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Conserved domains on  [gi|2065338647|ref|WP_217955907|]
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glycoside hydrolase family 71/99-like protein [Alistipes timonensis]

Protein Classification

glycoside hydrolase family 71/99-like protein( domain architecture ID 10184040)

glycoside hydrolase family 71/99-like protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH99_GH71_like_3 cd11575
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
23-428 6.00e-121

Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.


:

Pssm-ID: 211416  Cd Length: 376  Bit Score: 362.81  E-value: 6.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  23 QNGKKIYADYHGVRYTRVHDGKLGRWEMHAETaksktgrktlcyNADFMDAEGRHDIAAVAYPQAGMQSNLDPDYIEYQI 102
Cdd:cd11575     4 TNSKKVYAHYMPWFETRPDDGKWGWHWTMANF------------DPDHIDASGKRQIASHYYPLIGPYSSGDPDVIEYQL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 103 LSAKAAGIDGFFIEWGFMDHENDK-LLRAMQPVAAKYGFEIGVNWCDGWlyydWITRMHPEIDTREA--KTEHYARCYQY 179
Cdd:cd11575    72 LLMKLAGIDGVIVDWYGTGHFSDYaLLKENTEALIKKLFEVGLNFADCY----EDQTIEQKVNAGKLsdKVAAAKQDLQY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 180 LVDNVLSGPTAPTVGGRPVFYLFGPGAKPAEYAYAASKVRLPegmPQPAVLRRWAewgtlEANryvpvrwspeiESWKEL 259
Cdd:cd11575   148 LADNYFTSPSYLKVDGRPLLLLFGPQFLKSEEEWTVIFSALK---PKPVFLTLWG-----ETN-----------EVGANL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 260 GMIPTAWLPARVRPMdaahpyWDHYAEPDDLIEFMKPFRDsvwmsadpaYTVKSGFAMPGMDNRGCAGWGGQHFYYIPRD 339
Cdd:cd11575   209 ADGEFAWVPARLRVS------TARLEGLDYLDNFYTNFAD---------WPIAIGSAYPGFDDFYCEGGGGGSYWYIPRN 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 340 GGRTYERMWEFSMASrdSLDMMFIASWSDYTEGHEIEPTVENGDRELRTTLHYAAQFKEMPEDASGIALPARLFDLRKRS 419
Cdd:cd11575   274 NGETFLRTLDLALAS--GLDIIQIATWNDYGEGTMIEPTVEFGYRDLETTQQFARQKKGVSYSEADLTLPLELYQLRKEA 351

                  ....*....
gi 2065338647 420 EYLASARRK 428
Cdd:cd11575   352 AFLEAIQRQ 360
 
Name Accession Description Interval E-value
GH99_GH71_like_3 cd11575
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
23-428 6.00e-121

Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.


Pssm-ID: 211416  Cd Length: 376  Bit Score: 362.81  E-value: 6.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  23 QNGKKIYADYHGVRYTRVHDGKLGRWEMHAETaksktgrktlcyNADFMDAEGRHDIAAVAYPQAGMQSNLDPDYIEYQI 102
Cdd:cd11575     4 TNSKKVYAHYMPWFETRPDDGKWGWHWTMANF------------DPDHIDASGKRQIASHYYPLIGPYSSGDPDVIEYQL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 103 LSAKAAGIDGFFIEWGFMDHENDK-LLRAMQPVAAKYGFEIGVNWCDGWlyydWITRMHPEIDTREA--KTEHYARCYQY 179
Cdd:cd11575    72 LLMKLAGIDGVIVDWYGTGHFSDYaLLKENTEALIKKLFEVGLNFADCY----EDQTIEQKVNAGKLsdKVAAAKQDLQY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 180 LVDNVLSGPTAPTVGGRPVFYLFGPGAKPAEYAYAASKVRLPegmPQPAVLRRWAewgtlEANryvpvrwspeiESWKEL 259
Cdd:cd11575   148 LADNYFTSPSYLKVDGRPLLLLFGPQFLKSEEEWTVIFSALK---PKPVFLTLWG-----ETN-----------EVGANL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 260 GMIPTAWLPARVRPMdaahpyWDHYAEPDDLIEFMKPFRDsvwmsadpaYTVKSGFAMPGMDNRGCAGWGGQHFYYIPRD 339
Cdd:cd11575   209 ADGEFAWVPARLRVS------TARLEGLDYLDNFYTNFAD---------WPIAIGSAYPGFDDFYCEGGGGGSYWYIPRN 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 340 GGRTYERMWEFSMASrdSLDMMFIASWSDYTEGHEIEPTVENGDRELRTTLHYAAQFKEMPEDASGIALPARLFDLRKRS 419
Cdd:cd11575   274 NGETFLRTLDLALAS--GLDIIQIATWNDYGEGTMIEPTVEFGYRDLETTQQFARQKKGVSYSEADLTLPLELYQLRKEA 351

                  ....*....
gi 2065338647 420 EYLASARRK 428
Cdd:cd11575   352 AFLEAIQRQ 360
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
72-379 4.24e-04

Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer.


Pssm-ID: 435273  Cd Length: 341  Bit Score: 42.96  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  72 DAEGRH----DIAAVAYPQAGMQSNLDPDYIEYQILSAKAAGIDGFFIEWGFMDHENDKLLRAMQPVAAKYGFEIgvnwc 147
Cdd:pfam16317  43 YPGARHgppdDIGSNFYPELGSYSSRDPEIIETHMRMMRSASIGVLSVSWYGENDEATRSVPTILDKAAKYGLKV----- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 148 dgwlyydwitRMHPE-IDTREAKTEHyaRCYQYLVDNVLSGPTAPTVGGRPVFYLFGP-GAKPAEYAyaasKVRLPEGmp 225
Cdd:pfam16317 118 ----------TFHIEpYNNRSDQNMH--ANIKYIIDKYGNHPAFYRYKGKPLFYVYDSyITKPSEWA----KLLTPGG-- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 226 qpAVLRRWAEWGTLEANRYVPVRWSPEIESwkelgmiptawlparvRPMDAAHPYWDH----YAEPDDLIEFMKPFRDSV 301
Cdd:pfam16317 180 --ELSVRNSPYDGLFIGLLVEEKEKYDILQ----------------SGFDGFYTYFATngftYGSTHQNWPSLKGWASKH 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065338647 302 WMSADPAYTvksgfamPGMDNRGCAGWGGQHFYyiPRDGGRTYERMweFSMASRDSLDMMFIASWSDYTEGHEIEPTV 379
Cdd:pfam16317 242 NKLFIPSVG-------PGYIDTRIRPWNGQNTR--NRENGKYYDRM--LSAALQTKPSLISITSFNEWHEGTQIEPAV 308
 
Name Accession Description Interval E-value
GH99_GH71_like_3 cd11575
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
23-428 6.00e-121

Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.


Pssm-ID: 211416  Cd Length: 376  Bit Score: 362.81  E-value: 6.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  23 QNGKKIYADYHGVRYTRVHDGKLGRWEMHAETaksktgrktlcyNADFMDAEGRHDIAAVAYPQAGMQSNLDPDYIEYQI 102
Cdd:cd11575     4 TNSKKVYAHYMPWFETRPDDGKWGWHWTMANF------------DPDHIDASGKRQIASHYYPLIGPYSSGDPDVIEYQL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 103 LSAKAAGIDGFFIEWGFMDHENDK-LLRAMQPVAAKYGFEIGVNWCDGWlyydWITRMHPEIDTREA--KTEHYARCYQY 179
Cdd:cd11575    72 LLMKLAGIDGVIVDWYGTGHFSDYaLLKENTEALIKKLFEVGLNFADCY----EDQTIEQKVNAGKLsdKVAAAKQDLQY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 180 LVDNVLSGPTAPTVGGRPVFYLFGPGAKPAEYAYAASKVRLPegmPQPAVLRRWAewgtlEANryvpvrwspeiESWKEL 259
Cdd:cd11575   148 LADNYFTSPSYLKVDGRPLLLLFGPQFLKSEEEWTVIFSALK---PKPVFLTLWG-----ETN-----------EVGANL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 260 GMIPTAWLPARVRPMdaahpyWDHYAEPDDLIEFMKPFRDsvwmsadpaYTVKSGFAMPGMDNRGCAGWGGQHFYYIPRD 339
Cdd:cd11575   209 ADGEFAWVPARLRVS------TARLEGLDYLDNFYTNFAD---------WPIAIGSAYPGFDDFYCEGGGGGSYWYIPRN 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 340 GGRTYERMWEFSMASrdSLDMMFIASWSDYTEGHEIEPTVENGDRELRTTLHYAAQFKEMPEDASGIALPARLFDLRKRS 419
Cdd:cd11575   274 NGETFLRTLDLALAS--GLDIIQIATWNDYGEGTMIEPTVEFGYRDLETTQQFARQKKGVSYSEADLTLPLELYQLRKEA 351

                  ....*....
gi 2065338647 420 EYLASARRK 428
Cdd:cd11575   352 AFLEAIQRQ 360
GH99_GH71_like cd11573
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
94-387 9.35e-15

Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity.


Pssm-ID: 211414  Cd Length: 284  Bit Score: 74.84  E-value: 9.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  94 DPDYIEYQILSAKAAGIDGFFIEWGFMD-----HENDKLLRAMQPVAAKYGFEIGVnwCDGWLYYDWItrmhpeidtreA 168
Cdd:cd11573     9 TPEVMRKHIRWAQEAGIDGFAVDWYPEAdtsplAETTAILNKALDAAEEENFTIFF--MLDPASLREA-----------G 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 169 KTEHYARCYQYLVDNVLSGPTAPTVGGRPVFYLFGPGAK--PAEYAYAASKVRLPE----GMPQPAVLRRWAEWGTLE-- 240
Cdd:cd11573    76 ELDVVLERITRLINEYRNPSSYYKVGGKPLVFIWGPGLAytASEWEALKAQLRAGCpymiGLWTPWRVPNRDMITDMFdg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 241 ANRYVPVRWSPEIESWkelGMIPTAWLPARvrpmdaahpywdhyaepddliEFMKPFRDSVWMSADPAYTvksgfampgm 320
Cdd:cd11573   156 ASPWTPWRGTNPEEAY---GHGVKNWRPDQ---------------------EWMGANGKGYIPTVSPGFS---------- 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2065338647 321 DNRGCAGWGGQhfyYIPRDGGRTYERMWEFSMASrdSLDMMFIASWSDYTEGHEIEPTVENGDRELR 387
Cdd:cd11573   202 DINRRPGDPGD---IILRRDGQRLHSMLEAALKA--GPAMIQIASWNDWGEGTYIEPCEEYGPRDRK 263
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
41-202 3.11e-04

Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear.


Pssm-ID: 211415  Cd Length: 338  Bit Score: 43.07  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  41 HDGKLGRWEmHaETAKSKTGRKTLCYnadfmdaeGRH----DIAAVAYPQAGMQSNLDPDYIEYQILSAKAAGIDGFFIE 116
Cdd:cd11574    14 FDGKYGHWN-H-KILPHWDIAKKYPQ--------GRHdppdDIGSNFYPKLGPYSSSDPSVIDDHMKQIREAGIGVVVVS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 117 W------GFMDHENDKLLRAMQPVAAKYGFEIgvnwcdGWLY--YDWITR--MHPEIdtreaktehyarcyQYLVDNVLS 186
Cdd:cd11574    84 WygpgssDDNGKPSDDTIPLLLDIAHEYGLKV------AFHIepYEGRTAasLREDI--------------KYILDKYGS 143
                         170
                  ....*....|....*....
gi 2065338647 187 GPTAPTV---GGRPVFYLF 202
Cdd:cd11574   144 HPAFYKYkkgRGLPVFYIY 162
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
72-379 4.24e-04

Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer.


Pssm-ID: 435273  Cd Length: 341  Bit Score: 42.96  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  72 DAEGRH----DIAAVAYPQAGMQSNLDPDYIEYQILSAKAAGIDGFFIEWGFMDHENDKLLRAMQPVAAKYGFEIgvnwc 147
Cdd:pfam16317  43 YPGARHgppdDIGSNFYPELGSYSSRDPEIIETHMRMMRSASIGVLSVSWYGENDEATRSVPTILDKAAKYGLKV----- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 148 dgwlyydwitRMHPE-IDTREAKTEHyaRCYQYLVDNVLSGPTAPTVGGRPVFYLFGP-GAKPAEYAyaasKVRLPEGmp 225
Cdd:pfam16317 118 ----------TFHIEpYNNRSDQNMH--ANIKYIIDKYGNHPAFYRYKGKPLFYVYDSyITKPSEWA----KLLTPGG-- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 226 qpAVLRRWAEWGTLEANRYVPVRWSPEIESwkelgmiptawlparvRPMDAAHPYWDH----YAEPDDLIEFMKPFRDSV 301
Cdd:pfam16317 180 --ELSVRNSPYDGLFIGLLVEEKEKYDILQ----------------SGFDGFYTYFATngftYGSTHQNWPSLKGWASKH 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065338647 302 WMSADPAYTvksgfamPGMDNRGCAGWGGQHFYyiPRDGGRTYERMweFSMASRDSLDMMFIASWSDYTEGHEIEPTV 379
Cdd:pfam16317 242 NKLFIPSVG-------PGYIDTRIRPWNGQNTR--NRENGKYYDRM--LSAALQTKPSLISITSFNEWHEGTQIEPAV 308
GH71 cd11577
Glycoside hydrolase family 71; This family of glycoside hydrolases 71 (following the CAZY ...
99-397 4.42e-04

Glycoside hydrolase family 71; This family of glycoside hydrolases 71 (following the CAZY nomenclature) function as alpha-1,3-glucanases (mutanases, EC 3.2.1.59). They appear to have an endo-hydrolytic mode of enzymatic activity and bacterial members are investigated as candidates for the development of dental caries treatments.The member from fission yeast, endo-alpha-1,3-glucanase Agn1p, plays a vital role in daughter cell separation, while Agn2p has been associated with endolysis of the ascus wall.


Pssm-ID: 211418  Cd Length: 283  Bit Score: 42.65  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647  99 EYQILSAKAAGIDGFFIEWGFMDHENDKLLRAMQPVAAKYGFEIGVNWcD--GWLYYDWITRMHPEIDTREAkteHYARc 176
Cdd:cd11577    25 EKDIRLAQAAGIDGFALNIGSDDSQTPTQLALAYQAAEATGFKLFLSF-DmsGGWSASDVAEVIALIATYAA---HPAY- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 177 yqylvdnvlsgptaptVGGRPVFYLFGPGAKPAeyayaaskvrlpegmpqpavlrrwAEWGTLEAN-RYVPVRWSPEIES 255
Cdd:cd11577   100 ----------------YNGKPFVSTFEGEGDNA------------------------ADWADIKAQlLGTNIFFVPDWSS 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065338647 256 WkelgmIPTAWLPARVRPMD------AAHPYWDHYAEPDDLIEFMKPFRDSVWMSadpayTVKSGFAMPgmdnrgcagWG 329
Cdd:cd11577   140 L-----GGPSALNSGLDVADglfswdAWPPGGNNDMSTDTDAAYLAALGGKPYMA-----PVSPWFYTH---------LP 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065338647 330 GQHFYYIPRDGGrTYERMWEFSMASRDslDMMFIASWSDYTEGHEIEPTVENGDRELRTTLHYAAQFK 397
Cdd:cd11577   201 GYGKNWYWRGDD-LWRDRWEQIIALQP--DFVEIITWNDYGESHYIGPLRGKANSVGDASANYVDGFP 265
 
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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