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Conserved domains on  [gi|14589866|ref|NP_004309|]
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aspartyl/asparaginyl beta-hydroxylase isoform 1 [Homo sapiens]

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 ...
 591-745 7.14e-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: 236.39  E-value: 7.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   591 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 667
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14589866   668 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 745
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 ...
 43-108 2.78e-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: 139.21  E-value: 2.78e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14589866    43 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLG 108
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 339-548 8.73e-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: 8.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 339 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLPDVPADl 418
Cdd:COG2956  40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELDPDDAE- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 419 lklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFIL 498
Cdd:COG2956 112 ---ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14589866 499 KAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG2956 189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 121-314 3.54e-04

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: 44.01  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   121 PEEAEPHTEPeeQVPVEAEpQNIEDEAKEQIQSLLHEMVHaEHVEgedlqqedgptgEPQQEDDEflmatdvddrfETLE 200
Cdd:PTZ00341  936 PEHLKEHAEA--NIEEDAE-ENVEEDAEENVEENVEENVE-ENVE------------ENVEENVE-----------ENVE 988

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   201 PEVSHEETEHsyhVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLEN--EGIE--- 275
Cdd:PTZ00341  989 ENVEENVEEN---VEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENieENIEeyd 1065

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 14589866   276 ---ITEVTAPPEDNPVEDSQVIVEEvSIFPVEEQQEVPPETN 314
Cdd:PTZ00341 1066 eenVEEIEENIEENIEENVEENVEE-NVEEIEENVEENVEEN 1106
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 591-745 7.14e-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: 236.39  E-value: 7.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   591 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 667
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14589866   668 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 745
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 587-752 1.83e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 189.70  E-value: 1.83e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 587 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 661
Cdd:COG3555  20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 662 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLI 737
Cdd:COG3555  94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                       170
                ....*....|....*
gi 14589866 738 FIVDVWHPELTPQQR 752
Cdd:COG3555 172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 43-108 2.78e-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: 139.21  E-value: 2.78e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14589866    43 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLG 108
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 339-548 8.73e-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: 8.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 339 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLPDVPADl 418
Cdd:COG2956  40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELDPDDAE- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 419 lklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFIL 498
Cdd:COG2956 112 ---ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14589866 499 KAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG2956 189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 342-455 3.47e-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: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   342 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 413
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 14589866   414 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 455
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 121-314 3.54e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.01  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   121 PEEAEPHTEPeeQVPVEAEpQNIEDEAKEQIQSLLHEMVHaEHVEgedlqqedgptgEPQQEDDEflmatdvddrfETLE 200
Cdd:PTZ00341  936 PEHLKEHAEA--NIEEDAE-ENVEEDAEENVEENVEENVE-ENVE------------ENVEENVE-----------ENVE 988

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   201 PEVSHEETEHsyhVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLEN--EGIE--- 275
Cdd:PTZ00341  989 ENVEENVEEN---VEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENieENIEeyd 1065

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 14589866   276 ---ITEVTAPPEDNPVEDSQVIVEEvSIFPVEEQQEVPPETN 314
Cdd:PTZ00341 1066 eenVEEIEENIEENIEENVEENVEE-NVEEIEENVEENVEEN 1106
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 345-409 5.39e-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: 5.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14589866   345 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 409
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 ...
 591-745 7.14e-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: 236.39  E-value: 7.14e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   591 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 667
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14589866   668 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 745
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 587-752 1.83e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 189.70  E-value: 1.83e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 587 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 661
Cdd:COG3555  20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 662 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLI 737
Cdd:COG3555  94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                       170
                ....*....|....*
gi 14589866 738 FIVDVWHPELTPQQR 752
Cdd:COG3555 172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 43-108 2.78e-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: 139.21  E-value: 2.78e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14589866    43 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLG 108
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 339-548 8.73e-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: 8.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 339 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLPDVPADl 418
Cdd:COG2956  40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELDPDDAE- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 419 lklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFIL 498
Cdd:COG2956 112 ---ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14589866 499 KAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG2956 189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
351-516 3.20e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.04  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 351 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL-PDVPAdllklSLKRRSDR 429
Cdd:COG0457  18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGRYEE----ALADYEQALELdPDDAE-----ALNNLGLA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 430 QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIP 509
Cdd:COG0457  86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                ....*..
gi 14589866 510 YLKEGIE 516
Cdd:COG0457 166 LLEKLEA 172
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 347-548 7.69e-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: 7.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 347 AAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEddlaekRRSNEVLRgAIETYQEVASL-PDVPADLLKLSLkr 425
Cdd:COG2956  14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLY------RRRGEYDR-AIRIHQKLLERdPDRAEALLELAQ-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 426 rsDRQQfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIA 505
Cdd:COG2956  85 --DYLK-AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 14589866 506 ESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG2956 162 EAIEALEKALKL-DP--DCARALLLLAELYLEQGDyEEAIAALE 202
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 343-516 4.74e-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: 61.36  E-value: 4.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 343 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEvaslpdvpadllkls 422
Cdd:COG4783   6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI---LLQLGDLDE----AIVLLHE--------------- 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 423 lkrrsdrqqflghmrgslltlqrLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 502
Cdd:COG4783  64 -----------------------ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                       170
                ....*....|....
gi 14589866 503 KIAESIPYLKEGIE 516
Cdd:COG4783 121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 343-548 5.46e-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: 5.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 343 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASlpdvPADLLKLS 422
Cdd:COG3914   5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAA----ALLLLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 423 LKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 502
Cdd:COG3914  81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 14589866 503 KIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG3914 161 RLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
433-548 1.05e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.72  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 433 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 512
Cdd:COG0457  21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 14589866 513 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG0457 101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 367-517 3.30e-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: 59.20  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 367 LVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRL 446
Cdd:COG5010   1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14589866 447 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIES 517
Cdd:COG5010  81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 440-548 2.18e-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: 56.17  E-value: 2.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 440 LLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgD 519
Cdd:COG4235   3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                        90       100       110
                ....*....|....*....|....*....|
gi 14589866 520 PgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 548
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 ...
 342-455 3.47e-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: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   342 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 413
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 14589866   414 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 455
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 341-530 4.50e-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: 4.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 341 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYgkaqcedDLAEKRRSNEVLRGAIETYQEVASL-PDVPADLL 419
Cdd:COG3914  78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 420 KLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILK 499
Cdd:COG3914 151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                       170       180       190
                ....*....|....*....|....*....|.
gi 14589866 500 AQNKIAESIPYLKEGIESGDPGTDDGRFYFH 530
Cdd:COG3914 226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
447-548 5.33e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.71  E-value: 5.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 447 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGR 526
Cdd:COG0457   1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                        90       100
                ....*....|....*....|...
gi 14589866 527 FYFHLGDAMQRVGN-KEAYKWYE 548
Cdd:COG0457  78 ALNNLGLALQALGRyEEALEDYD 100
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 350-452 9.29e-08

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 51.15  E-value: 9.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 350 KLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL----PDVPADLLKLS 422
Cdd:COG1729   2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEA---YYALGD----YDEAAEAFEKLLKRypdsPKAPDALLKLG 74

                        90       100       110
                ....*....|....*....|....*....|
gi 14589866 423 LkrrsdRQQFLGHMRGSLLTLQRLVQLFPN 452
Cdd:COG1729  75 L-----SYLELGDYDKARATLEELIKKYPD 99
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
464-548 1.21e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 50.17  E-value: 1.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 464 YLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 542
Cdd:COG3063   2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                ....*.
gi 14589866 543 AYKWYE 548
Cdd:COG3063  78 ALAYLE 83
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 338-521 1.23e-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: 55.47  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   338 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY--GKAQCED-DL--AEKrrsnEVLRGAIETYQEVASLP 412
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEK----ELRKALSLGYPKNQVLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   413 DvpadLLKLSLKRRSDrqqflghmrgslltlQRLVQLFPNDTSLKND--------LGVGYLLIGDNDNAKKVYEEVLSVT 484
Cdd:TIGR02917  95 L----LARAYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAID 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 14589866   485 PNDGFAKVHYGFILKAQNKIAESIPYLKEgIESGDPG 521
Cdd:TIGR02917 156 PRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 341-527 1.78e-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: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   341 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAqceddLAEKRRSNevLRGAIETYQEVASL-PD-VPADL 418
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEyLPALL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   419 LK-LSLKRRSDRQQFLGHMRGSLL---------------------------TLQRLVQLFPNDTSLKNDLGVGYLLIGDN 470
Cdd:TIGR02917 300 LAgASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 14589866   471 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRF 527
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 433-523 1.84e-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: 50.77  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 433 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 512
Cdd:COG4235  30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                        90
                ....*....|.
gi 14589866 513 EGIESGDPGTD 523
Cdd:COG4235 110 KLLALLPADAP 120
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
433-516 3.22e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.93  E-value: 3.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 433 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKvYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 512
Cdd:COG3063   5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                ....
gi 14589866 513 EGIE 516
Cdd:COG3063  84 RALE 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 348-405 4.12e-05

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 43.44  E-value: 4.12e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14589866 348 AEKLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCEDDLAEKRRSNEVLRGAIETY 405
Cdd:COG1729  37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY 97
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 339-516 1.66e-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: 45.07  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   339 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQ--SPR---ARYGKAQCEDDLAE---------KRRSNEVL------ 398
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQeiEPAlalAQYYLGKGQLKKALailneaadaAPDSPEAWlmlgra 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   399 -------RGAIETYQEVASL-PDVPADLLKLSlkrrsDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDN 470
Cdd:TIGR02917 611 qlaagdlNKAVSSFKKLLALqPDSALALLLLA-----DAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRT 685

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 14589866   471 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIE 516
Cdd:TIGR02917 686 ESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
338-490 1.92e-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: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 338 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVlrgaietYQEVASLPDVPAD 417
Cdd:COG4785   3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQL 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14589866 418 LLKLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFA 490
Cdd:COG4785  76 YYERGVAYDS-----LGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 351-485 3.39e-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: 41.87  E-value: 3.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 351 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQevaslpdvpadllklslkrrsdrq 430
Cdd:COG5010  64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYE------------------------ 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14589866 431 qflghmrgslltlqRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTP 485
Cdd:COG5010 113 --------------KALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 121-314 3.54e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.01  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   121 PEEAEPHTEPeeQVPVEAEpQNIEDEAKEQIQSLLHEMVHaEHVEgedlqqedgptgEPQQEDDEflmatdvddrfETLE 200
Cdd:PTZ00341  936 PEHLKEHAEA--NIEEDAE-ENVEEDAEENVEENVEENVE-ENVE------------ENVEENVE-----------ENVE 988

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866   201 PEVSHEETEHsyhVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLEN--EGIE--- 275
Cdd:PTZ00341  989 ENVEENVEEN---VEENIEENVEENVEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENieENIEeyd 1065

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 14589866   276 ---ITEVTAPPEDNPVEDSQVIVEEvSIFPVEEQQEVPPETN 314
Cdd:PTZ00341 1066 eenVEEIEENIEENIEENVEENVEE-NVEEIEENVEENVEEN 1106
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 351-453 4.02e-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: 41.33  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 351 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL-PDVPAdllklSLKRRSDR 429
Cdd:COG4783  48 LLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLdPEHPE-----AYLRLARA 115

                        90       100
                ....*....|....*....|....
gi 14589866 430 QQFLGHMRGSLLTLQRLVQLFPND 453
Cdd:COG4783 116 YRALGRPDEAIAALEKALELDPDD 139
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 345-409 5.39e-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: 5.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14589866   345 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 409
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAAL 61
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 358-457 5.46e-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: 42.56  E-value: 5.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 358 EEAVNAFKELVRKYPQSPRARYGKA---QCEDDLAEK---------RRSNEV-----LRGAIETYQEVASLPDVPADLLK 420
Cdd:COG4105 131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 14589866 421 --LSLKRRSDRQQflghmrgsllTLQRLVQLFPNDTSLK 457
Cdd:COG4105 211 ayYALGRYDEAQD----------AAAVLGKNYPDSPYLK 239
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 338-452 6.03e-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: 6.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 338 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQC---EDDLAEkrrsnevlrgAIETYQEVASL 411
Cdd:COG4105  29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 14589866 412 ----PDVP-ADLLK-LS---LKRRSDRQQflGHMRGSLLTLQRLVQLFPN 452
Cdd:COG4105  99 ypnsPNADyAYYLRgLSyyeQSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 464-548 7.76e-04

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: 39.59  E-value: 7.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 464 YLLIGDNDNAKKVYEEVLSVTPNDGFA-KVHY--GFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN 540
Cdd:COG1729   3 LLKAGDYDEAIAAFKAFLKRYPNSPLApDALYwlGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGD 82


                ....*....
gi 14589866 541 KE-AYKWYE 548
Cdd:COG1729  83 YDkARATLE 91
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 345-425 1.77e-03

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 39.22  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 345 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL--PDVPADLLKLS 422
Cdd:COG4235  55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                ...
gi 14589866 423 LKR 425
Cdd:COG4235 128 IAE 130
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
385-548 4.16e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 39.51  E-value: 4.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 385 EDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGhmrgsLLTLQRLVQLFPNDTSLKNDLGVGY 464
Cdd:COG4785   9 LLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAAL-----AAERIDRALALPDLAQLYYERGVAY 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 465 LLIGDNDNAKKVYEEVLSVTPndGFAKVHY--GFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-K 541
Cdd:COG4785  84 DSLGDYDLAIADFDQALELDP--DLAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAYLNRGIALYYLGRyE 158


                ....*..
gi 14589866 542 EAYKWYE 548
Cdd:COG4785 159 LAIADLE 165
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 348-487 4.61e-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: 38.06  E-value: 4.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 348 AEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEVLRgaietyqevaslpdvpadllklslkrrs 427
Cdd:COG4235  24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEEAEE---------------------------- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14589866 428 drqqflghmrgsllTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPND 487
Cdd:COG4235  73 --------------LLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 343-407 4.72e-03

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: 38.25  E-value: 4.72e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14589866 343 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQE 407
Cdd:COG4783  74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
TPR_14 pfam13428
Tetratricopeptide repeat;
345-384 7.89e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 35.09  E-value: 7.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 14589866   345 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQC 384
Cdd:pfam13428   5 LALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 338-383 8.63e-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: 36.89  E-value: 8.63e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 14589866 338 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQ 383
Cdd:COG1729  64 PKAPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
 
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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