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Conserved domains on  [gi|447116465|ref|WP_001193721|]
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LPXTG-anchored hyaluronate lyase [Streptococcus pneumoniae]

Protein Classification

GAG_Lyase and LPXTG_anchor domain-containing protein( domain architecture ID 10375106)

protein containing domains CBM_4_9, GAG_Lyase, and LPXTG_anchor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
291-993 0e+00

Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase.


:

Pssm-ID: 238517 [Multi-domain]  Cd Length: 693  Bit Score: 800.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  291 TYTDRLDDWNGIIAGNQYYDSKneqMAKLNQELEGKVADSLSSISSQADRIYLWEKFSNYKTSANLTATYRKLEEMAKQV 370
Cdd:cd01083     1 EFDALRKRWADIITGNPAYDTS---MAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRLETLAKAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  371 TNPSSRYYQDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIKKYTDVIEKFVPDP 450
Cdd:cd01083    78 TTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSEELIKKYTDAIRWFVPDP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  451 EHFRkTTDNPFKALGGNLVDMGRVKVIAGLLRKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVL 530
Cdd:cd01083   158 EHQR-TKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTEGDGFYADGSFIQHGGVPYTGGYGNVL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  531 IDGLSQLLPVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIHRIADMSEGE 610
Cdd:cd01083   237 LKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  611 TKQRLQSLVKTIVQSDSYYDVFKNLKTYKDIslmQSLLSDAGVASVPRTSYLSAFNKMDKTAMYNAekGFGFGLSLFSSR 690
Cdd:cd01083   317 LAAALRSLIKRWITRDTYYPVFNNPKSYSDI---KLLLADASIAPAAEPQGHKQFNSMDRAVHRRP--DFAFGLSMYSTR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  691 TLNYEHMNKENKRGWYTSDGMFYLYNGDLSHYSDGYWPTVNPYKMPGTTETDAKRAD----SDTGKVLPSAFVGTSKLDD 766
Cdd:cd01083   392 TANYEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTIHLPLADlvegSWGMKRGTSNFVGGVSLGK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  767 aNATATMDFTNWNQTLTAHKSWFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESsnPYKVYVNDKEASLTEQEKDYPET 846
Cdd:cd01083   472 -YGAAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTG--PGTVYVNGKETALGEQSFTLTGG 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  847 QSVFLESsdskKNIGYFFFKKSSISMSKALQKGAWKDINEGQSDKEVENEFLTISQAHKQN--GDSYGYMLIPNVDRATF 924
Cdd:cd01083   549 SWVHLEG----DNIGYYFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLWIDHGKNptNASYAYVLLPGATREKV 624
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447116465  925 NQMIKELESSLIENNETLQSVYDAKQGVWGIVKYDDSVSTISNQFQVLKRGVYTIRKEGDEYKIAYYNP 993
Cdd:cd01083   625 KAYAKKPNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSLEITVNKPCSVMIRKESNGLKLSVSDP 693
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
1037-1067 1.11e-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: 37.45  E-value: 1.11e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 447116465  1037 LPQTGE-GQSILASLGFLLLG-AFYLFRRGKNN 1067
Cdd:TIGR01167    2 LPKTGEsGNSLLLLLGLLLLGlGGLLLRKRKKK 34
CBM_4_9 super family cl19911
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
53-190 1.54e-03

Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.


The actual alignment was detected with superfamily member pfam02018:

Pssm-ID: 418717  Cd Length: 134  Bit Score: 39.74  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465    53 KNLVENGDFgqtEDGS-SPWTGskaqGWSAWVDQKNSSADASTRVIEAKDGAITISSPeklraAVHRMVPIEAKKKYKLR 131
Cdd:pfam02018    1 GNLIKNGTF---EDGGlDGWKA----RGGSGKATVDVTSYNGTYSLKVSGRTATWDGQ-----IIDITIRLEKGTTYTVS 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447116465   132 FKIKTDNKVG---IAKVRIIEESGKDKRLWNSATTSgTKDWQTIEADYSPTLDVDKIKLELF 190
Cdd:pfam02018   69 FWVKASSGPPqtvSVTLQITDASGNYDTVADEKVVL-TGEWTKLEGTFTIPKTASTVELYVE 129
 
Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
291-993 0e+00

Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase.


Pssm-ID: 238517 [Multi-domain]  Cd Length: 693  Bit Score: 800.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  291 TYTDRLDDWNGIIAGNQYYDSKneqMAKLNQELEGKVADSLSSISSQADRIYLWEKFSNYKTSANLTATYRKLEEMAKQV 370
Cdd:cd01083     1 EFDALRKRWADIITGNPAYDTS---MAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRLETLAKAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  371 TNPSSRYYQDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIKKYTDVIEKFVPDP 450
Cdd:cd01083    78 TTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSEELIKKYTDAIRWFVPDP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  451 EHFRkTTDNPFKALGGNLVDMGRVKVIAGLLRKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVL 530
Cdd:cd01083   158 EHQR-TKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTEGDGFYADGSFIQHGGVPYTGGYGNVL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  531 IDGLSQLLPVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIHRIADMSEGE 610
Cdd:cd01083   237 LKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  611 TKQRLQSLVKTIVQSDSYYDVFKNLKTYKDIslmQSLLSDAGVASVPRTSYLSAFNKMDKTAMYNAekGFGFGLSLFSSR 690
Cdd:cd01083   317 LAAALRSLIKRWITRDTYYPVFNNPKSYSDI---KLLLADASIAPAAEPQGHKQFNSMDRAVHRRP--DFAFGLSMYSTR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  691 TLNYEHMNKENKRGWYTSDGMFYLYNGDLSHYSDGYWPTVNPYKMPGTTETDAKRAD----SDTGKVLPSAFVGTSKLDD 766
Cdd:cd01083   392 TANYEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTIHLPLADlvegSWGMKRGTSNFVGGVSLGK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  767 aNATATMDFTNWNQTLTAHKSWFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESsnPYKVYVNDKEASLTEQEKDYPET 846
Cdd:cd01083   472 -YGAAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTG--PGTVYVNGKETALGEQSFTLTGG 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  847 QSVFLESsdskKNIGYFFFKKSSISMSKALQKGAWKDINEGQSDKEVENEFLTISQAHKQN--GDSYGYMLIPNVDRATF 924
Cdd:cd01083   549 SWVHLEG----DNIGYYFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLWIDHGKNptNASYAYVLLPGATREKV 624
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447116465  925 NQMIKELESSLIENNETLQSVYDAKQGVWGIVKYDDSVSTISNQFQVLKRGVYTIRKEGDEYKIAYYNP 993
Cdd:cd01083   625 KAYAKKPNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSLEITVNKPCSVMIRKESNGLKLSVSDP 693
Lyase_8_N pfam08124
Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a ...
299-621 1.46e-159

Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.


Pssm-ID: 429830  Cd Length: 323  Bit Score: 474.59  E-value: 1.46e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   299 WNGIIAGNQYYDSKNEQMAKLNQELEGKVADSLSSISSQADRIYLWEKFSNYKTSANLTATYRKLEEMAKQVTNPSSRYY 378
Cdd:pfam08124    1 WNDVLTGALQYDTFDQDLKKYLQKLDEEARKNLDTLNPAPNRLYLWDDLPNDTPSANLTTTYTRLETMAKAYTEPGSEYY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   379 QDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIKKYTDVIEKFVPDPEHFRKTTD 458
Cdd:pfam08124   81 QDEKLLATIVKGLEYMHDTVYNSNKTEYGNWWDWEIGTPQALGDTLILLHDGLSAAEITKYTAAIRHFVPDPGFRKTLRN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   459 NPFKALGGNLVDMGRVKVIAGLLRKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVLIDGLSQLL 538
Cdd:pfam08124  161 YPFRSTGANRTDIALVVLIRGLLQKDDERISQAVEALPSVFKYVSKGEGFYTDGSYIQHGNVAYTGSYGNVLLKGLGQLL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   539 PVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIHRIADMSEGETKQRLQSL 618
Cdd:pfam08124  241 NIVAGTPYAMDDPKIQILYKWVDQSYLPLIVKGEMMDMVNGRSISRANATGHEHGAETIASMLLLAKGAPENTDARLQSL 320

                   ...
gi 447116465   619 VKT 621
Cdd:pfam08124  321 IKT 323
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
1037-1067 1.11e-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: 37.45  E-value: 1.11e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 447116465  1037 LPQTGE-GQSILASLGFLLLG-AFYLFRRGKNN 1067
Cdd:TIGR01167    2 LPKTGEsGNSLLLLLGLLLLGlGGLLLRKRKKK 34
CBM_4_9 pfam02018
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
53-190 1.54e-03

Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.


Pssm-ID: 396553  Cd Length: 134  Bit Score: 39.74  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465    53 KNLVENGDFgqtEDGS-SPWTGskaqGWSAWVDQKNSSADASTRVIEAKDGAITISSPeklraAVHRMVPIEAKKKYKLR 131
Cdd:pfam02018    1 GNLIKNGTF---EDGGlDGWKA----RGGSGKATVDVTSYNGTYSLKVSGRTATWDGQ-----IIDITIRLEKGTTYTVS 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447116465   132 FKIKTDNKVG---IAKVRIIEESGKDKRLWNSATTSgTKDWQTIEADYSPTLDVDKIKLELF 190
Cdd:pfam02018   69 FWVKASSGPPqtvSVTLQITDASGNYDTVADEKVVL-TGEWTKLEGTFTIPKTASTVELYVE 129
 
Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
291-993 0e+00

Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of secreted bacterial lyase enzymes capable of acting on glycosaminoglycans, such as hyaluronan and chondroitin, in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen. These are broad-specificity glycosaminoglycan lyases which recognize uronyl residues in polysaccharides and cleave their glycosidic bonds via a beta-elimination reaction to form a double bond between C-4 and C-5 of the non-reducing terminal uronyl residues of released products. Substrates include chondroitin, chondroitin 4-sulfate, chondroitin 6-sulfate, and hyaluronic acid. Family members include chondroitin AC lyase, chondroitin abc lyase, xanthan lyase, and hyalurate lyase.


Pssm-ID: 238517 [Multi-domain]  Cd Length: 693  Bit Score: 800.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  291 TYTDRLDDWNGIIAGNQYYDSKneqMAKLNQELEGKVADSLSSISSQADRIYLWEKFSNYKTSANLTATYRKLEEMAKQV 370
Cdd:cd01083     1 EFDALRKRWADIITGNPAYDTS---MAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRLETLAKAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  371 TNPSSRYYQDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIKKYTDVIEKFVPDP 450
Cdd:cd01083    78 TTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSEELIKKYTDAIRWFVPDP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  451 EHFRkTTDNPFKALGGNLVDMGRVKVIAGLLRKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVL 530
Cdd:cd01083   158 EHQR-TKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTEGDGFYADGSFIQHGGVPYTGGYGNVL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  531 IDGLSQLLPVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIHRIADMSEGE 610
Cdd:cd01083   237 LKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKA 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  611 TKQRLQSLVKTIVQSDSYYDVFKNLKTYKDIslmQSLLSDAGVASVPRTSYLSAFNKMDKTAMYNAekGFGFGLSLFSSR 690
Cdd:cd01083   317 LAAALRSLIKRWITRDTYYPVFNNPKSYSDI---KLLLADASIAPAAEPQGHKQFNSMDRAVHRRP--DFAFGLSMYSTR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  691 TLNYEHMNKENKRGWYTSDGMFYLYNGDLSHYSDGYWPTVNPYKMPGTTETDAKRAD----SDTGKVLPSAFVGTSKLDD 766
Cdd:cd01083   392 TANYEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTIHLPLADlvegSWGMKRGTSNFVGGVSLGK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  767 aNATATMDFTNWNQTLTAHKSWFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESsnPYKVYVNDKEASLTEQEKDYPET 846
Cdd:cd01083   472 -YGAAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTG--PGTVYVNGKETALGEQSFTLTGG 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465  847 QSVFLESsdskKNIGYFFFKKSSISMSKALQKGAWKDINEGQSDKEVENEFLTISQAHKQN--GDSYGYMLIPNVDRATF 924
Cdd:cd01083   549 SWVHLEG----DNIGYYFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLWIDHGKNptNASYAYVLLPGATREKV 624
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447116465  925 NQMIKELESSLIENNETLQSVYDAKQGVWGIVKYDDSVSTISNQFQVLKRGVYTIRKEGDEYKIAYYNP 993
Cdd:cd01083   625 KAYAKKPNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSLEITVNKPCSVMIRKESNGLKLSVSDP 693
Lyase_8_N pfam08124
Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a ...
299-621 1.46e-159

Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.


Pssm-ID: 429830  Cd Length: 323  Bit Score: 474.59  E-value: 1.46e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   299 WNGIIAGNQYYDSKNEQMAKLNQELEGKVADSLSSISSQADRIYLWEKFSNYKTSANLTATYRKLEEMAKQVTNPSSRYY 378
Cdd:pfam08124    1 WNDVLTGALQYDTFDQDLKKYLQKLDEEARKNLDTLNPAPNRLYLWDDLPNDTPSANLTTTYTRLETMAKAYTEPGSEYY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   379 QDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAINNTLSLMKEYFSDEEIKKYTDVIEKFVPDPEHFRKTTD 458
Cdd:pfam08124   81 QDEKLLATIVKGLEYMHDTVYNSNKTEYGNWWDWEIGTPQALGDTLILLHDGLSAAEITKYTAAIRHFVPDPGFRKTLRN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   459 NPFKALGGNLVDMGRVKVIAGLLRKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVLIDGLSQLL 538
Cdd:pfam08124  161 YPFRSTGANRTDIALVVLIRGLLQKDDERISQAVEALPSVFKYVSKGEGFYTDGSYIQHGNVAYTGSYGNVLLKGLGQLL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   539 PVIQKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIHRIADMSEGETKQRLQSL 618
Cdd:pfam08124  241 NIVAGTPYAMDDPKIQILYKWVDQSYLPLIVKGEMMDMVNGRSISRANATGHEHGAETIASMLLLAKGAPENTDARLQSL 320

                   ...
gi 447116465   619 VKT 621
Cdd:pfam08124  321 IKT 323
Lyase_8 pfam02278
Polysaccharide lyase family 8, super-sandwich domain; This family consists of a group of ...
664-920 7.85e-87

Polysaccharide lyase family 8, super-sandwich domain; This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.


Pssm-ID: 460521  Cd Length: 249  Bit Score: 279.93  E-value: 7.85e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   664 AFNKMDKTAMYNaeKGFGFGLSLFSSRTLNYEHMNKENKRGWYTSDGMFYLYNGDlSHYSDgYWPTVNPYKMPGTTETDA 743
Cdd:pfam02278    3 HFWAMDYMVHRR--PGYVFSLKMASSRTANYECGNGENLKGWHTGDGMTYLYLTG-DEYFD-IWPTWDWYRLPGTTVDQG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   744 KRADSDTGKVLPSAFVGTSKlDDANATATMDFTNWNQTLTAHKSWFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESSN 823
Cdd:pfam02278   79 ATALPCTGYTGKSDFVGGVS-DGEYGAAGMDLTNPGSTLTAKKSWFFFDDEIVCLGAGITSSDGRAVETTVDQRKLNGPG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465   824 PYKVyVNDKEASLTEQEKDYPETQSVFlessdsKKNIGYFFFKKSSISMSKALQKGAWKDINEGQSDKEVENEFLTISQA 903
Cdd:pfam02278  158 TATL-VDGKAKSSQGSSATLTGVRWLH------HDNIGYVFPDGANLSVSREERTGSWSDINTSSSTGEVTRDVFTLWLD 230
                          250
                   ....*....|....*....
gi 447116465   904 HKQN--GDSYGYMLIPNVD 920
Cdd:pfam02278  231 HGVNptNASYAYIVLPGAS 249
Lyase_8_C pfam02884
Polysaccharide lyase family 8, C-terminal beta-sandwich domain; This family consists of a ...
934-1001 1.35e-13

Polysaccharide lyase family 8, C-terminal beta-sandwich domain; This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.


Pssm-ID: 460736 [Multi-domain]  Cd Length: 69  Bit Score: 66.49  E-value: 1.35e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447116465   934 SLIENNETLQSVYDAKQGVWGIVKYDD-SVSTISNQFQVLKRGVYTIRKEGDEYKIAYYNPETQESAPD 1001
Cdd:pfam02884    1 EVLANTADVQAVRDKGLGLTAAVFWTAgTVTLIGLSLTVDKPAAVLVQKDGGTYTISVSDPTQTQSTVT 69
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
1037-1067 1.11e-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: 37.45  E-value: 1.11e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 447116465  1037 LPQTGE-GQSILASLGFLLLG-AFYLFRRGKNN 1067
Cdd:TIGR01167    2 LPKTGEsGNSLLLLLGLLLLGlGGLLLRKRKKK 34
CBM_4_9 pfam02018
Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.
53-190 1.54e-03

Carbohydrate binding domain; This family includes diverse carbohydrate binding domains.


Pssm-ID: 396553  Cd Length: 134  Bit Score: 39.74  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447116465    53 KNLVENGDFgqtEDGS-SPWTGskaqGWSAWVDQKNSSADASTRVIEAKDGAITISSPeklraAVHRMVPIEAKKKYKLR 131
Cdd:pfam02018    1 GNLIKNGTF---EDGGlDGWKA----RGGSGKATVDVTSYNGTYSLKVSGRTATWDGQ-----IIDITIRLEKGTTYTVS 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447116465   132 FKIKTDNKVG---IAKVRIIEESGKDKRLWNSATTSgTKDWQTIEADYSPTLDVDKIKLELF 190
Cdd:pfam02018   69 FWVKASSGPPqtvSVTLQITDASGNYDTVADEKVVL-TGEWTKLEGTFTIPKTASTVELYVE 129
 
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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