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Conserved domains on  [gi|1622960536|ref|XP_001090590|]
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aspartyl/asparaginyl beta-hydroxylase isoform X14 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 562-716 2.11e-74

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


:

Pssm-ID: 461552  Cd Length: 157  Bit Score: 237.55  E-value: 2.11e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 562 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 638
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960536 639 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 716
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 ...
 14-79 5.58e-26

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: 101.07  E-value: 5.58e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960536  14 NGRKGGPSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLG 79
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-519 3.06e-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: 82.47  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 304 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLP 383
Cdd:COG2956    34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 384 DVPADllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 463
Cdd:COG2956   107 PDDAE----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960536 464 HYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 562-716 2.11e-74

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 237.55  E-value: 2.11e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 562 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 638
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960536 639 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 716
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 558-723 6.36e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 190.47  E-value: 6.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 558 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 632
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 633 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLI 708
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 1622960536 709 FIVDVWHPELTPQQR 723
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 14-79 5.58e-26

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: 101.07  E-value: 5.58e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960536  14 NGRKGGPSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLG 79
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-519 3.06e-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: 82.47  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 304 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLP 383
Cdd:COG2956    34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 384 DVPADllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 463
Cdd:COG2956   107 PDDAE----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960536 464 HYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 313-426 3.32e-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: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 313 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 384
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622960536 385 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 426
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 316-380 5.18e-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: 5.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960536 316 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 380
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 ...
 562-716 2.11e-74

Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.


Pssm-ID: 461552  Cd Length: 157  Bit Score: 237.55  E-value: 2.11e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 562 ERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGD--WSQFTLWQQGRRNENACKGAPKTCTLLEKFP-ETTGCRRGQIKY 638
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960536 639 SIMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHP 716
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 558-723 6.36e-56

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 190.47  E-value: 6.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 558 VKSLERNWKLIRDEGLAVMDKAKGL-----FLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPettgcr 632
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 633 rgQIK---YSIMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLI 708
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 1622960536 709 FIVDVWHPELTPQQR 723
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 14-79 5.58e-26

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: 101.07  E-value: 5.58e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960536  14 NGRKGGPSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLG 79
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLG 66
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-519 3.06e-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: 82.47  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 304 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQceDDLAEKRrsnevLRGAIETYQEVASLP 383
Cdd:COG2956    34 ALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQ--DYLKAGL-----LDRAEELLEKLLELD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 384 DVPADllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 463
Cdd:COG2956   107 PDDAE----ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALL 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960536 464 HYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG2956   183 LLAELYLEQGDYEEAIAALERALEQ-DP--DYLPALPRLAELYEKLGDpEEALELLR 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
322-487 1.24e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 71.19  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 322 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL-PDVPAdllklSLKRRSDR 400
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLA---YLRLGRYEE----ALADYEQALELdPDDAE-----ALNNLGLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 401 QQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIP 480
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                  ....*..
gi 1622960536 481 YLKEGIE 487
Cdd:COG0457   166 LLEKLEA 172
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 318-519 3.05e-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: 70.53  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 318 AAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEddlaekRRSNEVLRgAIETYQEVASL-PDVPADLLKLSLkr 396
Cdd:COG2956    14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLY------RRRGEYDR-AIRIHQKLLERdPDRAEALLELAQ-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 397 rsDRQQfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIA 476
Cdd:COG2956    85 --DYLK-AGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622960536 477 ESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG2956   162 EAIEALEKALKL-DP--DCARALLLLAELYLEQGDyEEAIAALE 202
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 304-519 1.00e-11

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 66.29  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 304 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASLP 383
Cdd:COG2956    68 LLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEI---YEQEGDWEK----AIEVLERLLKLG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 384 DVPADLLKlslkRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKV 463
Cdd:COG2956   141 PENAHAYC----ELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALP 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622960536 464 HYGFILKAQNKIAESIPYLKEGIESgDPGTDDGRFYFHLgdAMQRVGNKEAYKWYE 519
Cdd:COG2956   217 RLAELYEKLGDPEEALELLRKALEL-DPSDDLLLALADL--LERKEGLEAALALLE 269
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 314-487 1.68e-11

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 62.52  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 314 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEvaslpdvpadllkls 393
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEI---LLQLGDLDE----AIVLLHE--------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 394 lkrrsdrqqflghmrgslltlqrLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 473
Cdd:COG4783    64 -----------------------ALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALG 120

                         170
                  ....*....|....
gi 1622960536 474 KIAESIPYLKEGIE 487
Cdd:COG4783   121 RPDEAIAALEKALE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
404-519 4.93e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.49  E-value: 4.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 404 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 483
Cdd:COG0457    21 LGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622960536 484 EGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG0457   101 KALEL-DP--DDAEALYNLGLALLELGRyDEAIEAYE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 314-519 5.14e-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: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 314 AELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASlpdvPADLLKLS 393
Cdd:COG3914     5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAA----ALLLLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 394 LKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQN 473
Cdd:COG3914    81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622960536 474 KIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG3914   161 RLEEAIAALRRALEL-DP--DNAEALNNLGNALQDLGRlEEAIAAYR 204
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 338-488 2.05e-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: 59.97  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 338 LVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRL 417
Cdd:COG5010     1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960536 418 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIES 488
Cdd:COG5010    81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 411-519 1.13e-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: 56.94  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 411 LLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgD 490
Cdd:COG4235     3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL-D 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622960536 491 PgtDDGRFYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG4235    82 P--DNPEALYLLGLAAFQQGDyAEAIAAWQ 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
418-519 2.51e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 418 VQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGR 497
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL-DP--DDAE 77

                          90       100
                  ....*....|....*....|...
gi 1622960536 498 FYFHLGDAMQRVGN-KEAYKWYE 519
Cdd:COG0457    78 ALNNLGLALQALGRyEEALEDYD 100
tol_pal_ybgF TIGR02795
tol-pal system protein YbgF; Members of this protein family are the product of one of seven ...
 313-426 3.32e-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: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 313 KAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPR---ARY--GKAQceddLAEKRrsnevLRGAIETYQEV-ASLPD-- 384
Cdd:TIGR02795   1 EAYYDAALLVLKAGDYADAIQAFQAFLKKYPKSTYapnAHYwlGEAY----YAQGD-----YADAAKAFLAVvKKYPKsp 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622960536 385 -VPADLLKLSLKrrsdrQQFLGHMRGSLLTLQRLVQLFPNDTS 426
Cdd:TIGR02795  72 kAPDALLKLGMS-----LQELGDKEKAKATLQQVIKRYPGSSA 109
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 312-501 4.25e-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: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 312 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYgkaqcedDLAEKRRSNEVLRGAIETYQEVASL-PDVPADLL 390
Cdd:COG3914    78 AALLELAALLLQALGRYEEALALYRRALALNPDNAEALF-------NLGNLLLALGRLEEALAALRRALALnPDFAEAYL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 391 KLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILK 470
Cdd:COG3914   151 NLGEALRR-----LGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622960536 471 AQNKIAESIPYLKEGIESGDPGTDDGRFYFH 501
Cdd:COG3914   226 QACDWEVYDRFEELLAALARGPSELSPFALL 256
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 321-423 5.22e-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: 51.53  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 321 KLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL----PDVPADLLKLS 393
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSplaPDALYWLGEA---YYALGD----YDEAAEAFEKLLKRypdsPKAPDALLKLG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622960536 394 LkrrsdRQQFLGHMRGSLLTLQRLVQLFPN 423
Cdd:COG1729    75 L-----SYLELGDYDKARATLEELIKKYPD 99
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
435-519 5.77e-08

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 50.94  E-value: 5.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 435 YLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYlKEGIESgDPgtDDGRFYFHLGDAMQRVGN-KE 513
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAEALLNLAELLLELGDyDE 77


                  ....*.
gi 1622960536 514 AYKWYE 519
Cdd:COG3063    78 ALAYLE 83
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 404-494 1.16e-07

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.16  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 404 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 483
Cdd:COG4235    30 LGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQ 109

                          90
                  ....*....|.
gi 1622960536 484 EGIESGDPGTD 494
Cdd:COG4235   110 KLLALLPADAP 120
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 309-492 1.16e-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: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 309 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARY--GKAQCED-DL--AEKrrsnEVLRGAIETYQEVASLP 383
Cdd:TIGR02917  19 DQSPEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFllGKIYLALgDYaaAEK----ELRKALSLGYPKNQVLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 384 DvpadLLKLSLKRRSDrqqflghmrgslltlQRLVQLFPNDTSLKND--------LGVGYLLIGDNDNAKKVYEEVLSVT 455
Cdd:TIGR02917  95 L----LARAYLLQGKF---------------QQVLDELPGKTLLDDEgaaellalRGLAYLGLGQLELAQKSYEQALAID 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622960536 456 PNDGFAKVHYGFILKAQNKIAESIPYLKEgIESGDPG 492
Cdd:TIGR02917 156 PRSLYAKLGLAQLALAENRFDEARALIDE-VLTADPG 191
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 312-498 1.68e-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: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 312 IKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAqceddLAEKRRSNevLRGAIETYQEVASL-PD-VPADL 389
Cdd:TIGR02917 227 IAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKA-----LVDFQKKN--YEDARETLQDALKSaPEyLPALL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 390 LK-LSLKRRSDRQQFLGHMRGSLL---------------------------TLQRLVQLFPNDTSLKNDLGVGYLLIGDN 441
Cdd:TIGR02917 300 LAgASEYQLGNLEQAYQYLNQILKyapnshqarrllasiqlrlgrvdeaiaTLSPALGLDPDDPAALSLLGEAYLALGDF 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622960536 442 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRF 498
Cdd:TIGR02917 380 EKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL 436
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
404-487 2.01e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 46.70  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 404 LGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKvYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLK 483
Cdd:COG3063     5 LGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLE 83


                  ....
gi 1622960536 484 EGIE 487
Cdd:COG3063    84 RALE 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 319-376 2.84e-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: 43.83  E-value: 2.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622960536 319 AEKLRKRGKIEEAVNAFKELVRKYPQS---PRARYGKAQCEDDLAEKRRSNEVLRGAIETY 376
Cdd:COG1729    37 GEAYYALGDYDEAAEAFEKLLKRYPDSpkaPDALLKLGLSYLELGDYDKARATLEELIKKY 97
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 304-424 1.36e-04

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.49  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 304 LLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIETYQEVASL- 382
Cdd:COG4783    30 ALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA---LLKAGDYDE----ALALLEKALKLd 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622960536 383 PDVPAdllklSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPND 424
Cdd:COG4783   103 PEHPE-----AYLRLARAYRALGRPDEAIAALEKALELDPDD 139
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 310-487 1.58e-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: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 310 KTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQ--SPR---ARYGKAQCEDDLAE---------KRRSNEVL------ 369
Cdd:TIGR02917 531 KNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQeiEPAlalAQYYLGKGQLKKALailneaadaAPDSPEAWlmlgra 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 370 -------RGAIETYQEVASL-PDVPADLLKLSlkrrsDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDN 441
Cdd:TIGR02917 611 qlaagdlNKAVSSFKKLLALqPDSALALLLLA-----DAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRT 685

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622960536 442 DNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIE 487
Cdd:TIGR02917 686 ESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALK 731
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
309-461 1.83e-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: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 309 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVlrgaietYQEVASLPDVPAD 388
Cdd:COG4785     3 ALALALLLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAALAAER-------IDRALALPDLAQL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622960536 389 LLKLSLKRRSdrqqfLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFA 461
Cdd:COG4785    76 YYERGVAYDS-----LGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 322-456 1.89e-04

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.64  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 322 LRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQevaslpdvpadllklslkrrsdrq 401
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALL---YSRSGD----KDEAKEYYE------------------------ 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622960536 402 qflghmrgslltlqRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTP 456
Cdd:COG5010   113 --------------KALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 435-519 5.05e-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: 40.36  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 435 YLLIGDNDNAKKVYEEVLSVTPNDGFA-KVHY--GFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN 511
Cdd:COG1729     3 LLKAGDYDEAIAAFKAFLKRYPNSPLApDALYwlGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGD 82


                  ....*....
gi 1622960536 512 KE-AYKWYE 519
Cdd:COG1729    83 YDkARATLE 91
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 316-380 5.18e-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: 5.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622960536 316 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQCeddLAEKRRsnevLRGAIETYQEVA 380
Cdd:pfam13432   1 LALARAALRAGDYDDAAAALEAALARFPESPdaaAALLLLGLA---ALRQGR----LAEAAAAYRAAL 61
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 329-428 5.21e-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: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 329 EEAVNAFKELVRKYPQSPRARYGKA---QCEDDLAEK---------RRSNEV-----LRGAIETYQEVASLPDVPADLLK 391
Cdd:COG4105   131 RKAIEAFQELINRYPDSEYAEDAKKridELRDKLARKelevaryylKRGAYVaainrFQNVLEDYPDTPAVEEALYLLVE 210

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622960536 392 --LSLKRRSDRQQflghmrgsllTLQRLVQLFPNDTSLK 428
Cdd:COG4105   211 ayYALGRYDEAQD----------AAAVLGKNYPDSPYLK 239
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 309-423 5.75e-04

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 42.18  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 309 DKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSP---RARYGKAQC---EDDLAEkrrsnevlrgAIETYQEVASL 382
Cdd:COG4105    29 SWDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPyaeQAQLMLAYAyykQGDYEE----------AIAAADRFIKL 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622960536 383 ----PDVP-ADLLK-LS---LKRRSDRQQflGHMRGSLLTLQRLVQLFPN 423
Cdd:COG4105    99 ypnsPNADyAYYLRgLSyyeQSPDSDRDQ--TSTRKAIEAFQELINRYPD 146
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 316-396 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 316 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRsnevLRGAIETYQEVASL--PDVPADLLKLS 393
Cdd:COG4235    55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA---AFQQGD----YAEAIAAWQKLLALlpADAPARLLEAS 127


                  ...
gi 1622960536 394 LKR 396
Cdd:COG4235   128 IAE 130
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 304-354 1.54e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 38.82  E-value: 1.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622960536 304 LLNKFDKTIKAE---LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQ 354
Cdd:COG1729    56 LLKRYPDSPKAPdalLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 319-458 2.42e-03

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.83  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 319 AEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCeddLAEKRRSNEvlrgAIEtyqevaslpdvpadllklslkrrs 398
Cdd:COG4235    24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA---LLAAGDTEE----AEE------------------------ 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 399 drqqflghmrgsllTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPND 458
Cdd:COG4235    73 --------------LLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
356-519 3.97e-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: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 356 EDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGhmrgsLLTLQRLVQLFPNDTSLKNDLGVGY 435
Cdd:COG4785     9 LLALALAAAAASKAAILLAALLFAAVLALAIALADLALALAAAALAAAAL-----AAERIDRALALPDLAQLYYERGVAY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622960536 436 LLIGDNDNAKKVYEEVLSVTPndGFAKVHY--GFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDAMQRVGN-K 512
Cdd:COG4785    84 DSLGDYDLAIADFDQALELDP--DLAEAYNnrGLAYLLLGDYDAALEDFDRALEL-DP--DYAYAYLNRGIALYYLGRyE 158


                  ....*..
gi 1622960536 513 EAYKWYE 519
Cdd:COG4785   159 LAIADLE 165
TPR_14 pfam13428
Tetratricopeptide repeat;
316-355 5.64e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 35.48  E-value: 5.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622960536 316 LDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQC 355
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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