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Conserved domains on  [gi|1622960534|ref|XP_015000921|]
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aspartyl/asparaginyl beta-hydroxylase isoform X13 [Macaca mulatta]

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 ...
 567-721 1.37e-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: 237.93  E-value: 1.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 567 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 643
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960534 644 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 721
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 ...
 47-127 8.38e-23

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


:

Pssm-ID: 428406  Cd Length: 66  Bit Score: 92.21  E-value: 8.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  47 NGRKGGPSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 126
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 1622960534 127 G 127
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 309-524 8.76e-17

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: 81.31  E-value: 8.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 309 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLP 388
Cdd:COG2956    34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 389 DVPADllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 468
Cdd:COG2956   107 PDDAE----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960534 469 HYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 160-284 8.86e-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: 45.93  E-value: 8.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  160 QNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDYNQDMEEMMSEQENPDASEPVGEDERLHHDTDDVTYQVYEEQ 239
Cdd:PTZ00341   969 ENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEEN 1048

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622960534  240 VVYEPPEN--ERIE------VTEVTVPPEDNPVEATQVIVEEvSISPVEEQQE 284
Cdd:PTZ00341  1049 AEENVEENieENIEeydeenVEEIEENIEENIEENVEENVEE-NVEEIEENVE 1100
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 567-721 1.37e-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: 237.93  E-value: 1.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 567 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 643
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960534 644 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 721
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 563-728 9.85e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 190.09  E-value: 9.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 563 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 637
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 638 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLI 713
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 1622960534 714 FIVDVWHPELTPQQR 728
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 47-127 8.38e-23

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


Pssm-ID: 428406  Cd Length: 66  Bit Score: 92.21  E-value: 8.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  47 NGRKGGPSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 126
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 1622960534 127 G 127
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 309-524 8.76e-17

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: 81.31  E-value: 8.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 309 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLP 388
Cdd:COG2956    34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 389 DVPADllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 468
Cdd:COG2956   107 PDDAE----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960534 469 HYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 318-431 3.35e-09

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


Pssm-ID: 188247 [Multi-domain]  Cd Length: 117  Bit Score: 54.98  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 318 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 389
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622960534 390 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 431
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 160-284 8.86e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 8.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  160 QNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDYNQDMEEMMSEQENPDASEPVGEDERLHHDTDDVTYQVYEEQ 239
Cdd:PTZ00341   969 ENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEEN 1048

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622960534  240 VVYEPPEN--ERIE------VTEVTVPPEDNPVEATQVIVEEvSISPVEEQQE 284
Cdd:PTZ00341  1049 AEENVEENieENIEeydeenVEEIEENIEENIEENVEENVEE-NVEEIEENVE 1100
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 321-385 5.22e-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: 38.86  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960534 321 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 385
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAAL 61
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 567-721 1.37e-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: 237.93  E-value: 1.37e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 567 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 643
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960534 644 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 721
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 563-728 9.85e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 190.09  E-value: 9.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 563 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 637
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 638 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLI 713
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 1622960534 714 FIVDVWHPELTPQQR 728
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 47-127 8.38e-23

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


Pssm-ID: 428406  Cd Length: 66  Bit Score: 92.21  E-value: 8.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  47 NGRKGGPSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 126
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 1622960534 127 G 127
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 309-524 8.76e-17

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: 81.31  E-value: 8.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 309 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLP 388
Cdd:COG2956    34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 389 DVPADllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 468
Cdd:COG2956   107 PDDAE----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960534 469 HYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
327-492 4.91e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 69.65  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 327 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL-PDVPAdllklSLKRRSDR 405
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGRYEE----ALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 406 QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIP 485
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 1622960534 486 YLKEGIE 492
Cdd:COG0457   166 LLEKLEA 172
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 323-524 8.71e-13

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: 69.37  E-value: 8.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 323 AAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEddlaekRRSNEVLRgAIETYQEVASL-PDVPADLLKLSLkr 401
Cdd:COG2956    14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLY------RRRGEYDR-AIRIHQKLLERdPDRAEALLELAQ-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 402 rsDRQQfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIA 481
Cdd:COG2956    85 --DYLK-AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622960534 482 ESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG2956   162 EAIEALEKALKL-DP--DCARALLLLAELYLEQGDyEEAIAALE 202
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 309-524 2.34e-11

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 65.14  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 309 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASLP 388
Cdd:COG2956    68 LLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEI---YEQEGDWEK----AIEVLERLLKLG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 389 DVPADLLKlslkRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 468
Cdd:COG2956   141 PENAHAYC----ELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALP 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960534 469 HYGFILKAQNKIAESIPYLKEGIESgDPGTDDGRFYFHLgdAMQRVGNKEAYKWYE 524
Cdd:COG2956   217 RLAELYEKLGDPEEALELLRKALEL-DPSDDLLLALADL--LERKEGLEAALALLE 269
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 319-492 5.09e-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: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 319 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEvaslpdvpadllkls 398
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI---LLQLGDLDE----AIVLLHE--------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 399 lkrrsdrqqflghmrgslltlqrLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 478
Cdd:COG4783    64 -----------------------ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                         170
                  ....*....|....
gi 1622960534 479 KIAESIPYLKEGIE 492
Cdd:COG4783   121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 319-524 5.19e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 66.17  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 319 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASlpdvPADLLKLS 398
Cdd:COG3914     5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAA----ALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 399 LKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 478
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622960534 479 KIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG3914   161 RLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
409-524 1.52e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.95  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 409 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 488
Cdd:COG0457    21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622960534 489 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG0457   101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 343-493 6.17e-10

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 58.43  E-value: 6.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 343 LVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRL 422
Cdd:COG5010     1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960534 423 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIES 493
Cdd:COG5010    81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 416-524 2.57e-09

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 55.78  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 416 LLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgD 495
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622960534 496 PgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG4235    82 P--DNPEALYLLGLAAFQQGDyAEAIAAWQ 109
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 318-431 3.35e-09

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


Pssm-ID: 188247 [Multi-domain]  Cd Length: 117  Bit Score: 54.98  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 318 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 389
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622960534 390 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 431
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 317-506 4.29e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 60.01  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 317 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYgkaqcedDLAEKRRSNEVLRGAIETYQEVASL-PDVPADLL 395
Cdd:COG3914    78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 396 KLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILK 475
Cdd:COG3914   151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622960534 476 AQNKIAESIPYLKEGIESGDPGTDDGRFYFH 506
Cdd:COG3914   226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
423-524 7.21e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.94  E-value: 7.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 423 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGR 502
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 1622960534 503 FYFHLGDAMQRVGN-KEAYKWYE 524
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 314-497 1.60e-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: 55.09  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 314 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY--GKAQCED-DL--AEKrrsnEVLRGAIETYQEVASLP 388
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEK----ELRKALSLGYPKNQVLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 389 DvpadLLKLSLKRRSDrqqflghmrgslltlQRLVQLFPNDTSLKND--------LGVGYLLIGDNDNAKKVYEEVLSVT 460
Cdd:TIGR02917  95 L----LARAYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAID 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622960534 461 PNDGFAKVHYGFILKAQNKIAESIPYLKEgIESGDPG 497
Cdd:TIGR02917 156 PRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
440-524 1.73e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 49.78  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 440 YLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 518
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 1622960534 519 AYKWYE 524
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 409-499 2.01e-07

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 50.39  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 409 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 488
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 1622960534 489 EGIESGDPGTD 499
Cdd:COG4235   110 KLLALLPADAP 120
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 326-428 2.03e-07

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 49.99  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 326 KLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL----PDVPADLLKLS 398
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEA---YYALGD----YDEAAEAFEKLLKRypdsPKAPDALLKLG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622960534 399 LkrrsdRQQFLGHMRGSLLTLQRLVQLFPN 428
Cdd:COG1729    75 L-----SYLELGDYDKARATLEELIKKYPD 99
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 317-503 2.43e-07

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 54.32  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 317 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAqceddLAEKRRSNevLRGAIETYQEVASL-PD-VPADL 394
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEyLPALL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 395 LK-LSLKRRSDRQQFLGHMRGSLL---------------------------TLQRLVQLFPNDTSLKNDLGVGYLLIGDN 446
Cdd:TIGR02917 300 LAgASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960534 447 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRF 503
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
409-492 4.25e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.55  E-value: 4.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 409 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKvYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 488
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 1622960534 489 EGIE 492
Cdd:COG3063    84 RALE 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 324-381 6.15e-05

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 42.67  E-value: 6.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960534 324 AEKLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCEDDLAEKRRSNEVLRGAIETY 381
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY 97
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 160-284 8.86e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 8.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  160 QNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDYNQDMEEMMSEQENPDASEPVGEDERLHHDTDDVTYQVYEEQ 239
Cdd:PTZ00341   969 ENVEENVEENVEENVEENVEENVEENVEENVEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEEN 1048

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622960534  240 VVYEPPEN--ERIE------VTEVTVPPEDNPVEATQVIVEEvSISPVEEQQE 284
Cdd:PTZ00341  1049 AEENVEENieENIEeydeenVEEIEENIEENIEENVEENVEE-NVEEIEENVE 1100
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 161-284 1.10e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  161 NIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDYNQDMEEMMSEQENPDASEPVGE--DERLHHDTDDvTYQVYEE 238
Cdd:PTZ00341   946 NIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEENVEENIEEnvEENVEENIEE-NVEEYDE 1024

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622960534  239 QVVYEPPEN----ERIEVTEVTVPPEDNPVEATQVIVEEVSISPVEEQQE 284
Cdd:PTZ00341  1025 ENVEEVEENveeyDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEE 1074
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
314-466 2.06e-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: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 314 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVlrgaietYQEVASLPDVPAD 393
Cdd:COG4785     3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960534 394 LLKLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFA 466
Cdd:COG4785    76 YYERGVAYDS-----LGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 315-492 2.13e-04

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 44.69  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 315 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQ--SPR---ARYGKAQCEDDLAE---------KRRSNEVL------ 374
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQeiEPAlalAQYYLGKGQLKKALailneaadaAPDSPEAWlmlgra 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 375 -------RGAIETYQEVASL-PDVPADLLKLSlkrrsDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDN 446
Cdd:TIGR02917 611 qlaagdlNKAVSSFKKLLALqPDSALALLLLA-----DAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRT 685

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622960534 447 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIE 492
Cdd:TIGR02917 686 ESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 309-429 2.85e-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: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 309 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL- 387
Cdd:COG4783    30 ALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLd 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622960534 388 PDVPAdllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPND 429
Cdd:COG4783   103 PEHPE-----AYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 321-385 5.22e-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: 38.86  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960534 321 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 385
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAAL 61
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 327-461 6.97e-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: 40.71  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 327 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQevaslpdvpadllklslkrrsdrq 406
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYE------------------------ 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622960534 407 qflghmrgslltlqRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTP 461
Cdd:COG5010   113 --------------KALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 334-433 8.54e-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: 41.79  E-value: 8.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 334 EEAVNAFKELVRKYPQSPRARYGKA---QCEDDLAEK---------RRSNEV-----LRGAIETYQEVASLPDVPADLLK 396
Cdd:COG4105   131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622960534 397 --LSLKRRSDRQQflghmrgsllTLQRLVQLFPNDTSLK 433
Cdd:COG4105   211 ayYALGRYDEAQD----------AAAVLGKNYPDSPYLK 239
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 314-428 1.01e-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: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 314 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQC---EDDLAEkrrsnevlrgAIETYQEVASL 387
Cdd:COG4105    29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622960534 388 ----PDVP-ADLLK-LS---LKRRSDRQQflGHMRGSLLTLQRLVQLFPN 428
Cdd:COG4105    99 ypnsPNADyAYYLRgLSyyeQSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 440-524 1.35e-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: 39.20  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 440 YLLIGDNDNAKKVYEEVLSVTPNDGFA-KVHY--GFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN 516
Cdd:COG1729     3 LLKAGDYDEAIAAFKAFLKRYPNSPLApDALYwlGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGD 82


                  ....*....
gi 1622960534 517 KE-AYKWYE 524
Cdd:COG1729    83 YDkARATLE 91
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 321-401 1.92e-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: 38.83  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 321 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL--PDVPADLLKLS 398
Cdd:COG4235    55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                  ...
gi 1622960534 399 LKR 401
Cdd:COG4235   128 IAE 130
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 152-290 2.32e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 41.31  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534  152 QAPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDYNQDMEEMMSEQENPDASEPVGE--DERLHHDTD 229
Cdd:PTZ00341   929 KNQNENVPEHLKEHAEANIEEDAEENVEEDAEENVEENVEENVEENVEENVEENVEENVEENVEENVEEnvEENIEENVE 1008

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960534  230 DVTYQVYEEQVVYEPPENERiEVTEVTVPPEDNPVEATQVIVEEVSISPVEEQQEVPPGTN 290
Cdd:PTZ00341  1009 ENVEENIEENVEEYDEENVE-EVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEEN 1068
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 309-359 3.08e-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: 3.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622960534 309 LLNKFDKTIKAE---LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQ 359
Cdd:COG1729    56 LLKRYPDSPKAPdalLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
361-524 4.71e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 39.13  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 361 EDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGhmrgsLLTLQRLVQLFPNDTSLKNDLGVGY 440
Cdd:COG4785     9 LLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAAL-----AAERIDRALALPDLAQLYYERGVAY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 441 LLIGDNDNAKKVYEEVLSVTPndGFAKVHY--GFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-K 517
Cdd:COG4785    84 DSLGDYDLAIADFDQALELDP--DLAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAYLNRGIALYYLGRyE 158


                  ....*..
gi 1622960534 518 EAYKWYE 524
Cdd:COG4785   159 LAIADLE 165
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 324-463 5.14e-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: 37.68  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 324 AEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEVLRgaietyqevaslpdvpadllklslkrrs 403
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEEAEE---------------------------- 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960534 404 drqqflghmrgsllTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPND 463
Cdd:COG4235    73 --------------LLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
TPR_14 pfam13428
Tetratricopeptide repeat;
321-360 9.59e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 34.71  E-value: 9.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622960534 321 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQC 360
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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