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Conserved domains on  [gi|446144418|ref|WP_000222273|]
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polysaccharide lyase 8 family protein [Staphylococcus aureus]

Protein Classification

polysaccharide lyase 8 family protein( domain architecture ID 10099508)

polysaccharide lyase 8 family protein similar to hyaluronate lyase that cleaves hyaluronate chains at a beta-D-GlcNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine

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 ...
48-770 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: 637.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  48 DYEKLRNTWLDVNYGYNKYDennDAMKKKFEATEKEAEKLLSSMKTESGRTYLWAgAENLETNSSHMTRTYRNIEKIAEA 127
Cdd:cd01083    1 EFDALRKRWADIITGNPAYD---TSMAKAITLLDEKARDNLSDLDPASSRTGVWY-DKDNFEDSANLTATYRRLETLAKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 128 MKHKNTKL-KTDENKTKVKDALEWLHENAYgkepdkkvadlktnfsksAPQKNTNLNWWDYEIGTPRALTNTLILLNGDI 206
Cdd:cd01083   77 YTTPGSTYyQDEELKSDILDALDYLYDQGY------------------NDGKGSYGNWWDWEIGIPRALNNTLVLMYDEL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 207 SSDEKKKYTAPIKTFAPKSdEILSSVGKAEPAKGGNLVDISKVKLLESIIEEDTTMMKESIVAFNKVFTYVQsnatdkER 286
Cdd:cd01083  139 SEELIKKYTDAIRWFVPDP-EHQRTKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVT------EG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 287 NGFYKDGSYIDHKDVPYTGAYGVVLLEGISQMMPMIKETPFNDKTQNNTTLKSWIDDGFLPLIYKGEMMDLSRGRAISRE 366
Cdd:cd01083  212 DGFYADGSFIQHGGVPYTGGYGNVLLKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRS 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 367 NETSHTASATVMKSLLRLSDTMDDSTKTKYKQIIKTSVKSDSSYNQNDYLNSYSDIdkmKKLIDDKSITTNDLTQQLKIY 446
Cdd:cd01083  292 NAQSHAVGVEILASLLLLADAAPKALAAALRSLIKRWITRDTYYPVFNNPKSYSDI---KLLLADASIAPAAEPQGHKQF 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 447 NDMDRVTYHNKdlDFAFGLSMTSKNVARYESINGENLKGWHTGAGMSYLYNSDVKHYRDNFWATADMKRLAGTTT----L 522
Cdd:cd01083  369 NSMDRAVHRRP--DFAFGLSMYSTRTANYEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTihlpL 446
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 523 DNEEPKSTDVKKSSKTFVGGTKfDDQHASIGMDFENQDKTLTAKKSYFILNDKIVFLGTGIKSTDSSkNPVTTIENRKAN 602
Cdd:cd01083  447 ADLVEGSWGMKRGTSNFVGGVS-LGKYGAAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGA-PVETTVDQRKLT 524
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 603 G-YTLYTDDKQTTAS----DNQGTNSVFLEStnkpkNNIGYHFLNKPKITVTKETHTGNWKEINKSQKDTQKTDEYYEVT 677
Cdd:cd01083  525 GpGTVYVNGKETALGeqsfTLTGGSWVHLEG-----DNIGYYFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLW 599
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 678 QKHS--NSDNKYGYVLYPGLSKDVFKSKASQ--VTVVKQDDDFHVVKDNE-SVWAGVNYSDSTqnfeINGTKVEVKAKGM 752
Cdd:cd01083  600 IDHGknPTNASYAYVLLPGATREKVKAYAKKpnVEVLENDETAQAVYDNTlGVTGANFWKDGT----STLSLEITVNKPC 675
                        730
                 ....*....|....*...
gi 446144418 753 FILKKKDDNTYECSFYNP 770
Cdd:cd01083  676 SVMIRKESNGLKLSVSDP 693
 
Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
48-770 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: 637.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  48 DYEKLRNTWLDVNYGYNKYDennDAMKKKFEATEKEAEKLLSSMKTESGRTYLWAgAENLETNSSHMTRTYRNIEKIAEA 127
Cdd:cd01083    1 EFDALRKRWADIITGNPAYD---TSMAKAITLLDEKARDNLSDLDPASSRTGVWY-DKDNFEDSANLTATYRRLETLAKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 128 MKHKNTKL-KTDENKTKVKDALEWLHENAYgkepdkkvadlktnfsksAPQKNTNLNWWDYEIGTPRALTNTLILLNGDI 206
Cdd:cd01083   77 YTTPGSTYyQDEELKSDILDALDYLYDQGY------------------NDGKGSYGNWWDWEIGIPRALNNTLVLMYDEL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 207 SSDEKKKYTAPIKTFAPKSdEILSSVGKAEPAKGGNLVDISKVKLLESIIEEDTTMMKESIVAFNKVFTYVQsnatdkER 286
Cdd:cd01083  139 SEELIKKYTDAIRWFVPDP-EHQRTKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVT------EG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 287 NGFYKDGSYIDHKDVPYTGAYGVVLLEGISQMMPMIKETPFNDKTQNNTTLKSWIDDGFLPLIYKGEMMDLSRGRAISRE 366
Cdd:cd01083  212 DGFYADGSFIQHGGVPYTGGYGNVLLKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRS 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 367 NETSHTASATVMKSLLRLSDTMDDSTKTKYKQIIKTSVKSDSSYNQNDYLNSYSDIdkmKKLIDDKSITTNDLTQQLKIY 446
Cdd:cd01083  292 NAQSHAVGVEILASLLLLADAAPKALAAALRSLIKRWITRDTYYPVFNNPKSYSDI---KLLLADASIAPAAEPQGHKQF 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 447 NDMDRVTYHNKdlDFAFGLSMTSKNVARYESINGENLKGWHTGAGMSYLYNSDVKHYRDNFWATADMKRLAGTTT----L 522
Cdd:cd01083  369 NSMDRAVHRRP--DFAFGLSMYSTRTANYEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTihlpL 446
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 523 DNEEPKSTDVKKSSKTFVGGTKfDDQHASIGMDFENQDKTLTAKKSYFILNDKIVFLGTGIKSTDSSkNPVTTIENRKAN 602
Cdd:cd01083  447 ADLVEGSWGMKRGTSNFVGGVS-LGKYGAAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGA-PVETTVDQRKLT 524
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 603 G-YTLYTDDKQTTAS----DNQGTNSVFLEStnkpkNNIGYHFLNKPKITVTKETHTGNWKEINKSQKDTQKTDEYYEVT 677
Cdd:cd01083  525 GpGTVYVNGKETALGeqsfTLTGGSWVHLEG-----DNIGYYFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLW 599
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 678 QKHS--NSDNKYGYVLYPGLSKDVFKSKASQ--VTVVKQDDDFHVVKDNE-SVWAGVNYSDSTqnfeINGTKVEVKAKGM 752
Cdd:cd01083  600 IDHGknPTNASYAYVLLPGATREKVKAYAKKpnVEVLENDETAQAVYDNTlGVTGANFWKDGT----STLSLEITVNKPC 675
                        730
                 ....*....|....*...
gi 446144418 753 FILKKKDDNTYECSFYNP 770
Cdd:cd01083  676 SVMIRKESNGLKLSVSDP 693
Lyase_8_N pfam08124
Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a ...
56-402 8.82e-83

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: 267.35  E-value: 8.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418   56 WLDVNYGYNKYDENNDAMKKKFEATEKEAEKLLSSMKTESGRTYLWAGAENLeTNSSHMTRTYRNIEKIAEAMKHKNTKL 135
Cdd:pfam08124   1 WNDVLTGALQYDTFDQDLKKYLQKLDEEARKNLDTLNPAPNRLYLWDDLPND-TPSANLTTTYTRLETMAKAYTEPGSEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  136 KTDENK-TKVKDALEWLHENAYGkepdkkvadlktnfsksaPQKNTNLNWWDYEIGTPRALTNTLILLNGDISSDEKKKY 214
Cdd:pfam08124  80 YQDEKLlATIVKGLEYMHDTVYN------------------SNKTEYGNWWDWEIGTPQALGDTLILLHDGLSAAEITKY 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  215 TAPIKTFAPKSDEILSSVGKAEPAKGGNLVDISKVKLLESIIEEDTTMMKESIVAFNKVFTYVQSNatdkerNGFYKDGS 294
Cdd:pfam08124 142 TAAIRHFVPDPGFRKTLRNYPFRSTGANRTDIALVVLIRGLLQKDDERISQAVEALPSVFKYVSKG------EGFYTDGS 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  295 YIDHKDVPYTGAYGVVLLEGISQMMPMIKETPFNDKTQNNTTLKSWIDDGFLPLIYKGEMMDLSRGRAISRENETSHTAS 374
Cdd:pfam08124 216 YIQHGNVAYTGSYGNVLLKGLGQLLNIVAGTPYAMDDPKIQILYKWVDQSYLPLIVKGEMMDMVNGRSISRANATGHEHG 295
                         330       340
                  ....*....|....*....|....*...
gi 446144418  375 ATVMKSLLRLSDTMDDSTKTKYKQIIKT 402
Cdd:pfam08124 296 AETIASMLLLAKGAPENTDARLQSLIKT 323
 
Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
48-770 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: 637.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  48 DYEKLRNTWLDVNYGYNKYDennDAMKKKFEATEKEAEKLLSSMKTESGRTYLWAgAENLETNSSHMTRTYRNIEKIAEA 127
Cdd:cd01083    1 EFDALRKRWADIITGNPAYD---TSMAKAITLLDEKARDNLSDLDPASSRTGVWY-DKDNFEDSANLTATYRRLETLAKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 128 MKHKNTKL-KTDENKTKVKDALEWLHENAYgkepdkkvadlktnfsksAPQKNTNLNWWDYEIGTPRALTNTLILLNGDI 206
Cdd:cd01083   77 YTTPGSTYyQDEELKSDILDALDYLYDQGY------------------NDGKGSYGNWWDWEIGIPRALNNTLVLMYDEL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 207 SSDEKKKYTAPIKTFAPKSdEILSSVGKAEPAKGGNLVDISKVKLLESIIEEDTTMMKESIVAFNKVFTYVQsnatdkER 286
Cdd:cd01083  139 SEELIKKYTDAIRWFVPDP-EHQRTKPNPITSTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVT------EG 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 287 NGFYKDGSYIDHKDVPYTGAYGVVLLEGISQMMPMIKETPFNDKTQNNTTLKSWIDDGFLPLIYKGEMMDLSRGRAISRE 366
Cdd:cd01083  212 DGFYADGSFIQHGGVPYTGGYGNVLLKGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRS 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 367 NETSHTASATVMKSLLRLSDTMDDSTKTKYKQIIKTSVKSDSSYNQNDYLNSYSDIdkmKKLIDDKSITTNDLTQQLKIY 446
Cdd:cd01083  292 NAQSHAVGVEILASLLLLADAAPKALAAALRSLIKRWITRDTYYPVFNNPKSYSDI---KLLLADASIAPAAEPQGHKQF 368
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 447 NDMDRVTYHNKdlDFAFGLSMTSKNVARYESINGENLKGWHTGAGMSYLYNSDVKHYRDNFWATADMKRLAGTTT----L 522
Cdd:cd01083  369 NSMDRAVHRRP--DFAFGLSMYSTRTANYEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTihlpL 446
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 523 DNEEPKSTDVKKSSKTFVGGTKfDDQHASIGMDFENQDKTLTAKKSYFILNDKIVFLGTGIKSTDSSkNPVTTIENRKAN 602
Cdd:cd01083  447 ADLVEGSWGMKRGTSNFVGGVS-LGKYGAAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGA-PVETTVDQRKLT 524
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 603 G-YTLYTDDKQTTAS----DNQGTNSVFLEStnkpkNNIGYHFLNKPKITVTKETHTGNWKEINKSQKDTQKTDEYYEVT 677
Cdd:cd01083  525 GpGTVYVNGKETALGeqsfTLTGGSWVHLEG-----DNIGYYFPKGATLSVSKEERTGAWKDINANGSDKEVTGNFFTLW 599
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418 678 QKHS--NSDNKYGYVLYPGLSKDVFKSKASQ--VTVVKQDDDFHVVKDNE-SVWAGVNYSDSTqnfeINGTKVEVKAKGM 752
Cdd:cd01083  600 IDHGknPTNASYAYVLLPGATREKVKAYAKKpnVEVLENDETAQAVYDNTlGVTGANFWKDGT----STLSLEITVNKPC 675
                        730
                 ....*....|....*...
gi 446144418 753 FILKKKDDNTYECSFYNP 770
Cdd:cd01083  676 SVMIRKESNGLKLSVSDP 693
Lyase_8_N pfam08124
Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a ...
56-402 8.82e-83

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: 267.35  E-value: 8.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418   56 WLDVNYGYNKYDENNDAMKKKFEATEKEAEKLLSSMKTESGRTYLWAGAENLeTNSSHMTRTYRNIEKIAEAMKHKNTKL 135
Cdd:pfam08124   1 WNDVLTGALQYDTFDQDLKKYLQKLDEEARKNLDTLNPAPNRLYLWDDLPND-TPSANLTTTYTRLETMAKAYTEPGSEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  136 KTDENK-TKVKDALEWLHENAYGkepdkkvadlktnfsksaPQKNTNLNWWDYEIGTPRALTNTLILLNGDISSDEKKKY 214
Cdd:pfam08124  80 YQDEKLlATIVKGLEYMHDTVYN------------------SNKTEYGNWWDWEIGTPQALGDTLILLHDGLSAAEITKY 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  215 TAPIKTFAPKSDEILSSVGKAEPAKGGNLVDISKVKLLESIIEEDTTMMKESIVAFNKVFTYVQSNatdkerNGFYKDGS 294
Cdd:pfam08124 142 TAAIRHFVPDPGFRKTLRNYPFRSTGANRTDIALVVLIRGLLQKDDERISQAVEALPSVFKYVSKG------EGFYTDGS 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  295 YIDHKDVPYTGAYGVVLLEGISQMMPMIKETPFNDKTQNNTTLKSWIDDGFLPLIYKGEMMDLSRGRAISRENETSHTAS 374
Cdd:pfam08124 216 YIQHGNVAYTGSYGNVLLKGLGQLLNIVAGTPYAMDDPKIQILYKWVDQSYLPLIVKGEMMDMVNGRSISRANATGHEHG 295
                         330       340
                  ....*....|....*....|....*...
gi 446144418  375 ATVMKSLLRLSDTMDDSTKTKYKQIIKT 402
Cdd:pfam08124 296 AETIASMLLLAKGAPENTDARLQSLIKT 323
Lyase_8 pfam02278
Polysaccharide lyase family 8, super-sandwich domain; This family consists of a group of ...
444-696 8.84e-83

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: 264.52  E-value: 8.84e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  444 KIYNDMDRVTYHNKDldFAFGLSMTSKNVARYESINGENLKGWHTGAGMSYLYNSDvKHYrDNFWATADMKRLAGTTTLD 523
Cdd:pfam02278   2 RHFWAMDYMVHRRPG--YVFSLKMASSRTANYECGNGENLKGWHTGDGMTYLYLTG-DEY-FDIWPTWDWYRLPGTTVDQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  524 NEEPKSTDVKKSSKTFVGGTKfDDQHASIGMDFENQDKTLTAKKSYFILNDKIVFLGTGIKSTDSSkNPVTTIENRKANG 603
Cdd:pfam02278  78 GATALPCTGYTGKSDFVGGVS-DGEYGAAGMDLTNPGSTLTAKKSWFFFDDEIVCLGAGITSSDGR-AVETTVDQRKLNG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446144418  604 YTLYTDDKQTTASDnQGTNSVFLESTNKPKNNIGYHFLNKPKITVTKETHTGNWKEINKSQKDTQKTDEYYEVTQKH--S 681
Cdd:pfam02278 156 PGTATLVDGKAKSS-QGSSATLTGVRWLHHDNIGYVFPDGANLSVSREERTGSWSDINTSSSTGEVTRDVFTLWLDHgvN 234
                         250
                  ....*....|....*
gi 446144418  682 NSDNKYGYVLYPGLS 696
Cdd:pfam02278 235 PTNASYAYIVLPGAS 249
 
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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