NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|746435098|ref|WP_039475379|]
View 

PAAR domain-containing protein [Pectobacterium carotovorum]

Protein Classification

PAAR domain-containing protein( domain architecture ID 10200489)

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); similar to Tequatrovirus T4 baseplate puncturing device gp5.4, a baseplate central spike complex-associated protein

CATH:  2.60.200.60
PubMed:  23925114
SCOP:  4005541

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PAAR_1 cd14737
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 2-99 2.10e-38

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: 134.33  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   2 PGAARLGDSCAGHGCFPATPIIEGSGDVIINGKPAARKSDAVLLHACPcpnvPHGVHNRAISAGSGTVIINGKLAARIGD 81
Cdd:cd14737    1 PAAARLGDICTGHGGFPPTPVIAGSPDVTVNGKPVLRQGDALAPHTCP----KHPPHGGVIASGSSTVFINGKPAARVGD 76

                         90
                 ....*....|....*...
gi 746435098  82 AIGCGGSVAAGSGNVIIG 99
Cdd:cd14737   77 PVSCGGTVAGGSPNVFIG 94
CVT17 super family cl44199
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 253-361 1.53e-06

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG5153:

Pssm-ID: 444061  Cd Length: 405  Bit Score: 50.01  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098 253 TMLTYRGTNnavtGVKDWLTNAGQAM--------------------GFET-------DQYKQAMYLAKQVKEVINPPPV- 304
Cdd:COG5153   47 TIIAFRGTQ----GKPDWKTDINASLhdydeknkeadeklplqvheGFEQyaaqvmdLDYDGAEELAAEVKKQYPDAELs 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 746435098 305 IIGHSLGGGLASAGVGVTGLPGYTFNAAGLHSNTVSRAGGADLAKTASLITTQAVDG 361
Cdd:COG5153  123 LTGHSLGGALASLVAVATGLSKVTFAAPGSGNHALADDLGKRIDAGEFVKSLDAVAG 179
 
Name Accession Description Interval E-value
PAAR_1 cd14737
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 2-99 2.10e-38

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: 134.33  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   2 PGAARLGDSCAGHGCFPATPIIEGSGDVIINGKPAARKSDAVLLHACPcpnvPHGVHNRAISAGSGTVIINGKLAARIGD 81
Cdd:cd14737    1 PAAARLGDICTGHGGFPPTPVIAGSPDVTVNGKPVLRQGDALAPHTCP----KHPPHGGVIASGSSTVFINGKPAARVGD 76

                         90
                 ....*....|....*...
gi 746435098  82 AIGCGGSVAAGSGNVIIG 99
Cdd:cd14737   77 PVSCGGTVAGGSPNVFIG 94
PAAR COG4104
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ...
 1-100 1.86e-24

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: 96.42  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   1 MPGAARLGDSCaghgcFPATPIIEGSGDVIINGKPAARKSDAVllhACPcpnvPHGVhnRAISAGSGTVIINGKLAARIG 80
Cdd:COG4104    2 PKPAARLGDKT-----SHGGPVISGSPTVLIGGRPAARVGDKV---SCP----KHGP--DTIAEGSPTVLINGKPAARVG 67

                         90       100
                 ....*....|....*....|
gi 746435098  81 DAIGCGGSVAAGSGNVIIGD 100
Cdd:COG4104   68 DKTACGGTIISGSPTVLIGG 87
PAAR_motif pfam05488
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ...
 21-90 2.03e-14

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: 67.98  E-value: 2.03e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   21 PIIEGSGDVIINGKPAARKSDavlLHACPcpnvPHGvHNRAISAGSGTVIINGKLAARIGDAIGCGGSVA 90
Cdd:pfam05488  10 VVITGSPTVLIGGKPAARVGD---LVVCP----PCG-GGGPIAEGSPTVLINGKPAAREGDKTACGATLI 71
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 253-361 1.53e-06

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 50.01  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098 253 TMLTYRGTNnavtGVKDWLTNAGQAM--------------------GFET-------DQYKQAMYLAKQVKEVINPPPV- 304
Cdd:COG5153   47 TIIAFRGTQ----GKPDWKTDINASLhdydeknkeadeklplqvheGFEQyaaqvmdLDYDGAEELAAEVKKQYPDAELs 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 746435098 305 IIGHSLGGGLASAGVGVTGLPGYTFNAAGLHSNTVSRAGGADLAKTASLITTQAVDG 361
Cdd:COG5153  123 LTGHSLGGALASLVAVATGLSKVTFAAPGSGNHALADDLGKRIDAGEFVKSLDAVAG 179
DUF6792 pfam20591
Domain of unknown function (DUF6792); This presumed domain is functionally uncharacterized. ...
 237-332 1.69e-03

Domain of unknown function (DUF6792); This presumed domain is functionally uncharacterized. This domain is found in bacteria, and is around 250 amino acids in length. There is a conserved sequence motif GHSLGG. It may have an alpha/beta hydrolase fold suggesting a catalytic role.


Pssm-ID: 466740  Cd Length: 218  Bit Score: 39.92  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098  237 KTGF-GSAL-FKSA---INgETMLTYRGTNNavTGVKDWLTNA-GQAMGFETDQYKQAMYLAKQVKEVIN-------PPP 303
Cdd:pfam20591  45 DSGFdGTAIhFYNEekgIN-EVYTISRGSES--SEDEDWIYNGfGIFAGQSDSQYDDAKIFVEEVTEKIKkktnndiELK 121

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 746435098  304 VI-IGHSLGGGLASA---------GVgvtglpgYTFNAA 332
Cdd:pfam20591 122 KYgLGHSLGGNNIQTlqlltgtfdEV-------YGINGA 153
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 255-316 3.22e-03

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 39.00  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098 255 LTYRGTNnavtGVKDWLTN--------------AGQAM-GFetdqYKQAMYLAKQVKEVI------NPPP--VIIGHSLG 311
Cdd:cd00519   67 IAFRGTV----SLADWLTDldfspvpldpplcsGGKVHsGF----YSAYKSLYNQVLPELksalkqYPDYkiIVTGHSLG 138


                 ....*
gi 746435098 312 GGLAS 316
Cdd:cd00519  139 GALAS 143
 
Name Accession Description Interval E-value
PAAR_1 cd14737
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 2-99 2.10e-38

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: 134.33  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   2 PGAARLGDSCAGHGCFPATPIIEGSGDVIINGKPAARKSDAVLLHACPcpnvPHGVHNRAISAGSGTVIINGKLAARIGD 81
Cdd:cd14737    1 PAAARLGDICTGHGGFPPTPVIAGSPDVTVNGKPVLRQGDALAPHTCP----KHPPHGGVIASGSSTVFINGKPAARVGD 76

                         90
                 ....*....|....*...
gi 746435098  82 AIGCGGSVAAGSGNVIIG 99
Cdd:cd14737   77 PVSCGGTVAGGSPNVFIG 94
PAAR COG4104
Zn-binding Pro-Ala-Ala-Arg (PAAR) domain, involved in Type VI secretion [Intracellular ...
 1-100 1.86e-24

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: 96.42  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   1 MPGAARLGDSCaghgcFPATPIIEGSGDVIINGKPAARKSDAVllhACPcpnvPHGVhnRAISAGSGTVIINGKLAARIG 80
Cdd:COG4104    2 PKPAARLGDKT-----SHGGPVISGSPTVLIGGRPAARVGDKV---SCP----KHGP--DTIAEGSPTVLINGKPAARVG 67

                         90       100
                 ....*....|....*....|
gi 746435098  81 DAIGCGGSVAAGSGNVIIGD 100
Cdd:COG4104   68 DKTACGGTIISGSPTVLIGG 87
PAAR_like cd14671
proline-alanine-alanine-arginine (PAAR) repeat superfamily; This domain is found in the PAAR ...
 4-92 8.00e-18

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: 77.75  E-value: 8.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   4 AARLGDSCAghgCFPATPIIEGSGDVIINGKPAARKSDavllhacpcpNVPHGVHNRAISAGSGTVIINGKLAARIGDAI 83
Cdd:cd14671    2 AARVGDPTA---HTPGGPVISGSPNVFINGRPAARVGD----------VGDHPGGGNAIVSGSGTVFINGKPAARVGDRT 68


                 ....*....
gi 746435098  84 GCGGSVAAG 92
Cdd:cd14671   69 SCGGVIVSG 77
PAAR_RHS cd14742
proline-alanine-alanine-arginine (PAAR) domain, also containing C-terminal Rearrangement ...
 3-99 4.48e-17

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: 75.70  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   3 GAARLGDSCAGHGcfpatPIIEGSGDVIINGKPAARKSDAVLlhACPcpnvPHGVHNRAISAGSGTVIINGKLAARIGDA 82
Cdd:cd14742    1 PAARVGDPIAHTG-----TITSGSPNVFINGKPAARAADSTV--ACS----KHPPPPQLIAEGSETVFINGQPAARKGDK 69

                         90
                 ....*....|....*..
gi 746435098  83 IGCGGSVAAGSGNVIIG 99
Cdd:cd14742   70 TTCSAVISEGSPNVFIG 86
PAAR_5 cd14741
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 2-98 8.77e-16

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: 72.42  E-value: 8.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   2 PGAARLGDScAGHGcfpaTPIIEGSG--DVIINGKPAARK-SDavlLHACPCPN--VPHGvhNRAISAGSGTVIINGKLA 76
Cdd:cd14741    1 PPAARIGDS-TAHG----GPLTPGPGspNVLIGGFPAWRAgGD---GHVCPLVTgpVPHV--GGVVAAGSTTVLINGLPA 70

                         90       100
                 ....*....|....*....|....*
gi 746435098  77 ARIGDAIGCGG---SVAAGSGNVII 98
Cdd:cd14741   71 ARMGDMIVEGGppnTIAMGAPTVLI 95
PAAR_3 cd14739
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 3-99 5.44e-15

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: 70.08  E-value: 5.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   3 GAARLGDScAGHGCFPATPiieGSGDVIINGKPAARKSDavlLHACPCPNVPHGVHNRAISAGSGTVIINGKLAARIGDA 82
Cdd:cd14739    1 AAARVGDP-TTHGGTITGP---GVPTVLIGGMPAAVVGD---MHACVIPPPPAHPPASPFPPGSATVLIGGRPAARVGDA 73

                         90
                 ....*....|....*..
gi 746435098  83 IGCGGSVAAGSGNVIIG 99
Cdd:cd14739   74 CGCGATIVVGAPTVLIG 90
PAAR_motif pfam05488
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ...
 21-90 2.03e-14

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: 67.98  E-value: 2.03e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   21 PIIEGSGDVIINGKPAARKSDavlLHACPcpnvPHGvHNRAISAGSGTVIINGKLAARIGDAIGCGGSVA 90
Cdd:pfam05488  10 VVITGSPTVLIGGKPAARVGD---LVVCP----PCG-GGGPIAEGSPTVLINGKPAAREGDKTACGATLI 71
PAAR_2 cd14738
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 21-99 4.94e-12

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: 61.88  E-value: 4.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098  21 PIIEGSG-DVIINGKPAARKSDAvllhaCPCPNVPHgvhnrAISAGSGTVIINGKLAARIGDAIGCGGSVAAGSGNVIIG 99
Cdd:cd14738   25 PIVGPGPtTVLIGGLPAARVGDM-----CVCVGPPD-----TIVQGSSTVLIGGKPAARMGDSTAHGGVIVSGVPTVLIG 94
PAAR_CT_1 cd14743
proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension; This domain is found ...
 35-102 2.34e-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: 56.54  E-value: 2.34e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746435098  35 PAARKSDavlLHACPCPNVPHgvhnrAISAGSGTVIINGKLAARIGDAIGCGGSVAAGSGNVIIGDSP 102
Cdd:cd14743    1 PAARVGD---PHACPLPGHGS-----TPIGSSSADFFDGLPAARVGDKTSCGATIVSGSINVLINGKP 60
PAAR_CT_2 cd14744
proline-alanine-alanine-arginine (PAAR) domain with uncharacterized C-terminal extension; This ...
 3-86 1.21e-09

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: 54.48  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   3 GAARLGD--SCAGHgcfpatpIIEGSGDVIINGKPAARKSDAVllhACPcpnVPHGVHnrAISAGSGTVIINGKLAARIG 80
Cdd:cd14744    2 GIIRLGDktTHGGV-------VISGSSTFTIDGRPVARVGDKV---TCP---KCKGTG--PIVEGGPTFTVDGRPVALDG 66


                 ....*.
gi 746435098  81 DAIGCG 86
Cdd:cd14744   67 DRVACG 72
PAAR_CT_1 cd14743
proline-alanine-alanine-arginine (PAAR) domain with C-terminal extension; This domain is found ...
 4-93 1.58e-09

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: 54.23  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098   4 AARLGD--SCAGHGcfpATPIIEGSGDV-IINGKPAARKSDAVllhACpcpnvphgvhNRAISAGSGTVIINGKLAARIG 80
Cdd:cd14743    2 AARVGDphACPLPG---HGSTPIGSSSAdFFDGLPAARVGDKT---SC----------GATIVSGSINVLINGKPAAVLG 65

                         90
                 ....*....|...
gi 746435098  81 DAIGCGGSVAAGS 93
Cdd:cd14743   66 STTSHGGVVIGGS 78
PAAR_4 cd14740
proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR ...
 17-102 4.35e-09

proline-alanine-alanine-arginine (PAAR) domain; This domain is found in the PAAR (proline-alanine-alanine-arginine) repeat family of bacteria, and forms a sharp conical extension on the VgrG spike, a trimeric protein complex of the bacterial type VI secretion system (T6SS). A few 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 such as DUF4150. 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: 269825  Cd Length: 121  Bit Score: 54.36  E-value: 4.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098  17 FPATPIIEGSGDVIINGKPAARKSDavlLHACPCPNVPHGVHNRA-----ISAGSGTVIINGKLAARIGD-AIGCGGSVA 90
Cdd:cd14740   32 GAGLIVGGLSPTVLIGGMPAATVGS---TAGNTPGGVPGGPSVPPanpgtIVMGSSTVFINGKPAARMGDmTATCNDPAP 108

                         90
                 ....*....|..
gi 746435098  91 AGSGNVIIGDSP 102
Cdd:cd14740  109 APVGTVVPPGAT 120
CVT17 COG5153
Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) ...
 253-361 1.53e-06

Putative lipase ATG15 (essential for vacuolar disintegration of autophagic bodies) [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444061  Cd Length: 405  Bit Score: 50.01  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098 253 TMLTYRGTNnavtGVKDWLTNAGQAM--------------------GFET-------DQYKQAMYLAKQVKEVINPPPV- 304
Cdd:COG5153   47 TIIAFRGTQ----GKPDWKTDINASLhdydeknkeadeklplqvheGFEQyaaqvmdLDYDGAEELAAEVKKQYPDAELs 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 746435098 305 IIGHSLGGGLASAGVGVTGLPGYTFNAAGLHSNTVSRAGGADLAKTASLITTQAVDG 361
Cdd:COG5153  123 LTGHSLGGALASLVAVATGLSKVTFAAPGSGNHALADDLGKRIDAGEFVKSLDAVAG 179
PAAR_motif pfam05488
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ...
 4-51 2.24e-06

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: 45.25  E-value: 2.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 746435098    4 AARLGDSCAGHGCFPATPIIEGSGDVIINGKPAARKSDAVllhACPCP 51
Cdd:pfam05488  25 AARVGDLVVCPPCGGGGPIAEGSPTVLINGKPAAREGDKT---ACGAT 69
PAAR_motif pfam05488
PAAR motif; This motif is found usually in pairs in a family of bacterial membrane proteins. ...
 62-102 2.29e-05

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: 42.17  E-value: 2.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 746435098   62 ISAGSGTVIINGKLAARIGDAIGC-----GGSVAAGSGNVIIGDSP 102
Cdd:pfam05488  11 VITGSPTVLIGGKPAARVGDLVVCppcggGGPIAEGSPTVLINGKP 56
DUF6792 pfam20591
Domain of unknown function (DUF6792); This presumed domain is functionally uncharacterized. ...
 237-332 1.69e-03

Domain of unknown function (DUF6792); This presumed domain is functionally uncharacterized. This domain is found in bacteria, and is around 250 amino acids in length. There is a conserved sequence motif GHSLGG. It may have an alpha/beta hydrolase fold suggesting a catalytic role.


Pssm-ID: 466740  Cd Length: 218  Bit Score: 39.92  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098  237 KTGF-GSAL-FKSA---INgETMLTYRGTNNavTGVKDWLTNA-GQAMGFETDQYKQAMYLAKQVKEVIN-------PPP 303
Cdd:pfam20591  45 DSGFdGTAIhFYNEekgIN-EVYTISRGSES--SEDEDWIYNGfGIFAGQSDSQYDDAKIFVEEVTEKIKkktnndiELK 121

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 746435098  304 VI-IGHSLGGGLASA---------GVgvtglpgYTFNAA 332
Cdd:pfam20591 122 KYgLGHSLGGNNIQTlqlltgtfdEV-------YGINGA 153
Lipase_3 cd00519
Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into ...
 255-316 3.22e-03

Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site.


Pssm-ID: 238287 [Multi-domain]  Cd Length: 229  Bit Score: 39.00  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746435098 255 LTYRGTNnavtGVKDWLTN--------------AGQAM-GFetdqYKQAMYLAKQVKEVI------NPPP--VIIGHSLG 311
Cdd:cd00519   67 IAFRGTV----SLADWLTDldfspvpldpplcsGGKVHsGF----YSAYKSLYNQVLPELksalkqYPDYkiIVTGHSLG 138


                 ....*
gi 746435098 312 GGLAS 316
Cdd:cd00519  139 GALAS 143
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH