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Conserved domains on  [gi|937518497|gb|ALI38983|]
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methyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

prepilin peptidase( domain architecture ID 11449472)

prepilin peptidase, A24 family peptidase, processes type 4 pilin precursor proteins (prepilins) to their mature forms by removal of leader peptides

CATH:  1.20.120.1220
EC:  3.4.23.43
Gene Ontology:  GO:0004190|GO:0016020
MEROPS:  A24
PubMed:  25793961|7961448

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
74-223 2.78e-39

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: 135.68  E-value: 2.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497  74 PIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNAQYGLIDLHDAVYGAVAGYGVLWCVYWGVWLVCHKEG 153
Cdd:COG1989   98 SLQLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEG 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937518497 154 LGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTITT-IAFGPWLALGSMINLGYLAWI 223
Cdd:COG1989  178 MGGGDVKLLAALGAWLGWQALLLILLLASLLGALVGLILLLLGRKGRKTpIPFGPFLALGGLIALLFGDQI 248
 
Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
74-223 2.78e-39

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: 135.68  E-value: 2.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497  74 PIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNAQYGLIDLHDAVYGAVAGYGVLWCVYWGVWLVCHKEG 153
Cdd:COG1989   98 SLQLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEG 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937518497 154 LGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTITT-IAFGPWLALGSMINLGYLAWI 223
Cdd:COG1989  178 MGGGDVKLLAALGAWLGWQALLLILLLASLLGALVGLILLLLGRKGRKTpIPFGPFLALGGLIALLFGDQI 248
Peptidase_A24 pfam01478
Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, ...
81-190 6.05e-15

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: 67.95  E-value: 6.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497   81 FLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNaqYGLIDLHDAVYGAVAGYGVLWCVYwgvwlvcHKEGLGYGDFK 160
Cdd:pfam01478   1 LVLLSLLLLLSVIDLRTRLIPNRLTLPLLWLGLIFA--LGLLSLLDALLGAAAGFLLLFLLY-------LKGGMGGGDVK 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 937518497  161 LLAAAGAWCGWQTLPMILLIASLGGIGYAI 190
Cdd:pfam01478  72 LLAALGAWLGWQLLLLFLLLASLLGAILGL 101
 
Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
74-223 2.78e-39

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: 135.68  E-value: 2.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497  74 PIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNAQYGLIDLHDAVYGAVAGYGVLWCVYWGVWLVCHKEG 153
Cdd:COG1989   98 SLQLLAALLLLSLLLALSFIDLDTQLLPDSLTLPLLWLGLLLSLLGGFVSLLDALLGALAGYLLLWLIYWLFKLLTGKEG 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937518497 154 LGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTITT-IAFGPWLALGSMINLGYLAWI 223
Cdd:COG1989  178 MGGGDVKLLAALGAWLGWQALLLILLLASLLGALVGLILLLLGRKGRKTpIPFGPFLALGGLIALLFGDQI 248
Peptidase_A24 pfam01478
Type IV leader peptidase family; Peptidase A24, or the prepilin peptidase as it is also known, ...
81-190 6.05e-15

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: 67.95  E-value: 6.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497   81 FLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFNaqYGLIDLHDAVYGAVAGYGVLWCVYwgvwlvcHKEGLGYGDFK 160
Cdd:pfam01478   1 LVLLSLLLLLSVIDLRTRLIPNRLTLPLLWLGLIFA--LGLLSLLDALLGAAAGFLLLFLLY-------LKGGMGGGDVK 71
                          90       100       110
                  ....*....|....*....|....*....|
gi 937518497  161 LLAAAGAWCGWQTLPMILLIASLGGIGYAI 190
Cdd:pfam01478  72 LLAALGAWLGWQLLLLFLLLASLLGAILGL 101
CpaA COG4960
Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, ...
73-223 2.30e-04

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


Pssm-ID: 443986  Cd Length: 161  Bit Score: 40.26  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497  73 TPIVTGALFLYFCFVLTLSVIDFRTQLLPDKLTLPLLWLGLVFN-AQYGLIDLHDAVYGAVAGYGVLWCVYWgvwlvchK 151
Cdd:COG4960    2 SLLLLLLLLLLLALLAFAAYTDLRTRRIPNRLVLALLLLGLLLAlLSGLLAGLGLSLLGALIGLAVGFPLFA-------L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937518497 152 EGLGYGDFKLLAAAGAWCGWQTLPMILLIASLGGIGYAIVSQLLQRRTI---------------TTIAFGPWLALGSMIN 216
Cdd:COG4960   75 GGMGGGDVKLLAALGLWLGPAALLLFLLLTALAGGVLALILLLLRRLPAaagrppwlarlrdrkRGVPYGVAIAAGALLA 154

                 ....*..
gi 937518497 217 LGYLAWI 223
Cdd:COG4960  155 LPASLLL 161
 
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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