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Conserved domains on  [gi|1907156373|ref|XP_036020083|]
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myogenesis-regulating glycosidase isoform X1 [Mus musculus]

Protein Classification

glycoside hydrolase family 31 protein( domain architecture ID 10159554)

glycoside hydrolase family 31 protein similar to myogenesis-regulating glycosidase that promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
313-684 0e+00

glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


:

Pssm-ID: 269878 [Multi-domain]  Cd Length: 364  Bit Score: 562.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 313 RDPIWSTWALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHP 392
Cdd:cd06592     1 RPPIWSTWAEYKYNINQEKVLEYAEEIRANGFPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 393 FVNYNSSSFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRD 472
Cdd:cd06592    81 FINPDSPNFRELRDKGYLVKEDSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASYLPAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 473 FSTYRPLSDPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDM 552
Cdd:cd06592   161 PATFPSGLNPNEYTTLYAELAAEFGLLNEVRSGWKSQGLPLFVRMSDKDSHWGYWNGLRSLIPTALTQGLLGYPFVLPDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 553 IGGNAVPERTagrqdgpgPERELYVRWLEVAAFMPAMQFSIPPWQ-YDAEVVAIAHKFAALRASLVaPLLLELAGEITDT 631
Cdd:cd06592   241 IGGNAYGNFP--------PDKELYIRWLQLSAFMPAMQFSVAPWRnYDEEVVDIARKLAKLREKLL-PYIYELAAEAVDT 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907156373 632 GDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKW 684
Cdd:cd06592   312 GEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
 
Name Accession Description Interval E-value
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
313-684 0e+00

glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269878 [Multi-domain]  Cd Length: 364  Bit Score: 562.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 313 RDPIWSTWALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHP 392
Cdd:cd06592     1 RPPIWSTWAEYKYNINQEKVLEYAEEIRANGFPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 393 FVNYNSSSFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRD 472
Cdd:cd06592    81 FINPDSPNFRELRDKGYLVKEDSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASYLPAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 473 FSTYRPLSDPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDM 552
Cdd:cd06592   161 PATFPSGLNPNEYTTLYAELAAEFGLLNEVRSGWKSQGLPLFVRMSDKDSHWGYWNGLRSLIPTALTQGLLGYPFVLPDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 553 IGGNAVPERTagrqdgpgPERELYVRWLEVAAFMPAMQFSIPPWQ-YDAEVVAIAHKFAALRASLVaPLLLELAGEITDT 631
Cdd:cd06592   241 IGGNAYGNFP--------PDKELYIRWLQLSAFMPAMQFSVAPWRnYDEEVVDIARKLAKLREKLL-PYIYELAAEAVDT 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907156373 632 GDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKW 684
Cdd:cd06592   312 GEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
315-712 3.78e-72

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 245.84  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 315 PIWST--WALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAY--GDFNFDEGKFPNASDMFRRLRDAGFRVTLWV 390
Cdd:COG1501   169 PRWAFgyWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIRWMDKYywGDFEWDPRRFPDPKAMVKELHDRGVKLVLWI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 391 HPFVNYNSSSFGEGveRELFVREPTGRlPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEvsYLP 470
Cdd:COG1501   249 NPYVAPDSAIFAEG--MANFVKIASGT-VFVGKMWPGTTGLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNE--GWP 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 471 RDFSTYrPLSDPSVWSRRYTeMAEPFFSLAEVRVGYqSQNISCFFR-----LVDRDSVWGYDL-----GLRSLIPAVLTV 540
Cdd:COG1501   324 TDVATF-PSNVPQQMRNLYG-LLEAKATFEGFRTSR-NNRTFILTRsgfagGQRYPVIWTGDNtssweSLEDQLTQGLNL 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 541 SMLGYPFILPDMIGGNAVPERtagrqdgpgperELYVRWLEVAAFMPAMQ-----FSIPPWQYDAEVVAIAHKFAALRAS 615
Cdd:COG1501   401 SLSGVPFWTPDIGGFFGSPSR------------ELWIRWFQVGAFSPFARihgwaSSTEPWFFDEEAKQIVKEYAQLRYR 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 616 LVaPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLePGKQERDVYLPAGKWRSY-KGELFDK 694
Cdd:COG1501   469 LL-PYIYSLFAKASTDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFwTGELIEG 546
                         410
                  ....*....|....*...
gi 1907156373 695 TPVLLtdYPVDLDEVAYF 712
Cdd:COG1501   547 GQWIT--VTAPLDRLPLY 562
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
328-706 6.98e-67

Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.


Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 227.06  E-value: 6.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 328 DQNKVLQFAQQIRQHRFNSS--HLEIDdmYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSS---FG 402
Cdd:pfam01055  41 SEEEVLEVVDGFRERDIPLDviWLDID--YMDGYRDFTWDPERFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPGyppYD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 403 EGVERELFVREPTGRLpaLVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVS---YLPRDFSTYRPL 479
Cdd:pfam01055 119 EGLEKGYFVKNPDGSL--YVGGWPGMSAFPDFTNPEARDWWADQLFKFLLDMGVDGIWNDMNEPSvfcGSGPEDTVAKDN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 480 SDPSVWSRRYT------EMAEPFFSLAEVRVGYQ------------SQniscffRLV-----DRDSVWGYdlgLRSLIPA 536
Cdd:pfam01055 197 DPGGGVEHYDVhnlyglLMAKATYEGLREKRPNKrpfvltrsgfagSQ------RYAahwsgDNTSTWEH---LRFSIPG 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 537 VLTVSMLGYPFILPDmIGGNAVPertagrqdgpgPERELYVRWLEVAAFMP-----AMQFSIP--PWQYDAEVVAIAHKF 609
Cdd:pfam01055 268 GLSLGLSGIPFWGAD-IGGFFNP-----------TTPELYVRWYQLGAFSPffrnhSSIDTRRrePWLFGEEVEEIIRKA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 610 AALRASLVaPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSY-K 688
Cdd:pfam01055 336 IRLRYRLL-PYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFwT 414
                         410
                  ....*....|....*...
gi 1907156373 689 GELFDKTPVLLTDYPVDL 706
Cdd:pfam01055 415 GERYEGGGTVPVTAPLDR 432
PRK10426 PRK10426
alpha-glucosidase; Provisional
365-693 5.03e-40

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 156.31  E-value: 5.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 365 DEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGRlPALVRWWNGIGAVLDFTHPEAREWFQ 444
Cdd:PRK10426  264 DSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGDLCEEAAEKGYLAKDADGG-DYLVEFGEFYAGVVDLTNPEAYEWFK 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 445 GHLRRLRLRYNVTSFKFDAGEvsYLPRDFSTYRPLSD-------PSVWSRRYTEMAEPFFSLAEV----RVGYQ-SQNIS 512
Cdd:PRK10426  343 EVIKKNMIGLGCSGWMADFGE--YLPTDAYLHNGVSAeimhnawPALWAKCNYEALEETGKLGEIlffmRAGYTgSQKYS 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 513 CFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDmIGG-----NAVpeRTagrqdgpgpeRELYVRWLEVAAFMP 587
Cdd:PRK10426  421 TLFWAGDQNVDWSLDDGLASVVPAALSLGMSGHGLHHSD-IGGyttlfGMK--RT----------KELLLRWCEFSAFTP 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 588 AM---QFSIPP--WQYDAEVVAIAH--KFAALRASLvAPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGD 660
Cdd:PRK10426  488 VMrthEGNRPGdnWQFDSDAETIAHfaRMTRVFTTL-KPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGR 566
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1907156373 661 TLLVAPVLEPGKQERDVYLPAGKWRS-YKGELFD 693
Cdd:PRK10426  567 DLLVAPVHEEGRTDWTVYLPEDKWVHlWTGEAFA 600
 
Name Accession Description Interval E-value
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
313-684 0e+00

glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269878 [Multi-domain]  Cd Length: 364  Bit Score: 562.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 313 RDPIWSTWALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHP 392
Cdd:cd06592     1 RPPIWSTWAEYKYNINQEKVLEYAEEIRANGFPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 393 FVNYNSSSFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRD 472
Cdd:cd06592    81 FINPDSPNFRELRDKGYLVKEDSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASYLPAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 473 FSTYRPLSDPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDM 552
Cdd:cd06592   161 PATFPSGLNPNEYTTLYAELAAEFGLLNEVRSGWKSQGLPLFVRMSDKDSHWGYWNGLRSLIPTALTQGLLGYPFVLPDM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 553 IGGNAVPERTagrqdgpgPERELYVRWLEVAAFMPAMQFSIPPWQ-YDAEVVAIAHKFAALRASLVaPLLLELAGEITDT 631
Cdd:cd06592   241 IGGNAYGNFP--------PDKELYIRWLQLSAFMPAMQFSVAPWRnYDEEVVDIARKLAKLREKLL-PYIYELAAEAVDT 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907156373 632 GDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKW 684
Cdd:cd06592   312 GEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
315-712 3.78e-72

Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 245.84  E-value: 3.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 315 PIWST--WALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAY--GDFNFDEGKFPNASDMFRRLRDAGFRVTLWV 390
Cdd:COG1501   169 PRWAFgyWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIRWMDKYywGDFEWDPRRFPDPKAMVKELHDRGVKLVLWI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 391 HPFVNYNSSSFGEGveRELFVREPTGRlPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEvsYLP 470
Cdd:COG1501   249 NPYVAPDSAIFAEG--MANFVKIASGT-VFVGKMWPGTTGLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNE--GWP 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 471 RDFSTYrPLSDPSVWSRRYTeMAEPFFSLAEVRVGYqSQNISCFFR-----LVDRDSVWGYDL-----GLRSLIPAVLTV 540
Cdd:COG1501   324 TDVATF-PSNVPQQMRNLYG-LLEAKATFEGFRTSR-NNRTFILTRsgfagGQRYPVIWTGDNtssweSLEDQLTQGLNL 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 541 SMLGYPFILPDMIGGNAVPERtagrqdgpgperELYVRWLEVAAFMPAMQ-----FSIPPWQYDAEVVAIAHKFAALRAS 615
Cdd:COG1501   401 SLSGVPFWTPDIGGFFGSPSR------------ELWIRWFQVGAFSPFARihgwaSSTEPWFFDEEAKQIVKEYAQLRYR 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 616 LVaPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLePGKQERDVYLPAGKWRSY-KGELFDK 694
Cdd:COG1501   469 LL-PYIYSLFAKASTDGTPVIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFwTGELIEG 546
                         410
                  ....*....|....*...
gi 1907156373 695 TPVLLtdYPVDLDEVAYF 712
Cdd:COG1501   547 GQWIT--VTAPLDRLPLY 562
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
328-706 6.98e-67

Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.


Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 227.06  E-value: 6.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 328 DQNKVLQFAQQIRQHRFNSS--HLEIDdmYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSS---FG 402
Cdd:pfam01055  41 SEEEVLEVVDGFRERDIPLDviWLDID--YMDGYRDFTWDPERFPDPKGMVDELHAKGQKLVVIIDPGIKKVDPGyppYD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 403 EGVERELFVREPTGRLpaLVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVS---YLPRDFSTYRPL 479
Cdd:pfam01055 119 EGLEKGYFVKNPDGSL--YVGGWPGMSAFPDFTNPEARDWWADQLFKFLLDMGVDGIWNDMNEPSvfcGSGPEDTVAKDN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 480 SDPSVWSRRYT------EMAEPFFSLAEVRVGYQ------------SQniscffRLV-----DRDSVWGYdlgLRSLIPA 536
Cdd:pfam01055 197 DPGGGVEHYDVhnlyglLMAKATYEGLREKRPNKrpfvltrsgfagSQ------RYAahwsgDNTSTWEH---LRFSIPG 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 537 VLTVSMLGYPFILPDmIGGNAVPertagrqdgpgPERELYVRWLEVAAFMP-----AMQFSIP--PWQYDAEVVAIAHKF 609
Cdd:pfam01055 268 GLSLGLSGIPFWGAD-IGGFFNP-----------TTPELYVRWYQLGAFSPffrnhSSIDTRRrePWLFGEEVEEIIRKA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 610 AALRASLVaPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSY-K 688
Cdd:pfam01055 336 IRLRYRLL-PYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFwT 414
                         410
                  ....*....|....*...
gi 1907156373 689 GELFDKTPVLLTDYPVDL 706
Cdd:pfam01055 415 GERYEGGGTVPVTAPLDR 432
GH_D cd14790
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
313-608 2.95e-63

Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.


Pssm-ID: 269891 [Multi-domain]  Cd Length: 253  Bit Score: 211.33  E-value: 2.95e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 313 RDPIWSTWALHGraVDQNKVLQFAQQIRQH--RFNSSHLEIDDMYTP--AYGDFNFDEGKFPNASDMFRRLRDAGFRVTL 388
Cdd:cd14790     1 PPMGWLTWERYR--QDIDEMLFMEMADRIAedELPYKVFNIDDCWAKkdAEGDFVPDPERFPRGEAMARRLHARGLKLGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 389 WVHPFVnynsssfgegverelfvreptgrlpalvrwwngigavldfthpeaREWFQGHLRRLRlRYNVTSFKFDAGEVSY 468
Cdd:cd14790    79 WGDPFR---------------------------------------------LDWVEDDLQTLA-EWGVDMFKLDFGESSG 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 469 LPRD-FSTYRPLSDPSVWSRRYTEMAEPFfSLAEVRVGYQSQN-----ISCFFRL-VDRDSVWGYDLGLRSLIPAVLTVS 541
Cdd:cd14790   113 TPVQwFPQKMPNKEQAQGYEQMARALNAT-GEPIVYSGSWSAYqgggeICNLWRNyDDIQDSWDAVLSIVDWFFTNQDVL 191
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156373 542 ML-GYPFILPDMIGGNAVpertagrqdgpgperelyvrwLEVAAFMPAMQFSIPPWqyDAEVVAIAHK 608
Cdd:cd14790   192 QAgGFHFNDPDMLIIGNF---------------------GLSAEQSRSQMALWTIM--DAPLLMSTDL 236
PRK10426 PRK10426
alpha-glucosidase; Provisional
365-693 5.03e-40

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 156.31  E-value: 5.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 365 DEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGRlPALVRWWNGIGAVLDFTHPEAREWFQ 444
Cdd:PRK10426  264 DSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGDLCEEAAEKGYLAKDADGG-DYLVEFGEFYAGVVDLTNPEAYEWFK 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 445 GHLRRLRLRYNVTSFKFDAGEvsYLPRDFSTYRPLSD-------PSVWSRRYTEMAEPFFSLAEV----RVGYQ-SQNIS 512
Cdd:PRK10426  343 EVIKKNMIGLGCSGWMADFGE--YLPTDAYLHNGVSAeimhnawPALWAKCNYEALEETGKLGEIlffmRAGYTgSQKYS 420
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 513 CFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDmIGG-----NAVpeRTagrqdgpgpeRELYVRWLEVAAFMP 587
Cdd:PRK10426  421 TLFWAGDQNVDWSLDDGLASVVPAALSLGMSGHGLHHSD-IGGyttlfGMK--RT----------KELLLRWCEFSAFTP 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 588 AM---QFSIPP--WQYDAEVVAIAH--KFAALRASLvAPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGD 660
Cdd:PRK10426  488 VMrthEGNRPGdnWQFDSDAETIAHfaRMTRVFTTL-KPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGR 566
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1907156373 661 TLLVAPVLEPGKQERDVYLPAGKWRS-YKGELFD 693
Cdd:PRK10426  567 DLLVAPVHEEGRTDWTVYLPEDKWVHlWTGEAFA 600
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
315-613 5.61e-34

CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial 3-alpha-isomaltosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsZ. CtsY and CtsZ both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsZ belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269883 [Multi-domain]  Cd Length: 326  Bit Score: 132.82  E-value: 5.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 315 PIWS----TWALHGRavDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPA-YGDFNFDEGKFPNASDMFRRLRDAGFRVTLW 389
Cdd:cd06597     7 PKWAfghwVSANEWN--SQAEVLELVEEYLAYDIPVGAVVIEAWSDEAtFYIFNDATGKWPDPKGMIDSLHEQGIKVILW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 390 VHPFVNYN-------SSSFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFD 462
Cdd:cd06597    85 QTPVVKTDgtdhaqkSNDYAEAIAKGYYVKNGDGTPYIPEGWWFGGGSLIDFTNPEAVAWWHDQRDYLLDELGIDGFKTD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 463 AGEvSYLPRDFSTYrPLSDPSVWSRRYTEM-AEPFFSLAEV---------RVGY-QSQNISCFFrLVDRDSVWGydlGLR 531
Cdd:cd06597   165 GGE-PYWGEDLIFS-DGKKGREMRNEYPNLyYKAYFDYIREigndgvlfsRAGDsGAQRYPIGW-VGDQDSTFE---GLQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 532 SLIPAVLTVSMLGYPFILPDmIGGNAvpertagrqdGPGPERELYVRWLEVAAFMPAMQF---------------SIPPW 596
Cdd:cd06597   239 SALKAGLSAAWSGYPFWGWD-IGGFS----------GPLPTAELYLRWTQLAAFSPIMQNhseknhrpwseerrwNVAER 307
                         330
                  ....*....|....*..
gi 1907156373 597 QYDAEVVAIAHKFAALR 613
Cdd:cd06597   308 TGDPEVLDIYRKYVKLR 324
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
361-684 6.23e-33

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 135.02  E-value: 6.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 361 DFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGRLPALVRWWNGIGAVlDFTHPEAR 440
Cdd:PRK10658  316 DFEWDPRTFPDPEGMLKRLKAKGLKICVWINPYIAQKSPLFKEGKEKGYLLKRPDGSVWQWDKWQPGMAIV-DFTNPDAC 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 441 EWFQGHLRRLrLRYNVTSFKFDAGEvsYLPRDFsTYRPLSDPSVWSRRYTEM-AEPFFSLAEVRVGyqsqniscffrlvD 519
Cdd:PRK10658  395 KWYADKLKGL-LDMGVDCFKTDFGE--RIPTDV-VWFDGSDPQKMHNYYTYLyNKTVFDVLKETRG-------------E 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 520 RDSV----------------WGYDL---------GLRSlipaVLTVSMLGYPFILPDmIGGNavpERTagrqdgpgPERE 574
Cdd:PRK10658  458 GEAVlfarsatvggqqfpvhWGGDCysnyesmaeSLRG----GLSLGLSGFGFWSHD-IGGF---ENT--------ATAD 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 575 LYVRWLevaafmpamQFSI--------------PPWQYDAEVVAIAHKFAALRASLVaPLLLELAGEITDTGDPIVRPLW 640
Cdd:PRK10658  522 VYKRWC---------AFGLlsshsrlhgsksyrVPWAYDEEAVDVVRFFTKLKCRLM-PYLYREAAEAHERGTPMMRAMV 591
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1907156373 641 WIAPGDETAHRIDSQFLIGDTLLVAPVLEPgKQERDVYLPAGKW 684
Cdd:PRK10658  592 LEFPDDPACDYLDRQYMLGDSLLVAPVFSE-AGDVEYYLPEGRW 634
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
328-616 1.71e-32

alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269879 [Multi-domain]  Cd Length: 308  Bit Score: 128.07  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 328 DQNKVLQFAQQIRQHRFNSSHLEIDD--MYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGV 405
Cdd:cd06593    22 SEEEVLEVADGMRERGIPCDVIHLDCfwMKEDWWCDFEWDEERFPDPEGMIARLKEKGFKVCLWINPYISQDSPLFKEAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 406 ERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLrLRYNVTSFKFDAGEvsYLPRD---FSTYRPLSDP 482
Cdd:cd06593   102 EKGYLVKNPDGSPWHQWDGWQPGMGIIDFTNPEAVAWYKEKLKRL-LDMGVDVIKTDFGE--RIPEDavyYDGSDGRKMH 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 483 SVWSRRYTEMA-----EPFFSLAEV--RVGYQ-SQNISCFfrlvdrdsvWGYDL-----GLRSLIPAVLTVSMLGYPFIL 549
Cdd:cd06593   179 NLYPLLYNKAVyeatkEVKGEEAVLwaRSAWAgSQRYPVH---------WGGDSestfeGMAASLRGGLSLGLSGFGFWS 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156373 550 PDmIGGNavpERTagrqdgpgPERELYVRWLEVAAFMPAMQF--SIP--PWQYDAEVVAIAHKFAALRASL 616
Cdd:cd06593   250 HD-IGGF---EGT--------PSPELYKRWTQFGLLSSHSRLhgSTPrePWEYGEEALDVVRKFAKLRYRL 308
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
349-704 1.54e-30

neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely related glycosyl hydrolase family 31 (GH31) isozymes, neutral alpha-glucosidase C (GANC) and the alpha subunit of heterodimeric neutral alpha-glucosidase AB (GANAB). Initially distinguished on the basis of differences in electrophoretic mobility in starch gel, GANC and GANAB have been shown to have other differences, including those of substrate specificity. GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. The GANC/GANAB family includes the alpha-glucosidase II (ModA) from Dictyostelium discoideum as well as the alpha-glucosidase II (GLS2, or ROT2 - Reversal of TOR2 lethality protein 2) from Saccharomyces cerevisiae.


Pssm-ID: 269889  Cd Length: 467  Bit Score: 125.71  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 349 LEIDdmYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSF--GEGVERELFVREPTGRlpALVRW-W 425
Cdd:cd06603    45 LDIE--HTDGKRYFTWDKKKFPDPKKMQEKLASKGRKLVTIVDPHIKRDDDYFvyKEAKEKDYFVKDSDGK--DFEGWcW 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 426 NGIGAVLDFTHPEAREWFQGhlrrlrlRYNVTSFK-----------------FDAGEVSyLPRD---------------- 472
Cdd:cd06603   121 PGSSSWPDFLNPEVRDWWAS-------LFSYDKYKgstenlyiwndmnepsvFNGPEIT-MPKDaihyggvehrdvhniy 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 473 -----FSTYRPLsdpsvwsRRYTEMAEPFFSLAevrvgyqsqniSCFFRLVDR---------DSVWGYdlgLRSLIPAVL 538
Cdd:cd06603   193 glymhMATFEGL-------LKRSNGKKRPFVLT-----------RSFFAGSQRygavwtgdnMATWEH---LKISIPMLL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 539 TVSMLGYPFILPDMIG--GNavpertagrqdgpgPERELYVRWLEVAAFMP-----AMQFSIP--PWQYDAEVVAIAHKF 609
Cdd:cd06603   252 SLSIAGIPFVGADVGGffGN--------------PDEELLVRWYQAGAFYPffrahAHIDTKRrePWLFGEETTEIIREA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 610 AALRASLVaPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAG------- 682
Cdd:cd06603   318 IRLRYRLL-PYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVEEGATSVTVYLPGGevwydyf 396
                         410       420
                  ....*....|....*....|..
gi 1907156373 683 KWRSYKGELFDKTPVLLTDYPV 704
Cdd:cd06603   397 TGQRVTGGGTKTVPVPLDSIPV 418
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
328-632 2.02e-23

Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.


Pssm-ID: 269890 [Multi-domain]  Cd Length: 339  Bit Score: 102.20  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 328 DQNKVLQFAQQIRQHRFNSS--HLEIDdmYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFV--NYNSSSFGE 403
Cdd:cd06604    22 PEEEVREVAKGFRERDIPCDaiYLDID--YMDGYRVFTWDKERFPDPKELIKELHEQGFRLVTIVDPGVkvDPGYEVYEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 404 GVERELFVREPTGRlPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLrLRYNVTSFKFDAGEVSYLPRDFSTYRPLSDPS 483
Cdd:cd06604   100 GLENDYFVKDPDGE-LYVGKVWPGKSVFPDFTNPEVREWWGDLYKEL-VDLGVDGIWNDMNEPAVFNAPGGTTMPLDAVH 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 484 VWSRRYTEMAE--PFFSLAEVRVGYQSqniscFFRLV-------------------------DRDSVWGydlGLRSLIPA 536
Cdd:cd06604   178 RLDGGKITHEEvhNLYGLLMARATYEG-----LRRLRpnkrpfvlsragyagiqryaaiwtgDNSSSWE---HLRLSIPM 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 537 VLTVSMLGYPFILPDmIGGNAvpertagrqDGPGPerELYVRWLEVAAFMP-----AMQFSIP--PWQYDAEVVAIAHKF 609
Cdd:cd06604   250 LLNLGLSGVPFVGAD-IGGFA---------GDPSP--ELLARWYQLGAFFPffrnhSAKGTRDqePWAFGEEVEEIARKA 317
                         330       340
                  ....*....|....*....|...
gi 1907156373 610 AALRASLVaPLLLELAGEITDTG 632
Cdd:cd06604   318 IELRYRLL-PYLYTLFYEAHETG 339
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
329-602 6.00e-22

E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family represented by Escherichia coli protein Aec37. The gene encoding Aec37 (aec-37) is located within a genomic island (AGI-3) isolated from the extraintestinal avian pathogenic Escherichia coli strain BEN2908. The function of Aec37 and its orthologs is unknown; however, deletion of a region of the genome that includes aec-37 affects the assimilation of seven carbohydrates, decreases growth rate of the strain in minimal medium containing galacturonate or trehalose, and attenuates the virulence of E. coli BEN2908 in chickens. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269885 [Multi-domain]  Cd Length: 319  Bit Score: 97.29  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 329 QNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGD----FNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEG 404
Cdd:cd06599    27 QEQILDFIDTCREHDIPCDGFHLSSGYTSIEDGkryvFNWNKDKFPDPKAFFRKFHERGIRLVANIKPGLLTDHPHYDEL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 405 VERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSF-----KFDAGEVSYLPRDFSTYRPL 479
Cdd:cd06599   107 AEKGAFIKDDDGGEPAVGRFWGGGGSYLDFTNPEGREWWKEGLKEQLLDYGIDSVwndnnEYEIWDDDAACCGFGKGGPI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 480 SdpsvwsrryteMAEPFFSLAEVRVGYQSQ-----NISCFfrLVDRD---------SVWGYDLG-----LRSLIPAVLTV 540
Cdd:cd06599   187 S-----------ELRPIQPLLMARASREAQlehapNKRPF--VISRSgcagiqryaQTWSGDNRtswktLKYNIAMGLGM 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156373 541 SMLGYPFILPDmIGGNAvpertagrqdGPGPERELYVRWLEVAAFMPamQFSIPPWQYDAEV 602
Cdd:cd06599   254 SLSGVANYGHD-IGGFA----------GPAPEPELFVRWVQNGIFQP--RFSIHSWNTDNTV 302
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
358-613 3.92e-20

xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269877 [Multi-domain]  Cd Length: 322  Bit Score: 91.85  E-value: 3.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 358 AYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGrlpalVRWWNGIGAVLDFTHP 437
Cdd:cd06591    54 GWGDMKFDPERFPDPKGMVDELHKMNVKLMISVWPTFGPGSENYKELDEKGLLLRTNRG-----NGGFGGGTAFYDATNP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 438 EAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDFSTYRPLSD-----------PSVWSR------RYTEMAEPFFSLa 500
Cdd:cd06591   129 EAREIYWKQLKDNYFDKGIDAWWLDATEPELDPYDFDNYDGRTAlgpgaevgnayPLMHAKgiyegqRATGPDKRVVIL- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 501 eVRVGYQ-SQNISCFFRLVDRDSVWGydlGLRSLIPAVLTVSMLGYPFILPDmIGGNAVPERTAGRQDgpgPE-RELYVR 578
Cdd:cd06591   208 -TRSAFAgQQRYGAAVWSGDISSSWE---TLRRQIPAGLNFGASGIPYWTTD-IGGFFGGDPEPGEDD---PAyRELYVR 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907156373 579 WLEVAAFMPAM------QFSIP--PWQYDAEVVAIAHKFAALR 613
Cdd:cd06591   280 WFQFGAFCPIFrshgtrPPREPneIWSYGEEAYDILVKYIKLR 322
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
360-616 3.42e-19

CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial 6-alpha-glucosyltransferase, first identified in Arthrobacter globiformis, that produces cyclic tetrasaccharides together with a closely related enzyme CtsY. CtsZ and CtsY both have a glycosyl hydrolase family 31 (GH31) catalytic domain; CtsY belongs to a different subfamily. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269884  Cd Length: 332  Bit Score: 89.28  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 360 GDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGR-LPALVRWWNGIGAVLDFTHPE 438
Cdd:cd06598    62 GDLDWDRKAFPDPAKMIADLKQQGVGTILIEEPYVLKNSDEYDELVKKGLLAKDKAGKpEPTLFNFWFGEGGMIDWSDPE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 439 AREWFQGHLRRLrLRYNVTSFKFDAGEVSYLPRDfSTYRPLSDPSV-------WSRrytemaepffSLAEvrvGYQSQNI 511
Cdd:cd06598   142 ARAWWHDRYKDL-IDMGVAGWWTDLGEPEMHPPD-MVHADGDAADVhniynllWAK----------SIYD---GYQRNFP 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 512 SCFFRLVDRD----------SVWGYDL-----GLRSLIPAVLTVSMLGYPFILPDmIGGNAvpertagrqDGPGPERELY 576
Cdd:cd06598   207 EQRPFIMSRSgtagsqrygvIPWSGDIgrtwgGLASQINLQLHMSLSGIDYYGSD-IGGFA---------RGETLDPELY 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907156373 577 VRWLEVAAFMPAM------QFSIPPWQYDAEVVAIAHKFAALRASL 616
Cdd:cd06598   277 TRWFQYGAFDPPVrphgqnLCNPETAPDREGTKAINRENIKLRYQL 322
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
365-610 9.33e-19

alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl hydrolase family 31 (GH31) domain that catalyzes the release of an alpha-glucosyl residue from the non-reducing end of alpha-glucoside substrates such as alpha-glucosyl fluoride. Orthologs of YihQ that have not yet been functionally characterized are present in plants and fungi. YihQ has sequence similarity to other GH31 enzymes such as CtsZ, a 6-alpha-glucosyltransferase from Bacillus globisporus, and YicI, an alpha-xylosidase from Echerichia coli. These latter two belong to different GH31 subfamilies than YihQ. In bacteria, YihQ (along with YihO) is important for bacterial O-antigen capsule assembly and translocation.


Pssm-ID: 269880 [Multi-domain]  Cd Length: 325  Bit Score: 88.02  E-value: 9.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 365 DEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSS--SFGEGVERELFVREPTGRlPALVRWWNGIGAVLDFTHPEAREW 442
Cdd:cd06594    66 DEELYPGWDELVKELKEQGIRVLGYINPFLANVGPlySYKEAEEKGYLVKNKTGE-PYLVDFGEFDAGLVDLTNPEARRW 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 443 FQGHLRRLRLRYNVTSFKFDAGEvsYLPRDFSTYRPlSDPSVWSRRYTEM-AEP---------------FFSlaevRVGY 506
Cdd:cd06594   145 FKEVIKENMIDFGLSGWMADFGE--YLPFDAVLHSG-EDAALYHNRYPELwARLnreaveeagkegeivFFM----RSGY 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 507 -QSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDmIGG-NAVPERTAG--RQdgpgpeRELYVRWLEV 582
Cdd:cd06594   218 tGSPRYSTLFWAGDQNVDWSRDDGLKSVIPGALSSGLSGFSLTHSD-IGGyTTLFNPLVGykRS------KELLMRWAEM 290
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1907156373 583 AAFMPAM---QFSIPP--WQYDAEVVAIAHkFA 610
Cdd:cd06594   291 AAFTPVMrthEGNRPDdnAQFYSDAETLAH-FA 322
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
317-609 1.16e-14

glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269876 [Multi-domain]  Cd Length: 265  Bit Score: 74.70  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 317 WSTWalhgRAVDQNKVLQFAQQIRQH--RFNSSHLEID-DMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPF 393
Cdd:cd06589    15 NSRY----GYYSEDEVEELVDRYREEgiPLDGFVLDSDwMDWGGNWGGFTWNREKFPDPKGMIDELHDKGVKLGLIVKPR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 394 VnynsssfgegverelfvreptgrlpalvrwwngigavldfthpeaREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDF 473
Cdd:cd06589    91 L---------------------------------------------RDWWWENIKKLLLEQGVDGWWTDMGEPLPFDDAT 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 474 STYRPLSD------PSVWSRRYTEMAEPFFSLAEV----RVGYQSQNISCFFRLVDRDSVWGYdlgLRSLIPAVLTVSML 543
Cdd:cd06589   126 FHNGGKAQkihnayPLNMAEATYEGQKKTFPNKRPfilsRSGYAGAQRYPAIWSGDNTTTWDS---LAFQIRAGLSASLS 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156373 544 GYPFILPDmIGGNAvpertagrqdGPGPERELYVRWLEVAAFMPAMQF-------SIPPWQYDAEVVAIAHKF 609
Cdd:cd06589   203 GVGYWGHD-IGGFT----------GGDPDKELYTRWVQFGAFSPIFRLhgdnsprDKEPWVYGEEALAIFRKY 264
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
331-687 1.54e-13

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 74.54  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 331 KVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSF--GEGVERE 408
Cdd:PLN02763  202 RVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEGYFvyDSGCEND 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 409 LFVREPTGRlPALVRWWNGIGAVLDFTHPEAREWFQGHLRrlrlrynvtsfKFDAGEVSYLPRDfstyrpLSDPSVWSRR 488
Cdd:PLN02763  282 VWIQTADGK-PFVGEVWPGPCVFPDFTNKKTRSWWANLVK-----------DFVSNGVDGIWND------MNEPAVFKTV 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 489 YTEMAEPFFSLAEVRVG---YQSQNISCFFRLVDRDSVWGYDLG----------------------------------LR 531
Cdd:PLN02763  344 TKTMPETNIHRGDEELGgvqNHSHYHNVYGMLMARSTYEGMLLAnknkrpfvltragfigsqryaatwtgdnlsnwehLH 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 532 SLIPAVLTVSMLGYPFILPDM--IGGNAVPertagrqdgpgperELYVRWLEVAAFMP-----AMQFSI--PPWQYDAEV 602
Cdd:PLN02763  424 MSIPMVLQLGLSGQPLSGPDIggFAGDATP--------------KLFGRWMGVGAMFPfarghSEQGTIdhEPWSFGEEC 489
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 603 VAIAhKFAALRASLVAPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVL-EPGKQERDVYLPA 681
Cdd:PLN02763  490 EEVC-RLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISASTLpDQGSDNLQHVLPK 568

                  ....*.
gi 1907156373 682 GKWRSY 687
Cdd:PLN02763  569 GIWQRF 574
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
519-687 6.08e-13

Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a glycosyl hydrolase family 31 (GH31) domain. The domain architecture of CPE1046 and its orthologs includes a C-terminal fibronectin type 3 (FN3) domain and a coagulation factor 5/8 type C domain in addition to the GH31 domain. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269882  Cd Length: 334  Bit Score: 70.45  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 519 DRDSVWGYdlgLRSLIPAVLTVSMLGYPFILPDM---IGGNAvpertagrqdgpgperELYVRWLEVAAFMPaMQFSIP- 594
Cdd:cd06596   167 DQSGSWEY---IRFHIPTYIGSGLSGQAYATSDVdgiFGGSP----------------ETYTRDLQWKAFTP-VLMNMSg 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 595 -------PWQYDAEVVAIAHKFAALRASLVaPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDS--QFLIGDTLLVA 665
Cdd:cd06596   227 waandkqPWVFGEPYTSINRKYLKLKMRLM-PYIYTYAREASVTGLPMVRAMFLEYPNDPTAYGTATqyQFMWGPDFLVA 305
                         170       180
                  ....*....|....*....|....*.
gi 1907156373 666 PVLE---PGKQERD-VYLPAGKWRSY 687
Cdd:cd06596   306 PVYQntaAGNDVRNgIYLPAGTWIDY 331
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
351-616 7.04e-11

maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).


Pssm-ID: 269888  Cd Length: 367  Bit Score: 64.45  E-value: 7.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 351 IDDMYtpAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSS----SFGEGVERELFVREPTGRlPALVRWWN 426
Cdd:cd06602    47 IDYMD--RYRDFTLDPVNFPGLPAFVDDLHANGQHYVPILDPGISANESggypPYDRGLEMDVFIKNDDGS-PYVGKVWP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 427 GIGAVLDFTHPEAREWFQGHLRRLrlrYNVTSF-----------KFDAGEVS-----------------YLPRDFStYRP 478
Cdd:cd06602   124 GYTVFPDFTNPNTQEWWTEEIKDF---HDQVPFdglwidmnepsNFCTGSCGnspnapgcpdnklnnppYVPNNLG-GGS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 479 LSDPSV--------WSRRY--------TEMAEPFFSLAEVRVGYQSQNIScffR-------------LVDRDSVWGYdlg 529
Cdd:cd06602   200 LSDKTIcmdavhydGGLHYdvhnlyglSEAIATYKALKEIFPGKRPFIIS---RstfpgsgkyaghwLGDNYSTWED--- 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 530 LRSLIPAVLTVSMLGYPFILPDMIG--GNAVPertagrqdgpgperELYVRWLEVAAFMPamqFS--------IP--PWQ 597
Cdd:cd06602   274 MRYSIPGMLEFNLFGIPMVGADICGfnGNTTE--------------ELCARWMQLGAFYP---FSrnhndigaIDqePYV 336
                         330
                  ....*....|....*....
gi 1907156373 598 YDAEVVAIAHKFAALRASL 616
Cdd:cd06602   337 WGPSVADASRKALLIRYSL 355
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
292-462 2.42e-10

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 61.14  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 292 HKYMVRRYFNKPSRVPaseafRDPIWSTWALHGRAVDQNKVLQFAQQIRQH---RFNsshleIDDMY-------TPAYGD 361
Cdd:COG3345    18 HRYVRARLAPGPPDKP-----RPVGWNSWEAYYFDFTEEKLLALADAAAELgveLFV-----LDDGWfggrrddTAGLGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 362 FNFDEGKFPNA-SDMFRRLRDAGFRVTLWVHPF-VNYNSSSFGEgvERELFVREPtGRLPALVRWWngigAVLDFTHPEA 439
Cdd:COG3345    88 WLVDPEKFPNGlKPLADRIHALGMKFGLWVEPEmVNPDSDLYRE--HPDWVLKDP-DGEPVEGRNQ----YVLDLSNPEV 160
                         170       180
                  ....*....|....*....|...
gi 1907156373 440 REWFQGHLRRLRLRYNVTSFKFD 462
Cdd:COG3345   161 RDYLFEVLDRLLAEWGIDYIKWD 183
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
313-462 1.54e-08

glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.


Pssm-ID: 269892 [Multi-domain]  Cd Length: 299  Bit Score: 56.85  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 313 RDPIWSTW-ALHGRaVDQNKVLQFAQQIRQHRFNSshLEIDDMY-------TPAYGDFNFDEGKFPNA-SDMFRRLRDAG 383
Cdd:cd14791     2 RPVGWNSWyAYYFD-ITEEKLLELADAAAELGVEL--FVIDDGWfgarnddYAGLGDWLVDPEKFPDGlKALADRIHALG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 384 FRVTLWVHPF-VNYNSSSFGEgvERELFVREPTGrlpALVRWWNGIgaVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFD 462
Cdd:cd14791    79 MKFGLWLEPEmVGPDSELYRE--HPDWLLKDPGG---PPVTGRNQY--VLDLSNPEVRDYLREVIDRLLREWGIDYLKWD 151
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
538-617 1.77e-05

glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.


Pssm-ID: 269881 [Multi-domain]  Cd Length: 304  Bit Score: 47.20  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 538 LTVSMLGYPFILPDmIGGNAvpertagrqdGPGPERELYVRWLEVAAFMPAMQFS--------IPPWQYDAEVVAIAHKF 609
Cdd:cd06595   225 ATAANVGYSWWSHD-IGGHK----------GGIEDPELYLRWVQFGVFSPILRLHsdkgpyykREPWLWDAKTFEIAKDY 293

                  ....*...
gi 1907156373 610 AALRASLV 617
Cdd:cd06595   294 LRLRHRLI 301
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
328-616 3.04e-04

alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 (GH31) enzymes that degrade alpha-1,4-glucans and maltooligosaccharides via a nonhydrolytic pathway to yield 1,5-D-anhydrofructose from the nonreducing end. GLases cleave the bond between C1 and O1 of the nonreducing sugar residue of alpha-glucans to generate a monosaccharide product with a double bond between C1 and C2. This family corresponds to subgroup 2 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269887 [Multi-domain]  Cd Length: 347  Bit Score: 43.55  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 328 DQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNY---NSSSFGEG 404
Cdd:cd06601    22 SRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMFSNLHAQGFKCSTNITPIITDpyiGGVNYGGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 405 VERELFVrePTGRLPALVRWW-------NGIGavLDF-----THPE---AREWFQGHLRRLRLRYNVTSFKFDAgEVSYL 469
Cdd:cd06601   102 LGSPGFY--PDLGRPEVREWWgqqykylFDMG--LEMvwqdmTTPAiapHKINGYGDMKTFPLRLLVTDDSVKN-EHTYK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 470 P----RDFSTYRPLSdpSVWSRRYTEMAEPF---FSLAevRVGYQSQNISCFFRLVDRDSVWGYdlgLRSLIPAVLTVSM 542
Cdd:cd06601   177 PaatlWNLYAYNLHK--ATYHGLNRLNARPNrrnFIIG--RGGYAGAQRFAGLWTGDNASTWDF---LQINIPQVLNLGL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 543 LGYPFILPDmIGGNAvPERTAGRQDGPGPerELYVRWLEVAAFMP--------------AMQFSIPPWQYDAeVVAIAHK 608
Cdd:cd06601   250 SGVPISGSD-IGGFA-SGSDENEGKWCDP--ELLIRWVQAGAFLPwfrnhydryikkkqQEKLYEPYYYYEP-VLPICRK 324

                  ....*...
gi 1907156373 609 FAALRASL 616
Cdd:cd06601   325 YVELRYRL 332
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
328-587 4.96e-04

maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. Alpha-glucosidase II is a GH31 enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes.


Pssm-ID: 269886 [Multi-domain]  Cd Length: 256  Bit Score: 42.48  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 328 DQNKVLQFAQQIRQHRF--NSSHLEIDdmYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPfvnynsssfgegv 405
Cdd:cd06600    22 DQDKVVEVVDIMQEAGIpyDVMWLDID--YMDSYKDFTWDPVRFPEPKKFVDELHKNGQKLVTIVDP------------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 406 erelfvreptgrlpalvrwwnGIgavldfthpeAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDFSTYRPLSDPSVW 485
Cdd:cd06600    87 ---------------------GI----------TREWWAGLISEFLYSQGIDGIWIDMNEPSNFYKVHNLYGFYEAMATA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156373 486 SRRYTEMAEPFFSLAevRVGYQSQNISCFFRLVDRDSVWGYdlgLRSLIPAVLTVSMLGYPFILPDmIGGNAVpertagr 565
Cdd:cd06600   136 EGLRTSHNERPFILS--RSTFAGSQKYAAHWTGDNTASWDD---LKLSIPLVLGLSLSGIPFVGAD-IGGFAG------- 202
                         250       260
                  ....*....|....*....|..
gi 1907156373 566 qdgpGPERELYVRWLEVAAFMP 587
Cdd:cd06600   203 ----DTSEELLVRWYQLGAFYP 220
 
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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