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Conserved domains on  [gi|2451137990|ref|XP_024427768|]
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aspartyl/asparaginyl beta-hydroxylase isoform X9 [Desmodus rotundus]

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 ...
 509-663 3.32e-73

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


:

Pssm-ID: 461552  Cd Length: 157  Bit Score: 232.92  E-value: 3.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 509 ERNWKLIRDEGVAVMDKTKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCSLLDKFP-ETTGCRRGQIKY 585
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2451137990 586 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKSWEEGKVLIFDDSFEHEVWQDATSLRLIFIVDVWHP 663
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 ...
 51-131 3.76e-22

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: 90.29  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990  51 NGKKGVLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLL 130
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2451137990 131 G 131
Cdd:pfam05279  66 G 66
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 357-466 2.71e-10

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: 58.66  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 357 AELDAAEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKAQV-----------------LNVTPNDGFAKVHYGFILKAQ 419
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEIllqlgdldeaivllheaLELDPDEPEARLNLGLALLKA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2451137990 420 NKIAESIPYLKEGIESgDPgtDDGRFYFHLGDALQRVG-SKEAYTWYE 466
Cdd:COG4783    86 GDYDEALALLEKALKL-DP--EHPEAYLRLARAYRALGrPDEAIAALE 130
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 509-663 3.32e-73

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


Pssm-ID: 461552  Cd Length: 157  Bit Score: 232.92  E-value: 3.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 509 ERNWKLIRDEGVAVMDKTKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCSLLDKFP-ETTGCRRGQIKY 585
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2451137990 586 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKSWEEGKVLIFDDSFEHEVWQDATSLRLIFIVDVWHP 663
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 505-670 2.70e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 187.78  E-value: 2.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 505 VKSLERNWKLIRDEGVAVMDKTKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCSLLDKFPettgcr 579
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 580 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKSWEEGKVLIFDDSFEHEVWQDATSLRLI 655
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2451137990 656 FIVDVWHPELTPQQR 670
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 51-131 3.76e-22

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: 90.29  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990  51 NGKKGVLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLL 130
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2451137990 131 G 131
Cdd:pfam05279  66 G 66
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 357-466 2.71e-10

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: 58.66  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 357 AELDAAEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKAQV-----------------LNVTPNDGFAKVHYGFILKAQ 419
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEIllqlgdldeaivllheaLELDPDEPEARLNLGLALLKA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2451137990 420 NKIAESIPYLKEGIESgDPgtDDGRFYFHLGDALQRVG-SKEAYTWYE 466
Cdd:COG4783    86 GDYDEALALLEKALKL-DP--EHPEAYLRLARAYRALGrPDEAIAALE 130
TPR_6 pfam13174
Tetratricopeptide repeat;
357-388 1.23e-03

Tetratricopeptide repeat;


Pssm-ID: 463800 [Multi-domain]  Cd Length: 33  Bit Score: 36.68  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2451137990 357 AELDAAEKLRKRGKTEEAKTVFEELIRKYPQS 388
Cdd:pfam13174   2 ALLKLALAYLELGDTDEAKEALERLIKKYPDS 33
 
Name Accession Description Interval E-value
Asp_Arg_Hydrox pfam05118
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
 509-663 3.32e-73

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


Pssm-ID: 461552  Cd Length: 157  Bit Score: 232.92  E-value: 3.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 509 ERNWKLIRDEGVAVMDKTKGLFLPEDENLREKGD--WSQFTLWQQGRKNENACKGAPKTCSLLDKFP-ETTGCRRGQIKY 585
Cdd:pfam05118   1 EANWQVIRDELLALLKQEEGLPPYEEEALDDFGDigWKTFYLYAYGARLPENCALCPKTAALLEQPGvKASGCPRGQAMF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2451137990 586 SVMHPGTHVWPHTGPTNCRLRMHLGLVIPkEGCKIRCANETKSWEEGKVLIFDDSFEHEVWQDATSLRLIFIVDVWHP 663
Cdd:pfam05118  81 SRLQPGTHIPPHRGPTNGRLRCHLGLVVP-PGCRIRVGGETRTWREGECLLFDDSFEHEAWNETDEPRVVLLVDVWRP 157
LpxO2 COG3555
Aspartyl/asparaginyl beta-hydroxylase, cupin superfamily [Posttranslational modification, ...
 505-670 2.70e-55

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


Pssm-ID: 442776  Cd Length: 220  Bit Score: 187.78  E-value: 2.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 505 VKSLERNWKLIRDEGVAVMDKTKGL-----FLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCSLLDKFPettgcr 579
Cdd:COG3555    20 LAELEANWPTIRAELLALLAEIEALppyhdISFDQANIFFDRGWKRFYLYWYGERHPSNCALCPKTAALLEQIP------ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 580 rgQIK---YSVMHPGTHVWPHTGPTNCRLRMHLGLVIP-KEGCKIRCANETKSWEEGKVLIFDDSFEHEVWQDATSLRLI 655
Cdd:COG3555    94 --GVKaamFSILPPGKHIPPHRGPYNGRLRYHLGLIVPnDDRCRIRVDGETYSWREGEAVLFDDTYEHEAWNDTDETRVV 171

                         170
                  ....*....|....*
gi 2451137990 656 FIVDVWHPELTPQQR 670
Cdd:COG3555   172 LFCDVWRPMLSPWER 186
Asp-B-Hydro_N pfam05279
Aspartyl beta-hydroxylase N-terminal region; This family includes the N-terminal regions of ...
 51-131 3.76e-22

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: 90.29  E-value: 3.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990  51 NGKKGVLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLakakdfrynlsevlqGKLGVYDADGDGDFDVDDAKVLL 130
Cdd:pfam05279   1 NGRKGGLSGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVL---------------GKLGVYDADGDGDFDVDDAKVLL 65


                  .
gi 2451137990 131 G 131
Cdd:pfam05279  66 G 66
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 357-466 2.71e-10

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: 58.66  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 357 AELDAAEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKAQV-----------------LNVTPNDGFAKVHYGFILKAQ 419
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEIllqlgdldeaivllheaLELDPDEPEARLNLGLALLKA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2451137990 420 NKIAESIPYLKEGIESgDPgtDDGRFYFHLGDALQRVG-SKEAYTWYE 466
Cdd:COG4783    86 GDYDEALALLEKALKL-DP--EHPEAYLRLARAYRALGrPDEAIAALE 130
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
365-466 6.02e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.16  E-value: 6.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 365 LRKRGKTEEAKTVFEELIRKYPQSPRA------------RYGKA-----QVLNVTPNDGFAKVHYGFILKAQNKIAESIP 427
Cdd:COG0457    18 YRRLGRYEEAIEDYEKALELDPDDAEAlynlglaylrlgRYEEAladyeQALELDPDDAEALNNLGLALQALGRYEEALE 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2451137990 428 YLKEGIESgDPgtDDGRFYFHLGDALQRVG-SKEAYTWYE 466
Cdd:COG0457    98 DYDKALEL-DP--DDAEALYNLGLALLELGrYDEAIEAYE 134
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 353-461 2.08e-05

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: 46.65  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 353 KTIKAELDAAEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKAQ-----------------VLNVTPNDGFAKVHYGFI 415
Cdd:COG2956    40 ETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQdylkaglldraeellekLLELDPDDAEALRLLAEI 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2451137990 416 LKAQNKIAESIPYLKEGIESGDpgtDDGRFYFHLGDALQRVGSKEA 461
Cdd:COG2956   120 YEQEGDWEKAIEVLERLLKLGP---ENAHAYCELAELYLEQGDYDE 162
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 364-466 1.39e-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: 41.90  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 364 KLRKRGKTEEAKTVFEELIRKYPQSPRARYgkaqvlnvtpndgfAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDG 443
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPLAPD--------------ALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAP 67

                          90       100
                  ....*....|....*....|....
gi 2451137990 444 RFYFHLGDALQRVGSKE-AYTWYE 466
Cdd:COG1729    68 DALLKLGLSYLELGDYDkARATLE 91
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 309-466 2.33e-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: 42.25  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 309 LEEVHAPPAEEQQEIPPETDRKTDDPEQKEKVKKKKPKLLNKFDKTIKAELDAAekLRKRGKTEEAKTVFEELIRKYPQS 388
Cdd:COG5010    10 LPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNL--YNKLGDFEESLALLEQALQLDPNN 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2451137990 389 PRARYgkaqvlnvtpndgfakvHYGFILKAQNKIAESIPYLKEGIESgDPgtDDGRFYFHLGDALQRVG-SKEAYTWYE 466
Cdd:COG5010    88 PELYY-----------------NLALLYSRSGDKDEAKEYYEKALAL-SP--DNPNAYSNLAALLLSLGqDDEAKAALQ 146
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 362-466 3.98e-04

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.79  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 362 AEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKA-----------------QVLNVTPNDGFAKVHYGFILKAQNKIAE 424
Cdd:COG2956   151 AELYLEQGDYDEAIEALEKALKLDPDCARALLLLAelyleqgdyeeaiaaleRALEQDPDYLPALPRLAELYEKLGDPEE 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2451137990 425 SIPYLKEGIESgDPGTDDGRFYFHLgdALQRVGSKEAYTWYE 466
Cdd:COG2956   231 ALELLRKALEL-DPSDDLLLALADL--LERKEGLEAALALLE 269
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 352-397 6.16e-04

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 39.97  E-value: 6.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2451137990 352 DKTIKAELDAAEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKAQ 397
Cdd:COG1729    64 PKAPDALLKLGLSYLELGDYDKARATLEELIKKYPDSEAAKEARAR 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
351-484 6.38e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.92  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 351 FDKTIKAELDAAEKL-------RKRGKTEEAKTVFEELIRKYPQSPRARYgkaqvlnvtpndgfakvHYGFILKAQNKIA 423
Cdd:COG0457    65 YEQALELDPDDAEALnnlglalQALGRYEEALEDYDKALELDPDDAEALY-----------------NLGLALLELGRYD 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2451137990 424 ESIPYLKEGIESgDPgtDDGRFYFHLGDALQRVG-SKEAYTWYELGHKRGHFASVWQRSLYN 484
Cdd:COG0457   128 EAIEAYERALEL-DP--DDADALYNLGIALEKLGrYEEALELLEKLEAAALAALLAAALGEA 186
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
365-466 9.95e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.00  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2451137990 365 LRKRGKTEEAKTVFEELIRKYPQSPRARYgkaqvlnvtpndgfakvHYGFILKAQNKIAESIPYlKEGIESgDPgtDDGR 444
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALN-----------------NLGLLLLEQGRYDEAIAL-EKALKL-DP--NNAE 60

                          90       100
                  ....*....|....*....|...
gi 2451137990 445 FYFHLGDALQRVG-SKEAYTWYE 466
Cdd:COG3063    61 ALLNLAELLLELGdYDEALAYLE 83
TPR_6 pfam13174
Tetratricopeptide repeat;
357-388 1.23e-03

Tetratricopeptide repeat;


Pssm-ID: 463800 [Multi-domain]  Cd Length: 33  Bit Score: 36.68  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2451137990 357 AELDAAEKLRKRGKTEEAKTVFEELIRKYPQS 388
Cdd:pfam13174   2 ALLKLALAYLELGDTDEAKEALERLIKKYPDS 33
TPR_14 pfam13428
Tetratricopeptide repeat;
359-398 1.29e-03

Tetratricopeptide repeat;


Pssm-ID: 463874 [Multi-domain]  Cd Length: 44  Bit Score: 37.02  E-value: 1.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2451137990 359 LDAAEKLRKRGKTEEAKTVFEELIRKYPQSPRARYGKAQV 398
Cdd:pfam13428   5 LALARALLALGDPDEALALLERALALDPDDPEAWLALAQL 44
ATG27 pfam09451
Autophagy-related protein 27;
42-74 6.47e-03

Autophagy-related protein 27;


Pssm-ID: 430622  Cd Length: 261  Bit Score: 38.85  E-value: 6.47e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2451137990  42 RDTKHGGHKNGKKGVLSGSSFFTWFMVIALLGV 74
Cdd:pfam09451 174 KDESDPDDGDGGGNGGSGWGWFTWFFIILFLFT 206
 
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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