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Conserved domains on  [gi|925177398|gb|ALC80364|]
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hypothetical protein AM592_01170 [Bacillus gobiensis]

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 ...
38-731 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: 745.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  38 EFEQLRGKWKEMLTGGEAFDPSdpdIANRIKKIDEAANEYWNSMDKSSDRSALWTDLTGTSNSSYITKSYDRLLAMALAL 117
Cdd:cd01083    1 EFDALRKRWADIITGNPAYDTS---MAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRLETLAKAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 118 STKGSSLENNETLKNDLIQALDWMYTYRYNENKPPYNNWWDWEIGTPLRLNNIVILLYSHLSTQQITNYMKAVEKFSPTP 197
Cdd:cd01083   78 TTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSEELIKKYTDAIRWFVPDP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 198 TG----------TGANRVWKVTVVAVRGMIVEDSSKLSKARDGLSNVFTYVTSGDGFYKDGSFIQHNNFAYNGGYGRSML 267
Cdd:cd01083  158 EHqrtkpnpitsTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTEGDGFYADGSFIQHGGVPYTGGYGNVLL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 268 ADIANVMYLLSDSTWQITDSNQQNVYRWVYDSFEPLIYKGAMMDMVRGRELSRHYAEDHVVGHETIQAIIRLAQSASESN 347
Cdd:cd01083  238 KGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKAL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 348 SLVYKEMVKSWIKEDTHLDFVKNTPSINMIQLaksIVNDPAIGSRKI-IKYQQFSSMDRAVLVRDKFAFGISMSSARIAN 426
Cdd:cd01083  318 AAALRSLIKRWITRDTYYPVFNNPKSYSDIKL---LLADASIAPAAEpQGHKQFNSMDRAVHRRPDFAFGLSMYSTRTAN 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 427 YESINGENLKGWYTGEGMTYLYNNDTAQYSDGYWPTVNPYRLPGTTVDTRQRTN---SSGHAYASSKRWVGGTEmQGTYG 503
Cdd:cd01083  395 YEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTIHLPLADlveGSWGMKRGTSNFVGGVS-LGKYG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 504 VSGMTLDAYNSTLDAKKSWFMFDDEIVAVGSGITSTDQRTIETIIENRKLKNSGdnTLIVNGyKKPAATGWTEKMDKVRW 583
Cdd:cd01083  474 AAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTGPG--TVYVNG-KETALGEQSFTLTGGSW 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 584 AYLSGNvesaNIGYYFPDQPTIKGLRESRTGAWSQIDsrSGIPTESITRNYLNLWFDHGVNPTNQKYSYVLLPNMTSTSV 663
Cdd:cd01083  551 VHLEGD----NIGYYFPKGATLSVSKEERTGAWKDIN--ANGSDKEVTGNFFTLWIDHGKNPTNASYAYVLLPGATREKV 624
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925177398 664 LDYSCKPEISIVENSADAHAVKEKTLNLIGINFWNDKVKTVG-GITSDKKASVMVRETESQLEVSVSDP 731
Cdd:cd01083  625 KAYAKKPNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSlEITVNKPCSVMIRKESNGLKLSVSDP 693
 
Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
38-731 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: 745.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  38 EFEQLRGKWKEMLTGGEAFDPSdpdIANRIKKIDEAANEYWNSMDKSSDRSALWTDLTGTSNSSYITKSYDRLLAMALAL 117
Cdd:cd01083    1 EFDALRKRWADIITGNPAYDTS---MAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRLETLAKAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 118 STKGSSLENNETLKNDLIQALDWMYTYRYNENKPPYNNWWDWEIGTPLRLNNIVILLYSHLSTQQITNYMKAVEKFSPTP 197
Cdd:cd01083   78 TTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSEELIKKYTDAIRWFVPDP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 198 TG----------TGANRVWKVTVVAVRGMIVEDSSKLSKARDGLSNVFTYVTSGDGFYKDGSFIQHNNFAYNGGYGRSML 267
Cdd:cd01083  158 EHqrtkpnpitsTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTEGDGFYADGSFIQHGGVPYTGGYGNVLL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 268 ADIANVMYLLSDSTWQITDSNQQNVYRWVYDSFEPLIYKGAMMDMVRGRELSRHYAEDHVVGHETIQAIIRLAQSASESN 347
Cdd:cd01083  238 KGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKAL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 348 SLVYKEMVKSWIKEDTHLDFVKNTPSINMIQLaksIVNDPAIGSRKI-IKYQQFSSMDRAVLVRDKFAFGISMSSARIAN 426
Cdd:cd01083  318 AAALRSLIKRWITRDTYYPVFNNPKSYSDIKL---LLADASIAPAAEpQGHKQFNSMDRAVHRRPDFAFGLSMYSTRTAN 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 427 YESINGENLKGWYTGEGMTYLYNNDTAQYSDGYWPTVNPYRLPGTTVDTRQRTN---SSGHAYASSKRWVGGTEmQGTYG 503
Cdd:cd01083  395 YEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTIHLPLADlveGSWGMKRGTSNFVGGVS-LGKYG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 504 VSGMTLDAYNSTLDAKKSWFMFDDEIVAVGSGITSTDQRTIETIIENRKLKNSGdnTLIVNGyKKPAATGWTEKMDKVRW 583
Cdd:cd01083  474 AAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTGPG--TVYVNG-KETALGEQSFTLTGGSW 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 584 AYLSGNvesaNIGYYFPDQPTIKGLRESRTGAWSQIDsrSGIPTESITRNYLNLWFDHGVNPTNQKYSYVLLPNMTSTSV 663
Cdd:cd01083  551 VHLEGD----NIGYYFPKGATLSVSKEERTGAWKDIN--ANGSDKEVTGNFFTLWIDHGKNPTNASYAYVLLPGATREKV 624
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925177398 664 LDYSCKPEISIVENSADAHAVKEKTLNLIGINFWNDKVKTVG-GITSDKKASVMVRETESQLEVSVSDP 731
Cdd:cd01083  625 KAYAKKPNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSlEITVNKPCSVMIRKESNGLKLSVSDP 693
Lyase_8_N pfam08124
Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a ...
46-356 4.01e-100

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: 312.42  E-value: 4.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398   46 WKEMLTGGEAFDPSDPDIANRIKKIDEAANEYWNSMDKSSDRSALWTDLTGTSNSSYITKSYDRLLAMALALSTKGSSLE 125
Cdd:pfam08124   1 WNDVLTGALQYDTFDQDLKKYLQKLDEEARKNLDTLNPAPNRLYLWDDLPNDTPSANLTTTYTRLETMAKAYTEPGSEYY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  126 NNETLKNDLIQALDWMYTYRYNENKPPYNNWWDWEIGTPLRLNNIVILLYSHLSTQQITNYMKAVEKFSPTP-------- 197
Cdd:pfam08124  81 QDEKLLATIVKGLEYMHDTVYNSNKTEYGNWWDWEIGTPQALGDTLILLHDGLSAAEITKYTAAIRHFVPDPgfrktlrn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  198 ---TGTGANRVWKVTVVAVRGMIVEDSSKLSKARDGLSNVFTYVTSGDGFYKDGSFIQHNNFAYNGGYGRSMLADIANVM 274
Cdd:pfam08124 161 ypfRSTGANRTDIALVVLIRGLLQKDDERISQAVEALPSVFKYVSKGEGFYTDGSYIQHGNVAYTGSYGNVLLKGLGQLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  275 YLLSDSTWQITDSNQQNVYRWVYDSFEPLIYKGAMMDMVRGRELSRHYAEDHVVGHETIQAIIRLAQSASESNSLVYKEM 354
Cdd:pfam08124 241 NIVAGTPYAMDDPKIQILYKWVDQSYLPLIVKGEMMDMVNGRSISRANATGHEHGAETIASMLLLAKGAPENTDARLQSL 320

                  ..
gi 925177398  355 VK 356
Cdd:pfam08124 321 IK 322
 
Name Accession Description Interval E-value
GAG_Lyase cd01083
Glycosaminoglycan (GAG) polysaccharide lyase family. This family consists of a group of ...
38-731 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: 745.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  38 EFEQLRGKWKEMLTGGEAFDPSdpdIANRIKKIDEAANEYWNSMDKSSDRSALWTDLTGTSNSSYITKSYDRLLAMALAL 117
Cdd:cd01083    1 EFDALRKRWADIITGNPAYDTS---MAKAITLLDEKARDNLSDLDPASSRTGVWYDKDNFEDSANLTATYRRLETLAKAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 118 STKGSSLENNETLKNDLIQALDWMYTYRYNENKPPYNNWWDWEIGTPLRLNNIVILLYSHLSTQQITNYMKAVEKFSPTP 197
Cdd:cd01083   78 TTPGSTYYQDEELKSDILDALDYLYDQGYNDGKGSYGNWWDWEIGIPRALNNTLVLMYDELSEELIKKYTDAIRWFVPDP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 198 TG----------TGANRVWKVTVVAVRGMIVEDSSKLSKARDGLSNVFTYVTSGDGFYKDGSFIQHNNFAYNGGYGRSML 267
Cdd:cd01083  158 EHqrtkpnpitsTGANRVDLARVVLIRGLLEKDAVKLKQASDGLSSVLQYVTEGDGFYADGSFIQHGGVPYTGGYGNVLL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 268 ADIANVMYLLSDSTWQITDSNQQNVYRWVYDSFEPLIYKGAMMDMVRGRELSRHYAEDHVVGHETIQAIIRLAQSASESN 347
Cdd:cd01083  238 KGLSQLLYLLSGTPFEVSDEARSNLYKWILEAYAPLIYKGEMMDMVRGRSISRSNAQSHAVGVEILASLLLLADAAPKAL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 348 SLVYKEMVKSWIKEDTHLDFVKNTPSINMIQLaksIVNDPAIGSRKI-IKYQQFSSMDRAVLVRDKFAFGISMSSARIAN 426
Cdd:cd01083  318 AAALRSLIKRWITRDTYYPVFNNPKSYSDIKL---LLADASIAPAAEpQGHKQFNSMDRAVHRRPDFAFGLSMYSTRTAN 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 427 YESINGENLKGWYTGEGMTYLYNNDTAQYSDGYWPTVNPYRLPGTTVDTRQRTN---SSGHAYASSKRWVGGTEmQGTYG 503
Cdd:cd01083  395 YEAGNGENLKGWYTGDGMTYLYNNDGDQYSDFYWPTWDWYRLPGTTTIHLPLADlveGSWGMKRGTSNFVGGVS-LGKYG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 504 VSGMTLDAYNSTLDAKKSWFMFDDEIVAVGSGITSTDQRTIETIIENRKLKNSGdnTLIVNGyKKPAATGWTEKMDKVRW 583
Cdd:cd01083  474 AAGMDLDNWDQSLTAKKSWFFLDDEIVALGSGITNTSGAPVETTVDQRKLTGPG--TVYVNG-KETALGEQSFTLTGGSW 550
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398 584 AYLSGNvesaNIGYYFPDQPTIKGLRESRTGAWSQIDsrSGIPTESITRNYLNLWFDHGVNPTNQKYSYVLLPNMTSTSV 663
Cdd:cd01083  551 VHLEGD----NIGYYFPKGATLSVSKEERTGAWKDIN--ANGSDKEVTGNFFTLWIDHGKNPTNASYAYVLLPGATREKV 624
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 925177398 664 LDYSCKPEISIVENSADAHAVKEKTLNLIGINFWNDKVKTVG-GITSDKKASVMVRETESQLEVSVSDP 731
Cdd:cd01083  625 KAYAKKPNVEVLENDETAQAVYDNTLGVTGANFWKDGTSTLSlEITVNKPCSVMIRKESNGLKLSVSDP 693
Lyase_8_N pfam08124
Polysaccharide lyase family 8, N terminal alpha-helical domain; This family consists of a ...
46-356 4.01e-100

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: 312.42  E-value: 4.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398   46 WKEMLTGGEAFDPSDPDIANRIKKIDEAANEYWNSMDKSSDRSALWTDLTGTSNSSYITKSYDRLLAMALALSTKGSSLE 125
Cdd:pfam08124   1 WNDVLTGALQYDTFDQDLKKYLQKLDEEARKNLDTLNPAPNRLYLWDDLPNDTPSANLTTTYTRLETMAKAYTEPGSEYY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  126 NNETLKNDLIQALDWMYTYRYNENKPPYNNWWDWEIGTPLRLNNIVILLYSHLSTQQITNYMKAVEKFSPTP-------- 197
Cdd:pfam08124  81 QDEKLLATIVKGLEYMHDTVYNSNKTEYGNWWDWEIGTPQALGDTLILLHDGLSAAEITKYTAAIRHFVPDPgfrktlrn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  198 ---TGTGANRVWKVTVVAVRGMIVEDSSKLSKARDGLSNVFTYVTSGDGFYKDGSFIQHNNFAYNGGYGRSMLADIANVM 274
Cdd:pfam08124 161 ypfRSTGANRTDIALVVLIRGLLQKDDERISQAVEALPSVFKYVSKGEGFYTDGSYIQHGNVAYTGSYGNVLLKGLGQLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  275 YLLSDSTWQITDSNQQNVYRWVYDSFEPLIYKGAMMDMVRGRELSRHYAEDHVVGHETIQAIIRLAQSASESNSLVYKEM 354
Cdd:pfam08124 241 NIVAGTPYAMDDPKIQILYKWVDQSYLPLIVKGEMMDMVNGRSISRANATGHEHGAETIASMLLLAKGAPENTDARLQSL 320

                  ..
gi 925177398  355 VK 356
Cdd:pfam08124 321 IK 322
Lyase_8 pfam02278
Polysaccharide lyase family 8, super-sandwich domain; This family consists of a group of ...
399-657 6.37e-100

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: 309.20  E-value: 6.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  399 QFSSMDRAVLVRDKFAFGISMSSARIANYESINGENLKGWYTGEGMTYLYNNDTaQYSDgYWPTVNPYRLPGTTVDTRQR 478
Cdd:pfam02278   3 HFWAMDYMVHRRPGYVFSLKMASSRTANYECGNGENLKGWHTGDGMTYLYLTGD-EYFD-IWPTWDWYRLPGTTVDQGAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  479 TNsSGHAYASSKRWVGGTEmQGTYGVSGMTLDAYNSTLDAKKSWFMFDDEIVAVGSGITSTDQRTIETIIENRKLKNSGD 558
Cdd:pfam02278  81 AL-PCTGYTGKSDFVGGVS-DGEYGAAGMDLTNPGSTLTAKKSWFFFDDEIVCLGAGITSSDGRAVETTVDQRKLNGPGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 925177398  559 NTLIvnGYKKPAATGWTEKMDKVRWAYLSgnvesaNIGYYFPDQPTIKGLRESRTGAWSQIDSRSgiPTESITRNYLNLW 638
Cdd:pfam02278 159 ATLV--DGKAKSSQGSSATLTGVRWLHHD------NIGYVFPDGANLSVSREERTGSWSDINTSS--STGEVTRDVFTLW 228
                         250
                  ....*....|....*....
gi 925177398  639 FDHGVNPTNQKYSYVLLPN 657
Cdd:pfam02278 229 LDHGVNPTNASYAYIVLPG 247
Lyase_8_C pfam02884
Polysaccharide lyase family 8, C-terminal beta-sandwich domain; This family consists of a ...
673-738 3.83e-18

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: 79.20  E-value: 3.83e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 925177398  673 SIVENSADAHAVKEKTLNLIGINFWNDK--VKTVGGITSDKKASVMVRETESQLEVSVSDPTQINTGV 738
Cdd:pfam02884   1 EVLANTADVQAVRDKGLGLTAAVFWTAGtvTLIGLSLTVDKPAAVLVQKDGGTYTISVSDPTQTQSTV 68
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
546-616 5.91e-03

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 38.88  E-value: 5.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 925177398 546 TIIENRKLKNSGDNTLIVNGYKKPAATGWTEKMDKV---RWAYLSGNVESANIGYYFPDQPTIKG-LR-ESRTGAW 616
Cdd:cd08868   80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVslrHWGIRENCYLSSGVSVEHPAMPPTKNyVRgENGPGCW 155
 
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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