  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295390525 305 DKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSP---RARYGKAQC---EDDLAEkqrsnevlrrAIETYQEAADL 378
Cdd:COG4105   29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 295390525 379 ----PDAPTDLVKLSL-----KRRSERQQflGHMRGSLLTLQRLVQLFP 418
Cdd:COG4105   99 ypnsPNADYAYYLRGLsyyeqSPDSDRDQ--TSTRKAIEAFQELINRYP 145
TPR_14 pfam13428
Tetratricopeptide repeat;
312-351 7.70e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 35.09  E-value: 7.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 295390525  312 LDAAEKLRKRGKIEEAVNAFEELVRKYPQSPRARYGKAQC 351
Cdd:pfam13428   5 LALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
 
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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