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Conserved domains on  [gi|1370512372|ref|XP_024302923|]
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aspartyl/asparaginyl beta-hydroxylase isoform X23 [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 ...
 544-725 1.32e-68

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: 222.14  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 544 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 620
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 621 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKngdfcpyvpgseikhshntgggaysleTWEEGKVLIFD 700
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETR---------------------------TWREGECLLFD 132

                         170       180
                  ....*....|....*....|....*
gi 1370512372 701 DSFEHEVWQDASSFRLIFIVDVWHP 725
Cdd:pfam05118 133 DSFEHEAWNETDEPRVVLLVDVWRP 157
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 43-123 2.22e-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: 93.75  E-value: 2.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  43 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 122
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 1370512372 123 G 123
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 292-501 4.93e-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: 82.08  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 292 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLPDVPADl 371
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELDPDDAE- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 372 lklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFIL 451
Cdd:COG2956   112 ---ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370512372 452 KAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
rne super family cl35953
ribonuclease E; Reviewed
 132-266 2.01e-05

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.11  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  132 PAVPPEEAEPHTEPEEQVpVEAEPQNIEDEAKEQIQSLLHE-------------MVHAEHETEHSYHVEETDS---SEPV 195
Cdd:PRK10811   846 PVVRPQDVQVEEQREAEE-VQVQPVVAEVPVAAAVEPVVSApvveavaevveepVVVAEPQPEEVVVVETTHPeviAAPV 924

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370512372  196 VEDERLHHDTDDVTYQVYEEQAvyEPLENEGIEITEVTAPPE--DNPVEDSQVIVEEVSIFPVEEQQEVPPET 266
Cdd:PRK10811   925 TEQPQVITESDVAVAQEVAEHA--EPVVEPQDETADIEEAAEtaEVVVAEPEVVAQPAAPVVAEVAAEVETVT 995
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 544-725 1.32e-68

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: 222.14  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 544 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 620
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 621 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKngdfcpyvpgseikhshntgggaysleTWEEGKVLIFD 700
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETR---------------------------TWREGECLLFD 132

                         170       180
                  ....*....|....*....|....*
gi 1370512372 701 DSFEHEVWQDASSFRLIFIVDVWHP 725
Cdd:pfam05118 133 DSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 540-732 3.11e-50

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 175.06  E-value: 3.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 540 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 614
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 615 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETkngdfcpyvpgseikhshntgggayslET 690
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGET---------------------------YS 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370512372 691 WEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQR 732
Cdd:COG3555   145 WREGEAVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 43-123 2.22e-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: 93.75  E-value: 2.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  43 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 122
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 1370512372 123 G 123
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 292-501 4.93e-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: 82.08  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 292 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLPDVPADl 371
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELDPDDAE- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 372 lklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFIL 451
Cdd:COG2956   112 ---ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370512372 452 KAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
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 ...
 295-408 3.37e-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: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 295 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 366
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370512372 367 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 408
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
rne PRK10811
ribonuclease E; Reviewed
 132-266 2.01e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.11  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  132 PAVPPEEAEPHTEPEEQVpVEAEPQNIEDEAKEQIQSLLHE-------------MVHAEHETEHSYHVEETDS---SEPV 195
Cdd:PRK10811   846 PVVRPQDVQVEEQREAEE-VQVQPVVAEVPVAAAVEPVVSApvveavaevveepVVVAEPQPEEVVVVETTHPeviAAPV 924

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370512372  196 VEDERLHHDTDDVTYQVYEEQAvyEPLENEGIEITEVTAPPE--DNPVEDSQVIVEEVSIFPVEEQQEVPPET 266
Cdd:PRK10811   925 TEQPQVITESDVAVAQEVAEHA--EPVVEPQDETADIEEAAEtaEVVVAEPEVVAQPAAPVVAEVAAEVETVT 995
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 298-362 5.25e-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: 5.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370512372 298 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 362
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 ...
 544-725 1.32e-68

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: 222.14  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 544 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 620
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 621 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKngdfcpyvpgseikhshntgggaysleTWEEGKVLIFD 700
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETR---------------------------TWREGECLLFD 132

                         170       180
                  ....*....|....*....|....*
gi 1370512372 701 DSFEHEVWQDASSFRLIFIVDVWHP 725
Cdd:pfam05118 133 DSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 540-732 3.11e-50

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 175.06  E-value: 3.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 540 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 614
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 615 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETkngdfcpyvpgseikhshntgggayslET 690
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGET---------------------------YS 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370512372 691 WEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQR 732
Cdd:COG3555   145 WREGEAVLFDDTYEHEAWNDTDETRVVLFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 43-123 2.22e-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: 93.75  E-value: 2.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  43 NGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGIYDADGDGDFDVDDAKVLL 122
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 1370512372 123 G 123
Cdd:pfam05279  66 G 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 292-501 4.93e-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: 82.08  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 292 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLPDVPADl 371
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELDPDDAE- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 372 lklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFIL 451
Cdd:COG2956   112 ---ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELY 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370512372 452 KAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
Cdd:COG2956   189 LEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
304-469 3.91e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 69.65  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 304 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL-PDVPAdllklSLKRRSDR 382
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGRYEE----ALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 383 QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIP 462
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 1370512372 463 YLKEGIE 469
Cdd:COG0457   166 LLEKLEA 172
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 300-501 4.75e-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: 70.14  E-value: 4.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 300 AAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEddlaekRRSNEVLRgAIETYQEVASL-PDVPADLLKLSLkr 378
Cdd:COG2956    14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLY------RRRGEYDR-AIRIHQKLLERdPDRAEALLELAQ-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 379 rsDRQQfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIA 458
Cdd:COG2956    85 --DYLK-AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370512372 459 ESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
Cdd:COG2956   162 EAIEALEKALKL-DP--DCARALLLLAELYLEQGDyEEAIAALE 202
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 296-469 3.07e-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: 61.75  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 296 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEvaslpdvpadllkls 375
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI---LLQLGDLDE----AIVLLHE--------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 376 lkrrsdrqqflghmrgslltlqrLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 455
Cdd:COG4783    64 -----------------------ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                         170
                  ....*....|....
gi 1370512372 456 KIAESIPYLKEGIE 469
Cdd:COG4783   121 RPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 296-501 5.24e-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: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 296 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASlpdvPADLLKLS 375
Cdd:COG3914     5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAA----ALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 376 LKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 455
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370512372 456 KIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
Cdd:COG3914   161 RLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
386-501 1.24e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.33  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 386 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 465
Cdd:COG0457    21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370512372 466 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
Cdd:COG0457   101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 320-470 3.81e-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: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 320 LVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRL 399
Cdd:COG5010     1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370512372 400 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIES 470
Cdd:COG5010    81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 393-501 1.46e-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: 56.55  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 393 LLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgD 472
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1370512372 473 PgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 501
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 ...
 295-408 3.37e-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: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 295 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 366
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370512372 367 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 408
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 294-483 4.33e-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: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 294 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYgkaqcedDLAEKRRSNEVLRGAIETYQEVASL-PDVPADLL 372
Cdd:COG3914    78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 373 KLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILK 452
Cdd:COG3914   151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370512372 453 AQNKIAESIPYLKEGIESGDPGTDDGRFYFH 483
Cdd:COG3914   226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
400-501 5.98e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 5.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 400 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGR 479
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 1370512372 480 FYFHLGDAMQRVGN-KEAYKWYE 501
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 291-474 1.18e-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: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 291 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY--GKAQCED-DL--AEKrrsnEVLRGAIETYQEVASLP 365
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEK----ELRKALSLGYPKNQVLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 366 DvpadLLKLSLKRRSDrqqflghmrgslltlQRLVQLFPNDTSLKND--------LGVGYLLIGDNDNAKKVYEEVLSVT 437
Cdd:TIGR02917  95 L----LARAYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAID 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370512372 438 PNDGFAKVHYGFILKAQNKIAESIPYLKEgIESGDPG 474
Cdd:TIGR02917 156 PRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
417-501 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 1370512372 417 YLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 495
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 1370512372 496 AYKWYE 501
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 386-476 1.40e-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: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 386 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 465
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 1370512372 466 EGIESGDPGTD 476
Cdd:COG4235   110 KLLALLPADAP 120
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 303-405 1.60e-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: 50.38  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 303 KLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL----PDVPADLLKLS 375
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEA---YYALGD----YDEAAEAFEKLLKRypdsPKAPDALLKLG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1370512372 376 LkrrsdRQQFLGHMRGSLLTLQRLVQLFPN 405
Cdd:COG1729    75 L-----SYLELGDYDKARATLEELIKKYPD 99
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 294-480 1.71e-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: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 294 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAqceddLAEKRRSNevLRGAIETYQEVASL-PD-VPADL 371
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEyLPALL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 372 LK-LSLKRRSDRQQFLGHMRGSLL---------------------------TLQRLVQLFPNDTSLKNDLGVGYLLIGDN 423
Cdd:TIGR02917 300 LAgASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370512372 424 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRF 480
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
386-469 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 1370512372 386 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKvYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 465
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 1370512372 466 EGIE 469
Cdd:COG3063    84 RALE 87
rne PRK10811
ribonuclease E; Reviewed
 132-266 2.01e-05

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 48.11  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  132 PAVPPEEAEPHTEPEEQVpVEAEPQNIEDEAKEQIQSLLHE-------------MVHAEHETEHSYHVEETDS---SEPV 195
Cdd:PRK10811   846 PVVRPQDVQVEEQREAEE-VQVQPVVAEVPVAAAVEPVVSApvveavaevveepVVVAEPQPEEVVVVETTHPeviAAPV 924

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370512372  196 VEDERLHHDTDDVTYQVYEEQAvyEPLENEGIEITEVTAPPE--DNPVEDSQVIVEEVSIFPVEEQQEVPPET 266
Cdd:PRK10811   925 TEQPQVITESDVAVAQEVAEHA--EPVVEPQDETADIEEAAEtaEVVVAEPEVVAQPAAPVVAEVAAEVETVT 995
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 301-358 5.30e-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: 43.06  E-value: 5.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370512372 301 AEKLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCEDDLAEKRRSNEVLRGAIETY 358
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY 97
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 292-469 1.60e-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: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 292 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQ--SPR---ARYGKAQCEDDLAE---------KRRSNEVL------ 351
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQeiEPAlalAQYYLGKGQLKKALailneaadaAPDSPEAWlmlgra 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 352 -------RGAIETYQEVASL-PDVPADLLKLSlkrrsDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDN 423
Cdd:TIGR02917 611 qlaagdlNKAVSSFKKLLALqPDSALALLLLA-----DAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRT 685

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370512372 424 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIE 469
Cdd:TIGR02917 686 ESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
291-443 1.86e-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: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 291 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVlrgaietYQEVASLPDVPAD 370
Cdd:COG4785     3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370512372 371 LLKLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFA 443
Cdd:COG4785    76 YYERGVAYDS-----LGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 304-406 2.96e-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: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 304 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL-PDVPAdllklSLKRRSDR 382
Cdd:COG4783    48 LLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLdPEHPE-----AYLRLARA 115

                          90       100
                  ....*....|....*....|....
gi 1370512372 383 QQFLGHMRGSLLTLQRLVQLFPND 406
Cdd:COG4783   116 YRALGRPDEAIAALEKALELDPDD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 304-438 4.13e-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: 41.48  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 304 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQevaslpdvpadllklslkrrsdrq 383
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYE------------------------ 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370512372 384 qflghmrgslltlqRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTP 438
Cdd:COG5010   113 --------------KALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 298-362 5.25e-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: 5.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370512372 298 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 362
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAAL 61
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 311-410 6.80e-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: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 311 EEAVNAFKELVRKYPQSPRARYGKA---QCEDDLAEK---------RRSNEV-----LRGAIETYQEVASLPDVPADLLK 373
Cdd:COG4105   131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370512372 374 --LSLKRRSDRQQflghmrgsllTLQRLVQLFPNDTSLK 410
Cdd:COG4105   211 ayYALGRYDEAQD----------AAAVLGKNYPDSPYLK 239
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 291-405 7.71e-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: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 291 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQC---EDDLAEkrrsnevlrgAIETYQEVASL 364
Cdd:COG4105    29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370512372 365 ----PDVP-ADLLK-LS---LKRRSDRQQflGHMRGSLLTLQRLVQLFPN 405
Cdd:COG4105    99 ypnsPNADyAYYLRgLSyyeQSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 417-501 1.02e-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: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 417 YLLIGDNDNAKKVYEEVLSVTPNDGFA-KVHY--GFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN 493
Cdd:COG1729     3 LLKAGDYDEAIAAFKAFLKRYPNSPLApDALYwlGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGD 82


                  ....*....
gi 1370512372 494 KE-AYKWYE 501
Cdd:COG1729    83 YDkARATLE 91
rne PRK10811
ribonuclease E; Reviewed
 126-269 1.15e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.33  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372  126 ERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETDSSEPVVEDERlhHDT 205
Cdd:PRK10811   880 EPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQD--ETA 957

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370512372  206 DDVTYQVYEEQAVYEPlenegieitEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPETNRK 269
Cdd:PRK10811   958 DIEEAAETAEVVVAEP---------EVVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVE 1012
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 298-378 1.24e-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: 39.60  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 298 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL--PDVPADLLKLS 375
Cdd:COG4235    55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                  ...
gi 1370512372 376 LKR 378
Cdd:COG4235   128 IAE 130
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 301-440 3.00e-03

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.45  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 301 AEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIEtyqevaslpdvpadllklslkrrs 380
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEE----AEE------------------------ 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 381 drqqflghmrgsllTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPND 440
Cdd:COG4235    73 --------------LLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 296-360 3.97e-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: 3.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370512372 296 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQE 360
Cdd:COG4783    74 ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
338-501 4.03e-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: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 338 EDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGhmrgsLLTLQRLVQLFPNDTSLKNDLGVGY 417
Cdd:COG4785     9 LLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAAL-----AAERIDRALALPDLAQLYYERGVAY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370512372 418 LLIGDNDNAKKVYEEVLSVTPndGFAKVHY--GFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-K 494
Cdd:COG4785    84 DSLGDYDLAIADFDQALELDP--DLAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAYLNRGIALYYLGRyE 158


                  ....*..
gi 1370512372 495 EAYKWYE 501
Cdd:COG4785   159 LAIADLE 165
TPR_14 pfam13428
Tetratricopeptide repeat;
298-337 7.68e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 35.09  E-value: 7.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370512372 298 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQC 337
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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