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Conserved domains on  [gi|313870665|gb|ADR82217|]
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truncated trimeric autotransporter adhesin 10s [Actinobacillus pleuropneumoniae]

Protein Classification

ESPR and LbR-like domain-containing protein( domain architecture ID 10586158)

ESPR and LbR-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ESPR pfam13018
Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ...
 1-34 4.04e-12

Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N-terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). So far, the ESPR is present only in Gram-negative bacterial proteins originating from the classes Beta- and Gamma-proteobacteria. ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation. Deletion of ESPR causes mis-folding of the TAAs passenger domain in the periplasm, substantially impairing its translocation across the outer membrane.


:

Pssm-ID: 463773 [Multi-domain]  Cd Length: 50  Bit Score: 59.86  E-value: 4.04e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 313870665    1 MNKIFKVIWSHATQTFVVVSELTRSKSKAKASVS 34
Cdd:pfam13018   1 MNKIYRVIWNRARGAWVVVSELAKSKGKSSSSSS 34
LbR-like super family cl17507
Left-handed beta-roll, including virulence factors and various other proteins; This family ...
 138-230 1.05e-05

Left-handed beta-roll, including virulence factors and various other proteins; This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric beta-rolls of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. The ice-binding protein of the grass Lolium perenne (LpIBP) discourages the recrystallization of ice. Ice-binding proteins produced by organisms to prevent the growing of ice are termed to anti-freeze proteins. LpIBP consists of an unusual left-handed beta roll. Ice-binding is mediated by a flat beta-sheet on one side of the helix. These domains form a left handed beta roll made up of a series of short repeated elements.


The actual alignment was detected with superfamily member cd12820:

Pssm-ID: 248061 [Multi-domain]  Cd Length: 126  Bit Score: 44.02  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665 138 NTVALGTYAYAWGHDSVAIGTNSQAvhdVQTDNAEFNSRNSVNA-GAIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGN 216
Cdd:cd12820   15 NSTAFGYNNKASGDNSSAFGYGNKA---SGENSSAFGYNNKASGeNSTAFGYGNKASGENSSAFGSNNTASGNNSSAFGY 91

                         90
                 ....*....|....
gi 313870665 217 DSYAMGVGSVVIGG 230
Cdd:cd12820   92 NNTASGENSTAFGN 105
 
Name Accession Description Interval E-value
ESPR pfam13018
Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ...
 1-34 4.04e-12

Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N-terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). So far, the ESPR is present only in Gram-negative bacterial proteins originating from the classes Beta- and Gamma-proteobacteria. ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation. Deletion of ESPR causes mis-folding of the TAAs passenger domain in the periplasm, substantially impairing its translocation across the outer membrane.


Pssm-ID: 463773 [Multi-domain]  Cd Length: 50  Bit Score: 59.86  E-value: 4.04e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 313870665    1 MNKIFKVIWSHATQTFVVVSELTRSKSKAKASVS 34
Cdd:pfam13018   1 MNKIYRVIWNRARGAWVVVSELAKSKGKSSSSSS 34
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 138-230 1.05e-05

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 44.02  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665 138 NTVALGTYAYAWGHDSVAIGTNSQAvhdVQTDNAEFNSRNSVNA-GAIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGN 216
Cdd:cd12820   15 NSTAFGYNNKASGDNSSAFGYGNKA---SGENSSAFGYNNKASGeNSTAFGYGNKASGENSSAFGSNNTASGNNSSAFGY 91

                         90
                 ....*....|....
gi 313870665 217 DSYAMGVGSVVIGG 230
Cdd:cd12820   92 NNTASGENSTAFGN 105
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 1-240 1.39e-05

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 46.40  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665    1 MNKIFKVIWSHATQTFVVVSELTRSKSKAKAsvsdvKKNEVSSLITSGfklsaisalLISTIPTAYAAVS----IGKAeV 76
Cdd:NF033481    1 MNKVYKVIWNASIGAWVATSEIAKSKTKTKS-----KTLNVSAAVLSG---------VICFAPNAFAGTNteggIGQG-T 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665   77 EKDNKYIVSQGTAANHGQNAIVIGeyAGNQRADDYISDAPNENekklNAYNKqkvsgndlsntvALGTYAYAWGHD-SVA 155
Cdd:NF033481   66 SISGTTSCREGSANTANQKDIAIG--CGAQTQDRTGSNIANRN----NPYNN------------STGAYAGAMKQGgAIS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665  156 IGTNSQAVHDVQTDNAEFNSRNSVNAgaIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGNDSYAMGVGSVVIGGDDSGY 235
Cdd:NF033481  128 VGTGAVVEKGLGTAIGSYATTQGISG--VAIGTGALSSGNTALAVGRQSAATADFSQAIGNVAAATGKGSLAIGHSATAE 205


                  ....*
gi 313870665  236 AYESI 240
Cdd:NF033481  206 GYRSI 210
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 138-232 5.44e-05

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 44.86  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665  138 NTVALGTYAYAWGHDSVAIGTNSQAVHDVQTdnAEFNSRNSVNAGAIAIGFQAIARG------DQTVSLGSRAAAYNRQA 211
Cdd:NF033481  400 NAIAVGVNASAAGREAMAIGGSAQAIGSGAI--AMGSSSQTVGRGDVAIGRNASTQGaegvnsNQSVAIGDQTKAIGDQS 477

                          90       100
                  ....*....|....*....|.
gi 313870665  212 TAIGNDSYAMGVGSVVIGGDD 232
Cdd:NF033481  478 VAIGADVIAKGNSSVAIGGDD 498
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 141-230 3.92e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 38.69  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665  141 ALGTYAYAWGHDSVAIGTNSQAVhdvQTDNAEFNSRNSVNAGAIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGNDSYA 220
Cdd:NF033481  585 ATGDGASAMGINSLASGTNSTAI---GSGNKPGEGAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKA 661

                          90
                  ....*....|
gi 313870665  221 MGVGSVVIGG 230
Cdd:NF033481  662 TGKNAAAIGG 671
 
Name Accession Description Interval E-value
ESPR pfam13018
Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for ...
 1-34 4.04e-12

Extended Signal Peptide of Type V secretion system; This conserved domain is called ESPR for Extended Signal Peptide Region. It is present at the N-terminus of the signal peptides of proteins belonging to the Type V secretion systems, including the autotransporters (T5aSS), TpsA exoproteins of the two-partner system (T5bSS) and trimeric autotransporters (TAAs). So far, the ESPR is present only in Gram-negative bacterial proteins originating from the classes Beta- and Gamma-proteobacteria. ESPR severely impairs inner membrane translocation, suggesting that it adopts a particular conformation or it interacts with a cytoplasmic or inner membrane co-factor, prior to exportation. Deletion of ESPR causes mis-folding of the TAAs passenger domain in the periplasm, substantially impairing its translocation across the outer membrane.


Pssm-ID: 463773 [Multi-domain]  Cd Length: 50  Bit Score: 59.86  E-value: 4.04e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 313870665    1 MNKIFKVIWSHATQTFVVVSELTRSKSKAKASVS 34
Cdd:pfam13018   1 MNKIYRVIWNRARGAWVVVSELAKSKGKSSSSSS 34
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 138-230 1.05e-05

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 44.02  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665 138 NTVALGTYAYAWGHDSVAIGTNSQAvhdVQTDNAEFNSRNSVNA-GAIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGN 216
Cdd:cd12820   15 NSTAFGYNNKASGDNSSAFGYGNKA---SGENSSAFGYNNKASGeNSTAFGYGNKASGENSSAFGSNNTASGNNSSAFGY 91

                         90
                 ....*....|....
gi 313870665 217 DSYAMGVGSVVIGG 230
Cdd:cd12820   92 NNTASGENSTAFGN 105
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 1-240 1.39e-05

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 46.40  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665    1 MNKIFKVIWSHATQTFVVVSELTRSKSKAKAsvsdvKKNEVSSLITSGfklsaisalLISTIPTAYAAVS----IGKAeV 76
Cdd:NF033481    1 MNKVYKVIWNASIGAWVATSEIAKSKTKTKS-----KTLNVSAAVLSG---------VICFAPNAFAGTNteggIGQG-T 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665   77 EKDNKYIVSQGTAANHGQNAIVIGeyAGNQRADDYISDAPNENekklNAYNKqkvsgndlsntvALGTYAYAWGHD-SVA 155
Cdd:NF033481   66 SISGTTSCREGSANTANQKDIAIG--CGAQTQDRTGSNIANRN----NPYNN------------STGAYAGAMKQGgAIS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665  156 IGTNSQAVHDVQTDNAEFNSRNSVNAgaIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGNDSYAMGVGSVVIGGDDSGY 235
Cdd:NF033481  128 VGTGAVVEKGLGTAIGSYATTQGISG--VAIGTGALSSGNTALAVGRQSAATADFSQAIGNVAAATGKGSLAIGHSATAE 205


                  ....*
gi 313870665  236 AYESI 240
Cdd:NF033481  206 GYRSI 210
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 138-232 5.44e-05

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 44.86  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665  138 NTVALGTYAYAWGHDSVAIGTNSQAVHDVQTdnAEFNSRNSVNAGAIAIGFQAIARG------DQTVSLGSRAAAYNRQA 211
Cdd:NF033481  400 NAIAVGVNASAAGREAMAIGGSAQAIGSGAI--AMGSSSQTVGRGDVAIGRNASTQGaegvnsNQSVAIGDQTKAIGDQS 477

                          90       100
                  ....*....|....*....|.
gi 313870665  212 TAIGNDSYAMGVGSVVIGGDD 232
Cdd:NF033481  478 VAIGADVIAKGNSSVAIGGDD 498
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 137-230 1.85e-04

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 40.56  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665 137 SNTVALGTYAYAWGHDSVAIGTNSQAvhdvQTDNA-EFNSRNSVNA-GAIAIGFQAIARGDQTVSLGSRAAAYNRQATAI 214
Cdd:cd12820   28 DNSSAFGYGNKASGENSSAFGYNNKA----SGENStAFGYGNKASGeNSSAFGSNNTASGNNSSAFGYNNTASGENSTAF 103

                         90       100
                 ....*....|....*....|...
gi 313870665 215 GN-------DSYAMGVGSVVIGG 230
Cdd:cd12820  104 GNnskasgeNSTALGNGNKASGN 126
LbR_YadA-like cd12820
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
 152-265 1.09e-03

YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.


Pssm-ID: 240612 [Multi-domain]  Cd Length: 126  Bit Score: 38.25  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665 152 DSVAIGTNSQAvhdvqtdnaefNSRNSvnagaIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGNDSYAMGVGSVVIGGD 231
Cdd:cd12820    1 NSTAIGYNNKA-----------SGENS-----TAFGYNNKASGDNSSAFGYGNKASGENSSAFGYNNKASGENSTAFGYG 64

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 313870665 232 DSGYAYESI-NGKDKRPWANNAGNLGYTNLATGFN 265
Cdd:cd12820   65 NKASGENSSaFGSNNTASGNNSSAFGYNNTASGEN 99
auto_Ata NF033481
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
 141-230 3.92e-03

trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.


Pssm-ID: 411124 [Multi-domain]  Cd Length: 1862  Bit Score: 38.69  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313870665  141 ALGTYAYAWGHDSVAIGTNSQAVhdvQTDNAEFNSRNSVNAGAIAIGFQAIARGDQTVSLGSRAAAYNRQATAIGNDSYA 220
Cdd:NF033481  585 ATGDGASAMGINSLASGTNSTAI---GSGNKPGEGAKATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKA 661

                          90
                  ....*....|
gi 313870665  221 MGVGSVVIGG 230
Cdd:NF033481  662 TGKNAAAIGG 671
 
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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