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Conserved domains on  [gi|525785413|ref|WP_020830752|]
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DUF4573 domain-containing protein [Listeria monocytogenes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-386 1.50e-27

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 114.65  E-value: 1.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  92 EGVEYLKNLTQVFGYGNQVSDLGP-LSNLTQLEIIQMPRNQISDL-TPIANLTALMSLDFEFNNLQTI-EPIKNLTNMLE 168
Cdd:COG4886  107 EELSNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKE 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 169 LNVSANPISDIS-AVKNMTQLEFLTIRDCEVSDLS-PVENLSNMLMFWAGRNNISDITPLKNMSKLLGLSLFGNQIKDVS 246
Cdd:COG4886  187 LDLSNNQITDLPePLGNLTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 247 VIKNLTSLEDFDIKANQVSDISSLATSTTLETLTLSFNQIIDISSLKNLTNLTRLELENQTRVLDAVEVDDPLILPAPVI 326
Cdd:COG4886  267 PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 327 DENGSRVQPTKVSHAGIYANGEITWEGLQSNYILNYEYNLPVAIGSLTTTYSGKITQPLL 386
Cdd:COG4886  347 LALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLA 406
Internalin_N pfam12354
Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and ...
 1-58 1.10e-10

Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with pfam00560, pfam08191, pfam09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.


:

Pssm-ID: 289150  Cd Length: 50  Bit Score: 56.96  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 525785413    1 MKKTIKITTSLLLSFACVFSIGdftkpHTVEAETVYSLTdskPINEIFPDPKLAQVVA 58
Cdd:pfam12354   1 LKKLLTLTLVLLLSLWVLTSNG-----TDVQAESITPPA---PINQIFPDPALAEEVK 50
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 508-538 3.73e-05

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: 40.92  E-value: 3.73e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 525785413  508 LPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:TIGR01167   2 LPKTGESGNSLLLLLGLLLLGLGGLLLRKRK 32
pullulan_Gpos super family cl37054
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ...
 467-538 8.58e-03

pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.


The actual alignment was detected with superfamily member TIGR02102:

Pssm-ID: 273973 [Multi-domain]  Cd Length: 1111  Bit Score: 39.07  E-value: 8.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525785413   467 PVNPSNQVNPIDPVKSVLQVTETLMKQTTSVNTIVAKDNrNLPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:TIGR02102 1039 KVDPKDNKDPLTPPGSDDENGETPKGNEEKKEEQPDKGA-NLPNTGTKNSNFILFGGLLVLLGTLGYLLKRK 1109
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-386 1.50e-27

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 114.65  E-value: 1.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  92 EGVEYLKNLTQVFGYGNQVSDLGP-LSNLTQLEIIQMPRNQISDL-TPIANLTALMSLDFEFNNLQTI-EPIKNLTNMLE 168
Cdd:COG4886  107 EELSNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKE 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 169 LNVSANPISDIS-AVKNMTQLEFLTIRDCEVSDLS-PVENLSNMLMFWAGRNNISDITPLKNMSKLLGLSLFGNQIKDVS 246
Cdd:COG4886  187 LDLSNNQITDLPePLGNLTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 247 VIKNLTSLEDFDIKANQVSDISSLATSTTLETLTLSFNQIIDISSLKNLTNLTRLELENQTRVLDAVEVDDPLILPAPVI 326
Cdd:COG4886  267 PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 327 DENGSRVQPTKVSHAGIYANGEITWEGLQSNYILNYEYNLPVAIGSLTTTYSGKITQPLL 386
Cdd:COG4886  347 LALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLA 406
LRR_adjacent pfam08191
LRR adjacent; These are small, all beta strand domains, structurally described for the protein ...
 330-386 2.32e-19

LRR adjacent; These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.


Pssm-ID: 369739 [Multi-domain]  Cd Length: 57  Bit Score: 81.64  E-value: 2.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 525785413  330 GSRVQPTKVSHAGIYANGEITWEGLQSNYILNYEYNLPVAIGSLTTTYSGKITQPLL 386
Cdd:pfam08191   1 GSLVAPSTISNNGTYADPNITWNLPSFTSEVSYTFNQPITIGKGTATFSGTVTQPLK 57
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 81-265 2.59e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 75.21  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  81 LHFDSKGVQSLEGVEYLKNLTQVFGYGNQVSDLGPLSNLTQLEIIQMPRNQISDLTPIANLTALMSLDFEFNNLQTIEPI 160
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 161 KNLTNMLELNVSANpisdisavkNMTQLEFLTIRDCEVSDLSP---VENLSNmlmfwagrNNISDITPLKNMSKLLGLSL 237
Cdd:cd21340   87 ENLTNLEELHIENQ---------RLPPGEKLTFDPRSLAALSNslrVLNISG--------NNIDSLEPLAPLRNLEQLDA 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 525785413 238 FGNQIKDVS----VIKNLTSLEDFDIKANQVS 265
Cdd:cd21340  150 SNNQISDLEelldLLSSWPSLRELDLTGNPVC 181
Internalin_N pfam12354
Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and ...
 1-58 1.10e-10

Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with pfam00560, pfam08191, pfam09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.


Pssm-ID: 289150  Cd Length: 50  Bit Score: 56.96  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 525785413    1 MKKTIKITTSLLLSFACVFSIGdftkpHTVEAETVYSLTdskPINEIFPDPKLAQVVA 58
Cdd:pfam12354   1 LKKLLTLTLVLLLSLWVLTSNG-----TDVQAESITPPA---PINQIFPDPALAEEVK 50
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 508-538 3.73e-05

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: 40.92  E-value: 3.73e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 525785413  508 LPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:TIGR01167   2 LPKTGESGNSLLLLLGLLLLGLGGLLLRKRK 32
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
501-538 1.36e-03

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 36.75  E-value: 1.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 525785413  501 VAKDNRNLPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:pfam00746   2 KKSKKKTLPKTGENSNIFLTAAGLLALLGGLLLLVKRR 39
pullulan_Gpos TIGR02102
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ...
 467-538 8.58e-03

pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.


Pssm-ID: 273973 [Multi-domain]  Cd Length: 1111  Bit Score: 39.07  E-value: 8.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525785413   467 PVNPSNQVNPIDPVKSVLQVTETLMKQTTSVNTIVAKDNrNLPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:TIGR02102 1039 KVDPKDNKDPLTPPGSDDENGETPKGNEEKKEEQPDKGA-NLPNTGTKNSNFILFGGLLVLLGTLGYLLKRK 1109
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-386 1.50e-27

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 114.65  E-value: 1.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  92 EGVEYLKNLTQVFGYGNQVSDLGP-LSNLTQLEIIQMPRNQISDL-TPIANLTALMSLDFEFNNLQTI-EPIKNLTNMLE 168
Cdd:COG4886  107 EELSNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKE 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 169 LNVSANPISDIS-AVKNMTQLEFLTIRDCEVSDLS-PVENLSNMLMFWAGRNNISDITPLKNMSKLLGLSLFGNQIKDVS 246
Cdd:COG4886  187 LDLSNNQITDLPePLGNLTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLP 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 247 VIKNLTSLEDFDIKANQVSDISSLATSTTLETLTLSFNQIIDISSLKNLTNLTRLELENQTRVLDAVEVDDPLILPAPVI 326
Cdd:COG4886  267 PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 327 DENGSRVQPTKVSHAGIYANGEITWEGLQSNYILNYEYNLPVAIGSLTTTYSGKITQPLL 386
Cdd:COG4886  347 LALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLA 406
LRR_adjacent pfam08191
LRR adjacent; These are small, all beta strand domains, structurally described for the protein ...
 330-386 2.32e-19

LRR adjacent; These are small, all beta strand domains, structurally described for the protein Internalin (InlA) and related proteins InlB, InlE, InlH from the pathogenic bacterium Listeria monocytogenes. Their function appears to be mainly structural: They are fused to the C-terminal end of leucine-rich repeats (LRR), significantly stabilising the LRR, and forming a common rigid entity with the LRR. They are themselves not involved in protein-protein-interactions but help to present the adjacent LRR-domain for this purpose. These domains belong to the family of Ig-like domains in that they consist of two sandwiched beta sheets that follow the classical connectivity of Ig-domains. The beta strands in one of the sheets is, however, much smaller than in most standard Ig-like domains, making it somewhat of an outlier.


Pssm-ID: 369739 [Multi-domain]  Cd Length: 57  Bit Score: 81.64  E-value: 2.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 525785413  330 GSRVQPTKVSHAGIYANGEITWEGLQSNYILNYEYNLPVAIGSLTTTYSGKITQPLL 386
Cdd:pfam08191   1 GSLVAPSTISNNGTYADPNITWNLPSFTSEVSYTFNQPITIGKGTATFSGTVTQPLK 57
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-305 7.62e-16

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.59  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  74 QLNTVKSLHFDSKGVQSL-EGVEYLKNLTQVFGYGNQVSDLG-PLSNLTQLEIIQMPRNQISDL-TPIANLTALMSLDFE 150
Cdd:COG4886  157 NLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLPePLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLS 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 151 FNNLQTIEPIKNLTNMLELNVSANPISDISAVKNMTQLEFLTIRDCEVSDLspveNLSNMLMFWAGRNNISDITPLKNMS 230
Cdd:COG4886  237 NNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDL----KLKELELLLGLNSLLLLLLLLNLLE 312

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525785413 231 KLLGLSLFGNQIKDVSVIKNLTSLEDFDIKANQVSDISSLATSTTLETLTLSFNQIIDISSLKNLTNLTRLELEN 305
Cdd:COG4886  313 LLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLL 387
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 81-265 2.59e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 75.21  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  81 LHFDSKGVQSLEGVEYLKNLTQVFGYGNQVSDLGPLSNLTQLEIIQMPRNQISDLTPIANLTALMSLDFEFNNLQTIEPI 160
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 161 KNLTNMLELNVSANpisdisavkNMTQLEFLTIRDCEVSDLSP---VENLSNmlmfwagrNNISDITPLKNMSKLLGLSL 237
Cdd:cd21340   87 ENLTNLEELHIENQ---------RLPPGEKLTFDPRSLAALSNslrVLNISG--------NNIDSLEPLAPLRNLEQLDA 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 525785413 238 FGNQIKDVS----VIKNLTSLEDFDIKANQVS 265
Cdd:cd21340  150 SNNQISDLEelldLLSSWPSLRELDLTGNPVC 181
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
97-307 9.16e-13

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 9.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413  97 LKNLTQVFGYGNQVSDLG-PLSNLTQLEIIQMPRNQISDLTPIANLTALMSLDFEFNNLQTIEPIKNLTNMLELNVSANP 175
Cdd:COG4886  204 LTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQ 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 176 ISDISaVKNMTQLEFLTIRDCEVSDLSPVENLSNMLMFWAGRNNISDITPLKNMSKLLGLSLFGNQIKDVSVIKNLTSLE 255
Cdd:COG4886  284 LTDLK-LKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLL 362

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525785413 256 DFDIKANQVSDISSLATSTTLETLTLSFNQIIDISSLKNLTNLTRLELENQT 307
Cdd:COG4886  363 LTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
Internalin_N pfam12354
Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and ...
 1-58 1.10e-10

Bacterial adhesion/invasion protein N terminal; This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with pfam00560, pfam08191, pfam09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.


Pssm-ID: 289150  Cd Length: 50  Bit Score: 56.96  E-value: 1.10e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 525785413    1 MKKTIKITTSLLLSFACVFSIGdftkpHTVEAETVYSLTdskPINEIFPDPKLAQVVA 58
Cdd:pfam12354   1 LKKLLTLTLVLLLSLWVLTSNG-----TDVQAESITPPA---PINQIFPDPALAEEVK 50
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
116-305 1.68e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.87  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 116 LSNLTQLEIIQMPRNQISDLTPIANLTALMSLDFEFNNLQTIEPIKNLTNMLELNVSANPISDISAVKNMTQLEFLTIRD 195
Cdd:COG4886   26 LLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 196 CEvsdlsPVENLSNMLMFWAGRNNISDITP-LKNMSKLLGLSLFGNQIKDV-SVIKNLTSLEDFDIKANQVSDISSLATS 273
Cdd:COG4886  106 NE-----ELSNLTNLESLDLSGNQLTDLPEeLANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEELGN 180

                        170       180       190
                 ....*....|....*....|....*....|....
gi 525785413 274 TTL-ETLTLSFNQIIDIS-SLKNLTNLTRLELEN 305
Cdd:COG4886  181 LTNlKELDLSNNQITDLPePLGNLTNLEELDLSG 214
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
 508-538 3.73e-05

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: 40.92  E-value: 3.73e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 525785413  508 LPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:TIGR01167   2 LPKTGESGNSLLLLLGLLLLGLGGLLLRKRK 32
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
138-305 8.40e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 8.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 138 IANLTALMSLDFEFNNLQTIEPIKNLTNMLELNVSANPISDISAVKNMTQLEFLTIRDCEVSDLSPVENLSNMLmfWAGR 217
Cdd:COG4886   23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLT--NLTE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525785413 218 NNISDITPLKNMSKLLGLSLFGNQIKDV-SVIKNLTSLEDFDIKANQVSDISSLATSTTLETL-TLSFNQIIDIS-SLKN 294
Cdd:COG4886  101 LDLSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSlDLSNNQLTDLPeELGN 180

                        170
                 ....*....|.
gi 525785413 295 LTNLTRLELEN 305
Cdd:COG4886  181 LTNLKELDLSN 191
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
501-538 1.36e-03

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 36.75  E-value: 1.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 525785413  501 VAKDNRNLPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:pfam00746   2 KKSKKKTLPKTGENSNIFLTAAGLLALLGGLLLLVKRR 39
pullulan_Gpos TIGR02102
pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important ...
 467-538 8.58e-03

pullulanase, extracellular, Gram-positive; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.


Pssm-ID: 273973 [Multi-domain]  Cd Length: 1111  Bit Score: 39.07  E-value: 8.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525785413   467 PVNPSNQVNPIDPVKSVLQVTETLMKQTTSVNTIVAKDNrNLPKTGDSGMHSSLVSGLMLAVSSVILLRKRK 538
Cdd:TIGR02102 1039 KVDPKDNKDPLTPPGSDDENGETPKGNEEKKEEQPDKGA-NLPNTGTKNSNFILFGGLLVLLGTLGYLLKRK 1109
 
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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