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Conserved domains on  [gi|1878368645|ref|WP_180757786|]
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LPXTG cell wall anchor domain-containing protein, partial [Streptococcus anginosus]

Protein Classification

LPXTG cell wall anchor domain-containing protein( domain architecture ID 10017673)

LPXTG cell wall anchor domain-containing protein similar to Listeria monocytogenes cell wall protein Lmo2714

Gene Ontology:  GO:0005576

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 132-160 1.16e-03

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


:

Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 34.76  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1878368645 132 TLPHTGEKEATLLVAMGMTLL--AAVYVMKR 160
Cdd:TIGR01167   1 KLPKTGESGNSLLLLLGLLLLglGGLLLRKR 31
PRK09418 super family cl35824
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
1-76 1.59e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


The actual alignment was detected with superfamily member PRK09418:

Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 38.15  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878368645   1 PTTPSTNPSTEPKQPTPgttpaePSEDDKKKEPQPTPKPTEE-----QPKT--TDEANQAGKSQVGTTSTSTGQVVQdVA 73
Cdd:PRK09418  667 PTTPPTGEGDNGENPTT------PPTGEGNNGENPTTPPTGEgnnggNPTTpsTDEGNNAGSGQTTTDNQNSKETTT-VS 739


                  ...
gi 1878368645  74 PNK 76
Cdd:PRK09418  740 ENK 742
 
Name Accession Description Interval E-value
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 132-160 1.16e-03

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 34.76  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1878368645 132 TLPHTGEKEATLLVAMGMTLL--AAVYVMKR 160
Cdd:TIGR01167   1 KLPKTGESGNSLLLLLGLLLLglGGLLLRKR 31
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
1-76 1.59e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 38.15  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878368645   1 PTTPSTNPSTEPKQPTPgttpaePSEDDKKKEPQPTPKPTEE-----QPKT--TDEANQAGKSQVGTTSTSTGQVVQdVA 73
Cdd:PRK09418  667 PTTPPTGEGDNGENPTT------PPTGEGNNGENPTTPPTGEgnnggNPTTpsTDEGNNAGSGQTTTDNQNSKETTT-VS 739


                  ...
gi 1878368645  74 PNK 76
Cdd:PRK09418  740 ENK 742
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
127-160 4.29e-03

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 33.67  E-value: 4.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1878368645 127 TGEKKTLPHTGEKEATLLVAMG--MTLLAAVYVMKR 160
Cdd:pfam00746   3 KSKKKTLPKTGENSNIFLTAAGllALLGGLLLLVKR 38
 
Name Accession Description Interval E-value
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 132-160 1.16e-03

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 34.76  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1878368645 132 TLPHTGEKEATLLVAMGMTLL--AAVYVMKR 160
Cdd:TIGR01167   1 KLPKTGESGNSLLLLLGLLLLglGGLLLRKR 31
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
1-76 1.59e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 38.15  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878368645   1 PTTPSTNPSTEPKQPTPgttpaePSEDDKKKEPQPTPKPTEE-----QPKT--TDEANQAGKSQVGTTSTSTGQVVQdVA 73
Cdd:PRK09418  667 PTTPPTGEGDNGENPTT------PPTGEGNNGENPTTPPTGEgnnggNPTTpsTDEGNNAGSGQTTTDNQNSKETTT-VS 739


                  ...
gi 1878368645  74 PNK 76
Cdd:PRK09418  740 ENK 742
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
127-160 4.29e-03

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 33.67  E-value: 4.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1878368645 127 TGEKKTLPHTGEKEATLLVAMG--MTLLAAVYVMKR 160
Cdd:pfam00746   3 KSKKKTLPKTGENSNIFLTAAGllALLGGLLLLVKR 38
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
1-51 7.14e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 36.09  E-value: 7.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1878368645   1 PTTPSTNPSTEPKQPTPGTTPAEPSEDDKKKEPQPTPKPTEEQPKTTDEAN 51
Cdd:PRK14948  384 SPPPAPIQPSAPKTKQAATTPSPPPAKASPPIPVPAEPTEPSPTPPANAAN 434
 
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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