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Conserved domains on  [gi|2445162546|gb|WDD96540|]
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PAAR domain-containing protein [Burkholderia sp. FERM BP-3421]

Protein Classification

PAAR domain-containing protein( domain architecture ID 11467868)

PAAR (proline-alanine-alanine-arginine) domain-containing protein forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS); contains uncharacterized C-terminal extension

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAAR COG4104
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ...
 1-80 1.04e-25

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: 90.64  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445162546  1 MRNVIRVGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPiaGHQACVIVEGDPNFVIDGRAVAFDGHRTSCGATLRST 80
Cdd:COG4104    2 PKPAARLGDKTSHGGPVISGSPTVLIGGRPAARVGDKVSCP--KHGPDTIAEGSPTVLINGKPAARVGDKTACGGTIISG 79
 
Name Accession Description Interval E-value
PAAR COG4104
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ...
 1-80 1.04e-25

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: 90.64  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445162546  1 MRNVIRVGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPiaGHQACVIVEGDPNFVIDGRAVAFDGHRTSCGATLRST 80
Cdd:COG4104    2 PKPAARLGDKTSHGGPVISGSPTVLIGGRPAARVGDKVSCP--KHGPDTIAEGSPTVLINGKPAARVGDKTACGGTIISG 79
PAAR_CT_2 cd14744
proline-alanine-alanine-arginine (PAAR) domain with uncharacterized C-terminal extension; This ...
 2-80 4.20e-25

proline-alanine-alanine-arginine (PAAR) domain with uncharacterized C-terminal extension; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of mostly beta- and gamma-proteobacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). Most members contain C-terminal domain extensions corresponding to several uncharacterized domains such as S-type pyocin, DUF2235, DUF2345 and cytotoxic proteins. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. 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: 269829  Cd Length: 78  Bit Score: 88.77  E-value: 4.20e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2445162546  2 RNVIRVGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPiAGHQACVIVEGDPNFVIDGRAVAFDGHRTSCGATLRST 80
Cdd:cd14744    1 RGIIRLGDKTTHGGVVISGSSTFTIDGRPVARVGDKVTCP-KCKGTGPIVEGGPTFTVDGRPVALDGDRVACGCPLIPS 78
PAAR_motif pfam05488
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ...
 7-77 8.41e-22

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: 80.31  E-value: 8.41e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2445162546  7 VGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPIAGHQaCVIVEGDPNFVIDGRAVAFDGHRTSCGATL 77
Cdd:pfam05488  1 LGDKTSHGGVVITGSPTVLIGGKPAARVGDLVVCPPCGGG-GPIAEGSPTVLINGKPAAREGDKTACGATL 70
 
Name Accession Description Interval E-value
PAAR COG4104
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ...
 1-80 1.04e-25

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: 90.64  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445162546  1 MRNVIRVGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPiaGHQACVIVEGDPNFVIDGRAVAFDGHRTSCGATLRST 80
Cdd:COG4104    2 PKPAARLGDKTSHGGPVISGSPTVLIGGRPAARVGDKVSCP--KHGPDTIAEGSPTVLINGKPAARVGDKTACGGTIISG 79
PAAR_CT_2 cd14744
proline-alanine-alanine-arginine (PAAR) domain with uncharacterized C-terminal extension; This ...
 2-80 4.20e-25

proline-alanine-alanine-arginine (PAAR) domain with uncharacterized C-terminal extension; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of mostly beta- and gamma-proteobacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). Most members contain C-terminal domain extensions corresponding to several uncharacterized domains such as S-type pyocin, DUF2235, DUF2345 and cytotoxic proteins. However, these terminal domains are exposed to solution, and do not distort the binding site of VgrG. 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: 269829  Cd Length: 78  Bit Score: 88.77  E-value: 4.20e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2445162546  2 RNVIRVGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPiAGHQACVIVEGDPNFVIDGRAVAFDGHRTSCGATLRST 80
Cdd:cd14744    1 RGIIRLGDKTTHGGVVISGSSTFTIDGRPVARVGDKVTCP-KCKGTGPIVEGGPTFTVDGRPVALDGDRVACGCPLIPS 78
PAAR_motif pfam05488
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ...
 7-77 8.41e-22

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: 80.31  E-value: 8.41e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2445162546  7 VGDPTSHGGVVETGDVGFVVDGRAVARVGDGCTCPIAGHQaCVIVEGDPNFVIDGRAVAFDGHRTSCGATL 77
Cdd:pfam05488  1 LGDKTSHGGVVITGSPTVLIGGKPAARVGDLVVCPPCGGG-GPIAEGSPTVLINGKPAAREGDKTACGATL 70
PAAR_CT_1 cd14743
proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension; This domain is found ...
 4-77 3.10e-10

proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of mostly gamma-proteobacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). Some members contains C-terminal domain extensions corresponding to Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences as well as uncharacterized domains. 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: 269828  Cd Length: 78  Bit Score: 51.15  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445162546  4 VIRVGDPTS---HGG---VVETGDVGFVvDGRAVARVGDGCTCpiaghqACVIVEGDPNFVIDGRAVAFDGHRTSCGATL 77
Cdd:cd14743    2 AARVGDPHAcplPGHgstPIGSSSADFF-DGLPAARVGDKTSC------GATIVSGSINVLINGKPAAVLGSTTSHGGVV 74
PAAR_like cd14671
proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR ...
 6-77 1.85e-09

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: 49.24  E-value: 1.85e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2445162546  6 RVGDPTSH--GGVVETGDVGFVVDGRAVARVGDGCTCPIAGHqacVIVEGDPNFVIDGRAVAFDGHRTSCGATL 77
Cdd:cd14671    4 RVGDPTAHtpGGPVISGSPNVFINGRPAARVGDVGDHPGGGN---AIVSGSGTVFINGKPAARVGDRTSCGGVI 74
PAAR_1 cd14737
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 3-79 1.63e-07

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, 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. 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: 269822  Cd Length: 94  Bit Score: 44.58  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445162546  3 NVIRVGDPTS-HGG----VVETGDVGFVVDGRAVARVGDGC---TCPIAGHQACVIVEGDPNFVIDGRAVAFDGHRTSCG 74
Cdd:cd14737    2 AAARLGDICTgHGGfpptPVIAGSPDVTVNGKPVLRQGDALaphTCPKHPPHGGVIASGSSTVFINGKPAARVGDPVSCG 81


                 ....*
gi 2445162546 75 ATLRS 79
Cdd:cd14737   82 GTVAG 86
PAAR_3 cd14739
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 6-77 7.73e-07

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, 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. 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: 269824  Cd Length: 90  Bit Score: 42.73  E-value: 7.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2445162546  6 RVGDPTSHGGVVETGDVGFV-VDGRAVARVGDGCTC----PIAGHQACVIVEGDPNFVIDGRAVAFDGHRTSCGATL 77
Cdd:cd14739    4 RVGDPTTHGGTITGPGVPTVlIGGMPAAVVGDMHACvippPPAHPPASPFPPGSATVLIGGRPAARVGDACGCGATI 80
PAAR_CT_1 cd14743
proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension; This domain is found ...
 30-84 1.47e-06

proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of mostly gamma-proteobacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). Some members contains C-terminal domain extensions corresponding to Rearrangement hotspot (Rhs) protein repeats and conserved Rhs repeat-associated unique core sequences as well as uncharacterized domains. 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: 269828  Cd Length: 78  Bit Score: 41.90  E-value: 1.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2445162546 30 AVARVGDGCTCPIAGHQACVIVEGDPNFViDGRAVAFDGHRTSCGATLRSTMERF 84
Cdd:cd14743    1 PAARVGDPHACPLPGHGSTPIGSSSADFF-DGLPAARVGDKTSCGATIVSGSINV 54
PAAR_RHS cd14742
proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement ...
 6-79 1.37e-04

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: 36.80  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2445162546  6 RVGDPTSHGGVVETGDVGFVVDGRAVARV-GDGCTCpiAGHQACV--IVEGDPNFVIDGRAVAFDGHRTSCGATLRS 79
Cdd:cd14742    4 RVGDPIAHTGTITSGSPNVFINGKPAARAaDSTVAC--SKHPPPPqlIAEGSETVFINGQPAARKGDKTTCSAVISE 78
PAAR_5 cd14741
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 6-74 1.08e-03

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family in bacteria as well as some archaea, 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. 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: 269826  Cd Length: 95  Bit Score: 34.68  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2445162546  6 RVGDPTSHGGVVETGDVGFVV--DGRAVAR-VGDGCTCPIAG----HQACVIVEGDPNFVIDGRAVAFDGHRTSCG 74
Cdd:cd14741    5 RIGDSTAHGGPLTPGPGSPNVliGGFPAWRaGGDGHVCPLVTgpvpHVGGVVAAGSTTVLINGLPAARMGDMIVEG 80
PAAR_1 cd14737
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 2-59 1.90e-03

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, 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. 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: 269822  Cd Length: 94  Bit Score: 34.18  E-value: 1.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2445162546  2 RNVIRVGDPTS---------HGGVVETGDVGFVVDGRAVARVGDGCTCpiaghqACVIVEGDPNFVI 59
Cdd:cd14737   33 KPVLRQGDALAphtcpkhppHGGVIASGSSTVFINGKPAARVGDPVSC------GGTVAGGSPNVFI 93
PAAR_2 cd14738
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 10-77 5.25e-03

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family, 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. 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: 269823  Cd Length: 94  Bit Score: 32.99  E-value: 5.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2445162546 10 PTSHGG--VVETGDVGFVVDGRAVARVGDGCTCpiAGHQAcVIVEGDPNFVIDGRAVAFDGHRTSCGATL 77
Cdd:cd14738   18 PVPHVGgpIVGPGPTTVLIGGLPAARVGDMCVC--VGPPD-TIVQGSSTVLIGGKPAARMGDSTAHGGVI 84
 
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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