RHS repeat-associated core domain-containing protein [Salmonella enterica]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||||||||||
| RHS_core super family | cl49306 | RHS element core protein; |
386-1445 | 4.53e-110 | |||||||||||||||||
RHS element core protein; The actual alignment was detected with superfamily member NF041261: Pssm-ID: 469161 [Multi-domain] Cd Length: 1261 Bit Score: 380.12 E-value: 4.53e-110
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| CdiA-CT_Ec-like | cd20692 | C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system (CdiA-CT) ... |
1444-1537 | 7.73e-39 | |||||||||||||||||
C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system (CdiA-CT) protein CdiA of Escherichia coli A0 34/86, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; this particular model contains the C-terminal (CT) domain Escherichia coli A0 34/86 CdiA. Activity of this E. coli CdiA-CT is as yet unknown. CDI(+) bacteria also produce a CDI immunity protein (CdiI) to specifically neutralize the CdiA-CT toxins to prevent auto-inhibition. This CdiA-CT binds its cognate CdiI with high affinity. : Pssm-ID: 411005 Cd Length: 99 Bit Score: 140.01 E-value: 7.73e-39
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| PAAR_like super family | cl21497 | proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR ... |
266-342 | 4.88e-10 | |||||||||||||||||
proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat superfamily, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. The PAAR-repeat proteins form a diverse superfamily with several subgroups extended both N- and C-terminally by domains with various predicted functions; the termini are exposed to solution, and do not distort the VgrG binding site. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli. The actual alignment was detected with superfamily member cd14742: Pssm-ID: 451275 Cd Length: 86 Bit Score: 57.60 E-value: 4.88e-10
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| Name | Accession | Description | Interval | E-value | |||||||||||||||||
| RHS_core | NF041261 | RHS element core protein; |
386-1445 | 4.53e-110 | |||||||||||||||||
RHS element core protein; Pssm-ID: 469161 [Multi-domain] Cd Length: 1261 Bit Score: 380.12 E-value: 4.53e-110
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| RhsA | COG3209 | Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
594-1517 | 1.52e-47 | |||||||||||||||||
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only]; Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 186.50 E-value: 1.52e-47
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| CdiA-CT_Ec-like | cd20692 | C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system (CdiA-CT) ... |
1444-1537 | 7.73e-39 | |||||||||||||||||
C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system (CdiA-CT) protein CdiA of Escherichia coli A0 34/86, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; this particular model contains the C-terminal (CT) domain Escherichia coli A0 34/86 CdiA. Activity of this E. coli CdiA-CT is as yet unknown. CDI(+) bacteria also produce a CDI immunity protein (CdiI) to specifically neutralize the CdiA-CT toxins to prevent auto-inhibition. This CdiA-CT binds its cognate CdiI with high affinity. Pssm-ID: 411005 Cd Length: 99 Bit Score: 140.01 E-value: 7.73e-39
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| Rhs_assc_core | TIGR03696 | RHS repeat-associated core domain; This model represents a conserved unique core sequence ... |
1368-1445 | 3.89e-32 | |||||||||||||||||
RHS repeat-associated core domain; This model represents a conserved unique core sequence shared by large numbers of proteins. It is occasional in the Archaea Methanosarcina barkeri) but common in bacteria and eukaryotes. Most fall into two large classes. One class consists of long proteins in which two classes of repeats are abundant: an FG-GAP repeat (pfam01839) class, and an RHS repeat (pfam05593) or YD repeat (TIGR01643). This class includes secreted bacterial insecticidal toxins and intercellular signalling proteins such as the teneurins in animals. The other class consists of uncharacterized proteins shorter than 400 amino acids, where this core domain of about 75 amino acids tends to occur in the N-terminal half. Over twenty such proteins are found in Pseudomonas putida alone; little sequence similarity or repeat structure is found among these proteins outside the region modeled by this domain. Pssm-ID: 274730 [Multi-domain] Cd Length: 77 Bit Score: 119.91 E-value: 3.89e-32
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| DUF6531 | pfam20148 | Domain of unknown function (DUF6531); This putative domain is found in a range of RHS proteins. |
401-478 | 1.44e-20 | |||||||||||||||||
Domain of unknown function (DUF6531); This putative domain is found in a range of RHS proteins. Pssm-ID: 466309 [Multi-domain] Cd Length: 74 Bit Score: 87.20 E-value: 1.44e-20
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| PAAR_RHS | cd14742 | proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement ... |
266-342 | 4.88e-10 | |||||||||||||||||
proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement hotspot (Rhs) extensions; This PAAR (proline-alanine-alanine-arginine) repeat subfamily, which forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS), contains C- and N-terminal domain extensions. These include Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences at the C-terminal, and various predicted functions at N- and C-terminal extensions. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. Rhs and related YD-peptide repeat proteins are widely distributed in bacteria. Rhs shares similar architecture with distantly related WapA proteins of Bacillus and Listeria species, suggesting intercellular growth inhibition as its primary function. Additionally, a plasmid-encoded Rhs protein has been implicated in bacteriocin production in Pseudomonas savastanoi. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. Pssm-ID: 269827 Cd Length: 86 Bit Score: 57.60 E-value: 4.88e-10
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| Ntox47 | pfam15540 | Bacterial toxin 47; A predicted RNase toxin found in bacterial polymorphic toxin systems that ... |
1430-1510 | 1.25e-04 | |||||||||||||||||
Bacterial toxin 47; A predicted RNase toxin found in bacterial polymorphic toxin systems that is proposed to adopt the BECR (Barnase-EndoU-ColicinE5/D-RelE) fold, and contains two conserved aspartates, a glutamate, a histidine and an arginine residue and an RT motif. In bacterial polymorphic toxin systems, the toxin is usually exported by the type 2, type 6 or type 7 secretion system. Pssm-ID: 406082 Cd Length: 111 Bit Score: 43.04 E-value: 1.25e-04
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| PAAR_motif | pfam05488 | PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ... |
274-326 | 6.05e-04 | |||||||||||||||||
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. It is also found as a triplet of tandem repeats comprising the entire length in a another family of hypothetical proteins. Pssm-ID: 428491 Cd Length: 71 Bit Score: 39.86 E-value: 6.05e-04
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| PAAR | COG4104 | Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ... |
298-343 | 2.69e-03 | |||||||||||||||||
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443280 Cd Length: 87 Bit Score: 38.26 E-value: 2.69e-03
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| Name | Accession | Description | Interval | E-value | |||||||||||||||||
| RHS_core | NF041261 | RHS element core protein; |
386-1445 | 4.53e-110 | |||||||||||||||||
RHS element core protein; Pssm-ID: 469161 [Multi-domain] Cd Length: 1261 Bit Score: 380.12 E-value: 4.53e-110
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| RhsA | COG3209 | Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
594-1517 | 1.52e-47 | |||||||||||||||||
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only]; Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 186.50 E-value: 1.52e-47
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| CdiA-CT_Ec-like | cd20692 | C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system (CdiA-CT) ... |
1444-1537 | 7.73e-39 | |||||||||||||||||
C-terminal (CT) domain of the contact-dependent growth inhibition (CDI) system (CdiA-CT) protein CdiA of Escherichia coli A0 34/86, and similar proteins; CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring cells. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered via the C-terminal domain. A wide variety of C-terminal toxin domains appear to exist; this particular model contains the C-terminal (CT) domain Escherichia coli A0 34/86 CdiA. Activity of this E. coli CdiA-CT is as yet unknown. CDI(+) bacteria also produce a CDI immunity protein (CdiI) to specifically neutralize the CdiA-CT toxins to prevent auto-inhibition. This CdiA-CT binds its cognate CdiI with high affinity. Pssm-ID: 411005 Cd Length: 99 Bit Score: 140.01 E-value: 7.73e-39
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| Rhs_assc_core | TIGR03696 | RHS repeat-associated core domain; This model represents a conserved unique core sequence ... |
1368-1445 | 3.89e-32 | |||||||||||||||||
RHS repeat-associated core domain; This model represents a conserved unique core sequence shared by large numbers of proteins. It is occasional in the Archaea Methanosarcina barkeri) but common in bacteria and eukaryotes. Most fall into two large classes. One class consists of long proteins in which two classes of repeats are abundant: an FG-GAP repeat (pfam01839) class, and an RHS repeat (pfam05593) or YD repeat (TIGR01643). This class includes secreted bacterial insecticidal toxins and intercellular signalling proteins such as the teneurins in animals. The other class consists of uncharacterized proteins shorter than 400 amino acids, where this core domain of about 75 amino acids tends to occur in the N-terminal half. Over twenty such proteins are found in Pseudomonas putida alone; little sequence similarity or repeat structure is found among these proteins outside the region modeled by this domain. Pssm-ID: 274730 [Multi-domain] Cd Length: 77 Bit Score: 119.91 E-value: 3.89e-32
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| DUF6531 | pfam20148 | Domain of unknown function (DUF6531); This putative domain is found in a range of RHS proteins. |
401-478 | 1.44e-20 | |||||||||||||||||
Domain of unknown function (DUF6531); This putative domain is found in a range of RHS proteins. Pssm-ID: 466309 [Multi-domain] Cd Length: 74 Bit Score: 87.20 E-value: 1.44e-20
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| RhsA | COG3209 | Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
593-1008 | 2.83e-20 | |||||||||||||||||
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only]; Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 98.29 E-value: 2.83e-20
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| RhsA | COG3209 | Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
564-942 | 1.10e-19 | |||||||||||||||||
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only]; Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 96.36 E-value: 1.10e-19
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| RHS | pfam03527 | RHS protein; |
1343-1377 | 1.77e-11 | |||||||||||||||||
RHS protein; Pssm-ID: 427349 [Multi-domain] Cd Length: 38 Bit Score: 60.01 E-value: 1.77e-11
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| PAAR_RHS | cd14742 | proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement ... |
266-342 | 4.88e-10 | |||||||||||||||||
proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement hotspot (Rhs) extensions; This PAAR (proline-alanine-alanine-arginine) repeat subfamily, which forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS), contains C- and N-terminal domain extensions. These include Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences at the C-terminal, and various predicted functions at N- and C-terminal extensions. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. Rhs and related YD-peptide repeat proteins are widely distributed in bacteria. Rhs shares similar architecture with distantly related WapA proteins of Bacillus and Listeria species, suggesting intercellular growth inhibition as its primary function. Additionally, a plasmid-encoded Rhs protein has been implicated in bacteriocin production in Pseudomonas savastanoi. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. Pssm-ID: 269827 Cd Length: 86 Bit Score: 57.60 E-value: 4.88e-10
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
921-957 | 2.72e-08 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 51.06 E-value: 2.72e-08
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
901-936 | 6.07e-08 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 49.90 E-value: 6.07e-08
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
880-920 | 3.30e-07 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 47.97 E-value: 3.30e-07
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
858-894 | 5.29e-07 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 47.21 E-value: 5.29e-07
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
921-959 | 4.48e-06 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 44.89 E-value: 4.48e-06
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
774-809 | 4.53e-06 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 44.90 E-value: 4.53e-06
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
880-915 | 2.57e-05 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 42.59 E-value: 2.57e-05
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
837-878 | 7.43e-05 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 41.42 E-value: 7.43e-05
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| RhsA | COG3209 | Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
511-785 | 8.07e-05 | |||||||||||||||||
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only]; Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 47.44 E-value: 8.07e-05
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
837-873 | 1.17e-04 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 40.66 E-value: 1.17e-04
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| Ntox47 | pfam15540 | Bacterial toxin 47; A predicted RNase toxin found in bacterial polymorphic toxin systems that ... |
1430-1510 | 1.25e-04 | |||||||||||||||||
Bacterial toxin 47; A predicted RNase toxin found in bacterial polymorphic toxin systems that is proposed to adopt the BECR (Barnase-EndoU-ColicinE5/D-RelE) fold, and contains two conserved aspartates, a glutamate, a histidine and an arginine residue and an RT motif. In bacterial polymorphic toxin systems, the toxin is usually exported by the type 2, type 6 or type 7 secretion system. Pssm-ID: 406082 Cd Length: 111 Bit Score: 43.04 E-value: 1.25e-04
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
816-850 | 4.58e-04 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 39.12 E-value: 4.58e-04
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
942-976 | 5.47e-04 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 38.73 E-value: 5.47e-04
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| PAAR_motif | pfam05488 | PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ... |
274-326 | 6.05e-04 | |||||||||||||||||
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. It is also found as a triplet of tandem repeats comprising the entire length in a another family of hypothetical proteins. Pssm-ID: 428491 Cd Length: 71 Bit Score: 39.86 E-value: 6.05e-04
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
647-684 | 7.21e-04 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 38.73 E-value: 7.21e-04
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
858-899 | 7.50e-04 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 38.73 E-value: 7.50e-04
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
774-810 | 8.44e-04 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 38.34 E-value: 8.44e-04
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
715-746 | 1.07e-03 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 37.96 E-value: 1.07e-03
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
1037-1072 | 1.46e-03 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 37.58 E-value: 1.46e-03
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
731-786 | 2.08e-03 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 37.19 E-value: 2.08e-03
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| PAAR_like | cd14671 | proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR ... |
290-326 | 2.65e-03 | |||||||||||||||||
proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat superfamily, where it forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). The T6SS is responsible for translocation of a wide variety of toxic effector molecules, allowing predatory cells to kill prokaryotic as well as eukaryotic prey cells. The pointed tip of the PAAR domain is stabilized by a zinc atom positioned close to the cone's vertex and is likely to be important for its integrity during penetration of the target cell envelope. The PAAR-repeat proteins form a diverse superfamily with several subgroups extended both N- and C-terminally by domains with various predicted functions; the termini are exposed to solution, and do not distort the VgrG binding site. VgrG proteins are orthologous to the central baseplate spikes of bacteriophages with contractile tails, and genes encoding proteins with PAAR motifs have been frequently found immediately downstream from vgrG-like genes. It has been shown that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae (encodes two PAAR proteins) and Acinetobacter baylyi (encodes three PAAR proteins); inactivation of all these PAAR genes results in inactivation of Hcp secretion as well as T6SS-dependent killing of E. coli. Pssm-ID: 269821 Cd Length: 77 Bit Score: 38.07 E-value: 2.65e-03
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| PAAR | COG4104 | Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ... |
298-343 | 2.69e-03 | |||||||||||||||||
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 443280 Cd Length: 87 Bit Score: 38.26 E-value: 2.69e-03
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
711-751 | 3.73e-03 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 36.80 E-value: 3.73e-03
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| YD_repeat_2x | TIGR01643 | YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
901-940 | 3.92e-03 | |||||||||||||||||
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin. Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 36.41 E-value: 3.92e-03
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| RHS_repeat | pfam05593 | RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
989-1018 | 5.52e-03 | |||||||||||||||||
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain. Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 36.04 E-value: 5.52e-03
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