Retinoic acid induced 16-like protein; This is the conserved N-terminal 450 residues of a ...
101-452
2.62e-139
Retinoic acid induced 16-like protein; This is the conserved N-terminal 450 residues of a family of proteins described as retinoic acid-induced protein 16-like proteins. The exact function is not known. The proteins are found from worms to humans.
:
Pssm-ID: 370927 Cd Length: 357 Bit Score: 422.89 E-value: 2.62e-139
Family of unknown function (DUF5917); This short presumed domain is found close to the ...
698-791
1.18e-23
Family of unknown function (DUF5917); This short presumed domain is found close to the C-terminus of FHIP proteins, FAM160B proteins and UPF0518 family proteins.
:
Pssm-ID: 466037 Cd Length: 94 Bit Score: 96.10 E-value: 1.18e-23
KELAA motif; This short motif is found at the C-terminus of FHIP proteins, FAM160B proteins ...
1012-1043
3.23e-09
KELAA motif; This short motif is found at the C-terminus of FHIP proteins, FAM160B proteins and UPF0518 family proteins. It has a conserved KELAA sequence for which it is named.
:
Pssm-ID: 466035 Cd Length: 32 Bit Score: 52.88 E-value: 3.23e-09
Retinoic acid induced 16-like protein; This is the conserved N-terminal 450 residues of a ...
101-452
2.62e-139
Retinoic acid induced 16-like protein; This is the conserved N-terminal 450 residues of a family of proteins described as retinoic acid-induced protein 16-like proteins. The exact function is not known. The proteins are found from worms to humans.
Pssm-ID: 370927 Cd Length: 357 Bit Score: 422.89 E-value: 2.62e-139
Family of unknown function (DUF5917); This short presumed domain is found close to the ...
698-791
1.18e-23
Family of unknown function (DUF5917); This short presumed domain is found close to the C-terminus of FHIP proteins, FAM160B proteins and UPF0518 family proteins.
Pssm-ID: 466037 Cd Length: 94 Bit Score: 96.10 E-value: 1.18e-23
KELAA motif; This short motif is found at the C-terminus of FHIP proteins, FAM160B proteins ...
1012-1043
3.23e-09
KELAA motif; This short motif is found at the C-terminus of FHIP proteins, FAM160B proteins and UPF0518 family proteins. It has a conserved KELAA sequence for which it is named.
Pssm-ID: 466035 Cd Length: 32 Bit Score: 52.88 E-value: 3.23e-09
Left-handed beta-roll, including virulence factors and various other proteins; This family ...
898-979
6.46e-03
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.
Pssm-ID: 240610 [Multi-domain] Cd Length: 99 Bit Score: 37.14 E-value: 6.46e-03
Retinoic acid induced 16-like protein; This is the conserved N-terminal 450 residues of a ...
101-452
2.62e-139
Retinoic acid induced 16-like protein; This is the conserved N-terminal 450 residues of a family of proteins described as retinoic acid-induced protein 16-like proteins. The exact function is not known. The proteins are found from worms to humans.
Pssm-ID: 370927 Cd Length: 357 Bit Score: 422.89 E-value: 2.62e-139
Family of unknown function (DUF5917); This short presumed domain is found close to the ...
698-791
1.18e-23
Family of unknown function (DUF5917); This short presumed domain is found close to the C-terminus of FHIP proteins, FAM160B proteins and UPF0518 family proteins.
Pssm-ID: 466037 Cd Length: 94 Bit Score: 96.10 E-value: 1.18e-23
KELAA motif; This short motif is found at the C-terminus of FHIP proteins, FAM160B proteins ...
1012-1043
3.23e-09
KELAA motif; This short motif is found at the C-terminus of FHIP proteins, FAM160B proteins and UPF0518 family proteins. It has a conserved KELAA sequence for which it is named.
Pssm-ID: 466035 Cd Length: 32 Bit Score: 52.88 E-value: 3.23e-09
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
831-1017
1.12e-04
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.45 E-value: 1.12e-04
Left-handed beta-roll, including virulence factors and various other proteins; This family ...
898-979
6.46e-03
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.
Pssm-ID: 240610 [Multi-domain] Cd Length: 99 Bit Score: 37.14 E-value: 6.46e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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