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Conserved domains on  [gi|499974574|ref|WP_011655292|]
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MULTISPECIES: prepilin peptidase [Rhizobium]

Protein Classification

prepilin peptidase( domain architecture ID 10008983)

prepilin peptidase processes type 4 pilin precursor proteins (prepilins) to their mature forms by removal of leader peptides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CpaA COG4960
Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, ...
20-180 5.41e-19

Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


:

Pssm-ID: 443986  Cd Length: 161  Bit Score: 79.16  E-value: 5.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574  20 CTMTAAVLDHRHGHIPNAVTYPCLLGGFMLAAVSGGLAGIGLAFAGLLAAGLIFIIAFAAGSCGGGDVKLMAALGAILGL 99
Cdd:COG4960   15 LLAFAAYTDLRTRRIPNRLVLALLLLGLLLALLSGLLAGLGLSLLGALIGLAVGFPLFALGGMGGGDVKLLAALGLWLGP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574 100 WPAIDVTLASLMAGGVIAVFSMARRVqwsvlartvglfallLPAGFRDAASVLKPRETHHTVRFGVAAALGLLWCLFMPD 179
Cdd:COG4960   95 AALLLFLLLTALAGGVLALILLLLRR---------------LPAAAGRPPWLARLRDRKRGVPYGVAIAAGALLALPASL 159

                 .
gi 499974574 180 F 180
Cdd:COG4960  160 L 160
 
Name Accession Description Interval E-value
CpaA COG4960
Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, ...
20-180 5.41e-19

Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 443986  Cd Length: 161  Bit Score: 79.16  E-value: 5.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574  20 CTMTAAVLDHRHGHIPNAVTYPCLLGGFMLAAVSGGLAGIGLAFAGLLAAGLIFIIAFAAGSCGGGDVKLMAALGAILGL 99
Cdd:COG4960   15 LLAFAAYTDLRTRRIPNRLVLALLLLGLLLALLSGLLAGLGLSLLGALIGLAVGFPLFALGGMGGGDVKLLAALGLWLGP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574 100 WPAIDVTLASLMAGGVIAVFSMARRVqwsvlartvglfallLPAGFRDAASVLKPRETHHTVRFGVAAALGLLWCLFMPD 179
Cdd:COG4960   95 AALLLFLLLTALAGGVLALILLLLRR---------------LPAAAGRPPWLARLRDRKRGVPYGVAIAAGALLALPASL 159

                 .
gi 499974574 180 F 180
Cdd:COG4960  160 L 160
Peptidase_A24 pfam01478
Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, ...
23-118 1.12e-07

Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, processes the N-terminus of the prepilins. The processing is essential for the correct formation of the pseudopili of type IV bacterial protein secretion. The enzyme is found across eubacteria and archaea.


Pssm-ID: 426281  Cd Length: 101  Bit Score: 47.92  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574   23 TAAVLDHRHGHIPNAVTYPCLLGGFMLAavsGGLAGIGLAFAGLLAAGLIFIIAFAAGSCGGGDVKLMAALGAILGLWPA 102
Cdd:pfam01478   9 LLSVIDLRTRLIPNRLTLPLLWLGLIFA---LGLLSLLDALLGAAAGFLLLFLLYLKGGMGGGDVKLLAALGAWLGWQLL 85
                          90
                  ....*....|....*.
gi 499974574  103 IDVTLASLMAGGVIAV 118
Cdd:pfam01478  86 LLFLLLASLLGAILGL 101
 
Name Accession Description Interval E-value
CpaA COG4960
Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, ...
20-180 5.41e-19

Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 443986  Cd Length: 161  Bit Score: 79.16  E-value: 5.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574  20 CTMTAAVLDHRHGHIPNAVTYPCLLGGFMLAAVSGGLAGIGLAFAGLLAAGLIFIIAFAAGSCGGGDVKLMAALGAILGL 99
Cdd:COG4960   15 LLAFAAYTDLRTRRIPNRLVLALLLLGLLLALLSGLLAGLGLSLLGALIGLAVGFPLFALGGMGGGDVKLLAALGLWLGP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574 100 WPAIDVTLASLMAGGVIAVFSMARRVqwsvlartvglfallLPAGFRDAASVLKPRETHHTVRFGVAAALGLLWCLFMPD 179
Cdd:COG4960   95 AALLLFLLLTALAGGVLALILLLLRR---------------LPAAAGRPPWLARLRDRKRGVPYGVAIAAGALLALPASL 159

                 .
gi 499974574 180 F 180
Cdd:COG4960  160 L 160
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
22-124 4.23e-11

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 59.80  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574  22 MTAAVLDHRHGHIPNAVTYPCLLGGFMLAAVSGGLAGIGLAFAGLLAAGLIFIIAFAAGSC------GGGDVKLMAALGA 95
Cdd:COG1989  112 LALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLtgkegmGGGDVKLLAALGA 191
                         90       100
                 ....*....|....*....|....*....
gi 499974574  96 ILGLWPAIDVTLASLMAGGVIAVFSMARR 124
Cdd:COG1989  192 WLGWQALLLILLLASLLGALVGLILLLLG 220
Peptidase_A24 pfam01478
Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, ...
23-118 1.12e-07

Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, processes the N-terminus of the prepilins. The processing is essential for the correct formation of the pseudopili of type IV bacterial protein secretion. The enzyme is found across eubacteria and archaea.


Pssm-ID: 426281  Cd Length: 101  Bit Score: 47.92  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499974574   23 TAAVLDHRHGHIPNAVTYPCLLGGFMLAavsGGLAGIGLAFAGLLAAGLIFIIAFAAGSCGGGDVKLMAALGAILGLWPA 102
Cdd:pfam01478   9 LLSVIDLRTRLIPNRLTLPLLWLGLIFA---LGLLSLLDALLGAAAGFLLLFLLYLKGGMGGGDVKLLAALGAWLGWQLL 85
                          90
                  ....*....|....*.
gi 499974574  103 IDVTLASLMAGGVIAV 118
Cdd:pfam01478  86 LLFLLLASLLGAILGL 101
 
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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