NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|28571438|ref|NP_788858|]
View 

uncharacterized protein Dmel_CG33080, isoform A [Drosophila melanogaster]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
511-888 4.65e-127

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: 387.73  E-value: 4.65e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 511 EEPVWRIPhTELPESLNESAICDYSESAIAMGL--GHIVINEFWQENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQ 588
Cdd:cd06592   1 RPPIWSTW-AEYKYNINQEKVLEYAEEIRANGFppSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 589 PFISTDSANFKDAVKRKLLIYErhsERSIPALTRYKSSSSAGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYN 668
Cdd:cd06592  80 PFINPDSPNFRELRDKGYLVKE---DSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 669 LPHYYQCRQTLDNPDTYARLFTASLEGAGLMA-VSTASVVPKPPTF---LSTPPANATWEGLRETLGAVLNYGVIGYPFV 744
Cdd:cd06592 157 LPADPATFPSGLNPNEYTTLYAELAAEFGLLNeVRSGWKSQGLPLFvrmSDKDSHWGYWNGLRSLIPTALTQGLLGYPFV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 745 LPGVIGGDYllqrplskmvsfyslSQPPLPDPELFIRWLQLATFMPAMQFSHLPSEYRSDLVTRVAQELKEVRQLiVIPL 824
Cdd:cd06592 237 LPDMIGGNA---------------YGNFPPDKELYIRWLQLSAFMPAMQFSVAPWRNYDEEVVDIARKLAKLREK-LLPY 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571438 825 LKKYLNPSMNEGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANREEREVYLPQGVW 888
Cdd:cd06592 301 IYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
 
Name Accession Description Interval E-value
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
511-888 4.65e-127

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: 387.73  E-value: 4.65e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 511 EEPVWRIPhTELPESLNESAICDYSESAIAMGL--GHIVINEFWQENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQ 588
Cdd:cd06592   1 RPPIWSTW-AEYKYNINQEKVLEYAEEIRANGFppSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 589 PFISTDSANFKDAVKRKLLIYErhsERSIPALTRYKSSSSAGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYN 668
Cdd:cd06592  80 PFINPDSPNFRELRDKGYLVKE---DSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 669 LPHYYQCRQTLDNPDTYARLFTASLEGAGLMA-VSTASVVPKPPTF---LSTPPANATWEGLRETLGAVLNYGVIGYPFV 744
Cdd:cd06592 157 LPADPATFPSGLNPNEYTTLYAELAAEFGLLNeVRSGWKSQGLPLFvrmSDKDSHWGYWNGLRSLIPTALTQGLLGYPFV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 745 LPGVIGGDYllqrplskmvsfyslSQPPLPDPELFIRWLQLATFMPAMQFSHLPSEYRSDLVTRVAQELKEVRQLiVIPL 824
Cdd:cd06592 237 LPDMIGGNA---------------YGNFPPDKELYIRWLQLSAFMPAMQFSVAPWRNYDEEVVDIARKLAKLREK-LLPY 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571438 825 LKKYLNPSMNEGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANREEREVYLPQGVW 888
Cdd:cd06592 301 IYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
546-918 4.26e-43

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 166.49  E-value: 4.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 546 IVINEFWQE--NIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKrKLLIYERHSersiPALTRY 623
Cdd:COG1501 205 IHLDIRWMDkyYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSAIFAEGMA-NFVKIASGT----VFVGKM 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 624 KSSSSaGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGY---------NLPHYYQCRQT-LDNPDTYARLFTASL 693
Cdd:COG1501 280 WPGTT-GLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNEGWptdvatfpsNVPQQMRNLYGlLEAKATFEGFRTSRN 358
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 694 EGA-GLMAVSTASVVPKPptFLSTPPANATWEGLRETLGAVLNYGVIGYPFVLPGVIGGDyllqrplskmvsfyslsqpP 772
Cdd:COG1501 359 NRTfILTRSGFAGGQRYP--VIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDIGGFF-------------------G 417
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 773 LPDPELFIRWLQLATFMPAMQ-----FSHLPSEYrSDLVTRVAQELKEVRQLIvIPLLKKYLNPSMNEGLPLVRPLWMMD 847
Cdd:COG1501 418 SPSRELWIRWFQVGAFSPFARihgwaSSTEPWFF-DEEAKQIVKEYAQLRYRL-LPYIYSLFAKASTDGTPVIRPLFLEF 495
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571438 848 PHDPACLIVSDEFSVGEELIVAPILhANREEREVYLPQGVWKDGIDGSLRKGSRWMHgYRVPKDKIAYFRK 918
Cdd:COG1501 496 PDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIEGGQWIT-VTAPLDRLPLYVR 564
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
552-913 7.65e-39

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: 150.40  E-value: 7.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   552 WQENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFIS---TDSANFKDAVKRKLLIYERHSERSIpaltrYKSSSS 628
Cdd:pfam01055  68 YMDGYRDFTWDPERFPDPKGMVDELHAKGQKLVVIIDPGIKkvdPGYPPYDEGLEKGYFVKNPDGSLYV-----GGWPGM 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   629 AGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYNLPHYYQCRQTLDNPDTYARLFTA---SLEGAgLMAVSTAS 705
Cdd:pfam01055 143 SAFPDFTNPEARDWWADQLFKFLLDMGVDGIWNDMNEPSVFCGSGPEDTVAKDNDPGGGVEHYdvhNLYGL-LMAKATYE 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   706 VVP-----KPPTFLS---TP-----PA------NATWEGLRETLGAVLNYGVIGYPFVlpGV-IGGdyllqrplskmvsF 765
Cdd:pfam01055 222 GLRekrpnKRPFVLTrsgFAgsqryAAhwsgdnTSTWEHLRFSIPGGLSLGLSGIPFW--GAdIGG-------------F 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   766 YSLsqpplPDPELFIRWLQLATFMPAMQF-SHLPSEYR-----SDLVTRVAQELKEVR-QLIviPLLkkYlnpSMN---- 834
Cdd:pfam01055 287 FNP-----TTPELYVRWYQLGAFSPFFRNhSSIDTRRRepwlfGEEVEEIIRKAIRLRyRLL--PYL--Y---TLFyeah 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   835 -EGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANREEREVYLPQGVWKDGIDGSLRKGSRWMHgYRVPKDKI 913
Cdd:pfam01055 355 eTGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYEGGGTVP-VTAPLDRI 433
PRK10426 PRK10426
alpha-glucosidase; Provisional
562-888 2.87e-24

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 108.93  E-value: 2.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  562 DKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIYERHSERSIPALTRYksssSAGVLDITNNASVP 641
Cdd:PRK10426 264 DSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGDLCEEAAEKGYLAKDADGGDYLVEFGEF----YAGVVDLTNPEAYE 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  642 WLLEKLQRLKEEYGVQSFYLDLGTGynLP-----HYYQCRQTLDN--PDTYARLFTASLEGAGLM--AV----STASVVP 708
Cdd:PRK10426 340 WFKEVIKKNMIGLGCSGWMADFGEY--LPtdaylHNGVSAEIMHNawPALWAKCNYEALEETGKLgeILffmrAGYTGSQ 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  709 KPPTFLSTPPANATW---EGLRETLGAVLNYGVIGYPFVLPGvIGGdYllqRPLSKMVSfyslsqpplpDPELFIRWLQL 785
Cdd:PRK10426 418 KYSTLFWAGDQNVDWsldDGLASVVPAALSLGMSGHGLHHSD-IGG-Y---TTLFGMKR----------TKELLLRWCEF 482
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  786 ATFMPAMQfSH---LPSE---YRSDLVTrVAQELKEVRqliVIPLLKKYLNPSMNE----GLPLVRPLWMMDPHDPACLI 855
Cdd:PRK10426 483 SAFTPVMR-THegnRPGDnwqFDSDAET-IAHFARMTR---VFTTLKPYLKELVAEaaktGLPVMRPLFLHYEDDAATYT 557
                        330       340       350
                 ....*....|....*....|....*....|...
gi 28571438  856 VSDEFSVGEELIVAPILHANREEREVYLPQGVW 888
Cdd:PRK10426 558 LKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKW 590
 
Name Accession Description Interval E-value
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
511-888 4.65e-127

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: 387.73  E-value: 4.65e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 511 EEPVWRIPhTELPESLNESAICDYSESAIAMGL--GHIVINEFWQENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQ 588
Cdd:cd06592   1 RPPIWSTW-AEYKYNINQEKVLEYAEEIRANGFppSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLWVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 589 PFISTDSANFKDAVKRKLLIYErhsERSIPALTRYKSSSSAGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYN 668
Cdd:cd06592  80 PFINPDSPNFRELRDKGYLVKE---DSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEASY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 669 LPHYYQCRQTLDNPDTYARLFTASLEGAGLMA-VSTASVVPKPPTF---LSTPPANATWEGLRETLGAVLNYGVIGYPFV 744
Cdd:cd06592 157 LPADPATFPSGLNPNEYTTLYAELAAEFGLLNeVRSGWKSQGLPLFvrmSDKDSHWGYWNGLRSLIPTALTQGLLGYPFV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 745 LPGVIGGDYllqrplskmvsfyslSQPPLPDPELFIRWLQLATFMPAMQFSHLPSEYRSDLVTRVAQELKEVRQLiVIPL 824
Cdd:cd06592 237 LPDMIGGNA---------------YGNFPPDKELYIRWLQLSAFMPAMQFSVAPWRNYDEEVVDIARKLAKLREK-LLPY 300
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571438 825 LKKYLNPSMNEGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANREEREVYLPQGVW 888
Cdd:cd06592 301 IYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDILVAPVLEKGARSRDVYLPKGRW 364
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
546-918 4.26e-43

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 166.49  E-value: 4.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 546 IVINEFWQE--NIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKrKLLIYERHSersiPALTRY 623
Cdd:COG1501 205 IHLDIRWMDkyYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSAIFAEGMA-NFVKIASGT----VFVGKM 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 624 KSSSSaGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGY---------NLPHYYQCRQT-LDNPDTYARLFTASL 693
Cdd:COG1501 280 WPGTT-GLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNEGWptdvatfpsNVPQQMRNLYGlLEAKATFEGFRTSRN 358
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 694 EGA-GLMAVSTASVVPKPptFLSTPPANATWEGLRETLGAVLNYGVIGYPFVLPGVIGGDyllqrplskmvsfyslsqpP 772
Cdd:COG1501 359 NRTfILTRSGFAGGQRYP--VIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDIGGFF-------------------G 417
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 773 LPDPELFIRWLQLATFMPAMQ-----FSHLPSEYrSDLVTRVAQELKEVRQLIvIPLLKKYLNPSMNEGLPLVRPLWMMD 847
Cdd:COG1501 418 SPSRELWIRWFQVGAFSPFARihgwaSSTEPWFF-DEEAKQIVKEYAQLRYRL-LPYIYSLFAKASTDGTPVIRPLFLEF 495
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571438 848 PHDPACLIVSDEFSVGEELIVAPILhANREEREVYLPQGVWKDGIDGSLRKGSRWMHgYRVPKDKIAYFRK 918
Cdd:COG1501 496 PDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIEGGQWIT-VTAPLDRLPLYVR 564
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
552-913 7.65e-39

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: 150.40  E-value: 7.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   552 WQENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFIS---TDSANFKDAVKRKLLIYERHSERSIpaltrYKSSSS 628
Cdd:pfam01055  68 YMDGYRDFTWDPERFPDPKGMVDELHAKGQKLVVIIDPGIKkvdPGYPPYDEGLEKGYFVKNPDGSLYV-----GGWPGM 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   629 AGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYNLPHYYQCRQTLDNPDTYARLFTA---SLEGAgLMAVSTAS 705
Cdd:pfam01055 143 SAFPDFTNPEARDWWADQLFKFLLDMGVDGIWNDMNEPSVFCGSGPEDTVAKDNDPGGGVEHYdvhNLYGL-LMAKATYE 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   706 VVP-----KPPTFLS---TP-----PA------NATWEGLRETLGAVLNYGVIGYPFVlpGV-IGGdyllqrplskmvsF 765
Cdd:pfam01055 222 GLRekrpnKRPFVLTrsgFAgsqryAAhwsgdnTSTWEHLRFSIPGGLSLGLSGIPFW--GAdIGG-------------F 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   766 YSLsqpplPDPELFIRWLQLATFMPAMQF-SHLPSEYR-----SDLVTRVAQELKEVR-QLIviPLLkkYlnpSMN---- 834
Cdd:pfam01055 287 FNP-----TTPELYVRWYQLGAFSPFFRNhSSIDTRRRepwlfGEEVEEIIRKAIRLRyRLL--PYL--Y---TLFyeah 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438   835 -EGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANREEREVYLPQGVWKDGIDGSLRKGSRWMHgYRVPKDKI 913
Cdd:pfam01055 355 eTGLPVMRPLFLEFPDDPNTFDIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYEGGGTVP-VTAPLDRI 433
PRK10426 PRK10426
alpha-glucosidase; Provisional
562-888 2.87e-24

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 108.93  E-value: 2.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  562 DKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIYERHSERSIPALTRYksssSAGVLDITNNASVP 641
Cdd:PRK10426 264 DSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGDLCEEAAEKGYLAKDADGGDYLVEFGEF----YAGVVDLTNPEAYE 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  642 WLLEKLQRLKEEYGVQSFYLDLGTGynLP-----HYYQCRQTLDN--PDTYARLFTASLEGAGLM--AV----STASVVP 708
Cdd:PRK10426 340 WFKEVIKKNMIGLGCSGWMADFGEY--LPtdaylHNGVSAEIMHNawPALWAKCNYEALEETGKLgeILffmrAGYTGSQ 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  709 KPPTFLSTPPANATW---EGLRETLGAVLNYGVIGYPFVLPGvIGGdYllqRPLSKMVSfyslsqpplpDPELFIRWLQL 785
Cdd:PRK10426 418 KYSTLFWAGDQNVDWsldDGLASVVPAALSLGMSGHGLHHSD-IGG-Y---TTLFGMKR----------TKELLLRWCEF 482
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  786 ATFMPAMQfSH---LPSE---YRSDLVTrVAQELKEVRqliVIPLLKKYLNPSMNE----GLPLVRPLWMMDPHDPACLI 855
Cdd:PRK10426 483 SAFTPVMR-THegnRPGDnwqFDSDAET-IAHFARMTR---VFTTLKPYLKELVAEaaktGLPVMRPLFLHYEDDAATYT 557
                        330       340       350
                 ....*....|....*....|....*....|...
gi 28571438  856 VSDEFSVGEELIVAPILHANREEREVYLPQGVW 888
Cdd:PRK10426 558 LKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKW 590
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
527-794 2.12e-22

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: 99.31  E-value: 2.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 527 NESAICDYSESAIAMGL--GHIVINEFWQEniGDFTV---DKARFPTLKDTIDVLHRRGFKVVLTIQPFISTD------- 594
Cdd:cd06597  22 SQAEVLELVEEYLAYDIpvGAVVIEAWSDE--ATFYIfndATGKWPDPKGMIDSLHEQGIKVILWQTPVVKTDgtdhaqk 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 595 SANFKDAVKRKLLIYERHSERSIPALTRYKSSSsagVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGY---NLPh 671
Cdd:cd06597 100 SNDYAEAIAKGYYVKNGDGTPYIPEGWWFGGGS---LIDFTNPEAVAWWHDQRDYLLDELGIDGFKTDGGEPYwgeDLI- 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 672 YYQCRQTLDNPDTYARLFTAS--------LEGAGLMAVSTASVVPKPPTFLSTPpANATWEGLRETLGAVLNYGVIGYPF 743
Cdd:cd06597 176 FSDGKKGREMRNEYPNLYYKAyfdyireiGNDGVLFSRAGDSGAQRYPIGWVGD-QDSTFEGLQSALKAGLSAAWSGYPF 254
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 28571438 744 vlPGV-IGGdyllqrplskmvsfYSLsqpPLPDPELFIRWLQLATFMPAMQF 794
Cdd:cd06597 255 --WGWdIGG--------------FSG---PLPTAELYLRWTQLAAFSPIMQN 287
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
721-916 1.63e-20

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: 95.67  E-value: 1.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 721 ATWEGLRETLGAVLNYGVIGYPFVlpGV-IGGdyllqrplskmvsFYSLsqpplPDPELFIRWLQLATFMPAM-QFSHLP 798
Cdd:cd06603 238 ATWEHLKISIPMLLSLSIAGIPFV--GAdVGG-------------FFGN-----PDEELLVRWYQAGAFYPFFrAHAHID 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 799 SEYR-----SDLVTRVAQELKEVRQLIvIPLLKKYLNPSMNEGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILH 873
Cdd:cd06603 298 TKRRepwlfGEETTEIIREAIRLRYRL-LPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSLLVKPVVE 376
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 28571438 874 ANREEREVYLPQG-VWKDGIDGSLRKGSRWmHGYRVPKDKIAYF 916
Cdd:cd06603 377 EGATSVTVYLPGGeVWYDYFTGQRVTGGGT-KTVPVPLDSIPVF 419
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
551-790 6.93e-16

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: 79.53  E-value: 6.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 551 FWQEN--IGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIyerHSERSIPALTRYKSSSS 628
Cdd:cd06593  48 FWMKEdwWCDFEWDEERFPDPEGMIARLKEKGFKVCLWINPYISQDSPLFKEAAEKGYLV---KNPDGSPWHQWDGWQPG 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 629 AGVLDITNNASVPWLLEKLQRLKEEyGVQSFYLDLG-------------TGYNLPHYYqcrqtldnPDTYARL-FTASLE 694
Cdd:cd06593 125 MGIIDFTNPEAVAWYKEKLKRLLDM-GVDVIKTDFGeripedavyydgsDGRKMHNLY--------PLLYNKAvYEATKE 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 695 GAGlmavsTASVVPKPPTFLSTP--PA------NATWEGLRETLGAVLNYGVIGYPFVlpGV-IGGdyllqrplskmvsF 765
Cdd:cd06593 196 VKG-----EEAVLWARSAWAGSQryPVhwggdsESTFEGMAASLRGGLSLGLSGFGFW--SHdIGG-------------F 255
                       250       260
                ....*....|....*....|....*
gi 28571438 766 YslsqpPLPDPELFIRWLQLATFMP 790
Cdd:cd06593 256 E-----GTPSPELYKRWTQFGLLSS 275
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
558-906 2.12e-13

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 74.16  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  558 DFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIyeRHSERSI-------PALtrykssssaG 630
Cdd:PRK10658 316 DFEWDPRTFPDPEGMLKRLKAKGLKICVWINPYIAQKSPLFKEGKEKGYLL--KRPDGSVwqwdkwqPGM---------A 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  631 VLDITNNASVPWLLEKLQRLKEEyGVQSFYLDLGTgyNLP--------------HYYqcrqtldnpdtYARLFtaslega 696
Cdd:PRK10658 385 IVDFTNPDACKWYADKLKGLLDM-GVDCFKTDFGE--RIPtdvvwfdgsdpqkmHNY-----------YTYLY------- 443
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  697 glmavstasvvpkpptflstppaNAT-WEGLRETLG---AVL---NYGVIGYPFvlPGVIGGDYL---------LQRPLS 760
Cdd:PRK10658 444 -----------------------NKTvFDVLKETRGegeAVLfarSATVGGQQF--PVHWGGDCYsnyesmaesLRGGLS 498
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  761 KMVS---FYSL------SQPplpDPELFIRWLQlatfmpamqFSHLPS--------EYR--------SDLVTRVAQELKe 815
Cdd:PRK10658 499 LGLSgfgFWSHdiggfeNTA---TADVYKRWCA---------FGLLSShsrlhgskSYRvpwaydeeAVDVVRFFTKLK- 565
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  816 vrqLIVIPLLKKYLNPSMNEGLPLVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANREErEVYLPQGVWKDGIDGS 895
Cdd:PRK10658 566 ---CRLMPYLYREAAEAHERGTPMMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVFSEAGDV-EYYLPEGRWTHLLTGE 641
                        410
                 ....*....|....
gi 28571438  896 LRKGSRWM---HGY 906
Cdd:PRK10658 642 EVEGGRWHkeqHDF 655
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
557-792 1.09e-12

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: 70.41  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 557 GDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIYERHSERSIPALTRYksSSSAGVLDITN 636
Cdd:cd06598  62 GDLDWDRKAFPDPAKMIADLKQQGVGTILIEEPYVLKNSDEYDELVKKGLLAKDKAGKPEPTLFNFW--FGEGGMIDWSD 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 637 NASVPWLLEKLQRLKEEyGVQSFYLDLG--------TGY-NLPH------------------YYQcrqtlDNPDTyaRLF 689
Cdd:cd06598 140 PEARAWWHDRYKDLIDM-GVAGWWTDLGepemhppdMVHaDGDAadvhniynllwaksiydgYQR-----NFPEQ--RPF 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 690 TASLEG-AGL----MAVSTASVvpkpptflstppaNATWEGLRETLGAVLNYGVIGYPFV---LPGVIGGDYllqrplsk 761
Cdd:cd06598 212 IMSRSGtAGSqrygVIPWSGDI-------------GRTWGGLASQINLQLHMSLSGIDYYgsdIGGFARGET-------- 270
                       250       260       270
                ....*....|....*....|....*....|.
gi 28571438 762 mvsfyslsqpplPDPELFIRWLQLATFMPAM 792
Cdd:cd06598 271 ------------LDPELYTRWFQYGAFDPPV 289
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
559-888 9.48e-12

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 69.15  E-value: 9.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  559 FTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANF------------KDAVKRKLLIYERHSERSIPALTRYKSS 626
Cdd:PLN02763 233 FTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEGYFvydsgcendvwiQTADGKPFVGEVWPGPCVFPDFTNKKTR 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  627 S----------SAGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYNLPHYYQCRQTLDNPDTYarlftaslEGA 696
Cdd:PLN02763 313 SwwanlvkdfvSNGVDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELGGVQNHSHYHNVYGMLMARSTY--------EGM 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  697 GLMAVSTASVVPKPPTFLSTPPANATWEG--------LRETLGAVLNYGVIGYPFVLPGV--IGGDyllqrplskmvsfy 766
Cdd:PLN02763 385 LLANKNKRPFVLTRAGFIGSQRYAATWTGdnlsnwehLHMSIPMVLQLGLSGQPLSGPDIggFAGD-------------- 450
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438  767 slsqpplPDPELFIRWLQLATFMPamqFSHLPSEYRSDLVT--RVAQELKEV------RQLIVIPLLKKYLNPSMNEGLP 838
Cdd:PLN02763 451 -------ATPKLFGRWMGVGAMFP---FARGHSEQGTIDHEpwSFGEECEEVcrlalkRRYRLLPHFYTLFYKAHTTGLP 520
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 28571438  839 LVRPLWMMDPHDPACLIVSDEFSVGEELIVAPILHANR-EEREVYLPQGVW 888
Cdd:PLN02763 521 VMTPIFFADPKDPSLRKVENSFLLGPLLISASTLPDQGsDNLQHVLPKGIW 571
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
546-792 1.84e-11

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: 66.43  E-value: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 546 IVINEF-WQEN-IGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIYERHSERSIPALTRY 623
Cdd:cd06591  43 IVQDWFyWTEQgWGDMKFDPERFPDPKGMVDELHKMNVKLMISVWPTFGPGSENYKELDEKGLLLRTNRGNGGFGGGTAF 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 624 kssssagvLDITNNASVPWLLEKLQRLKEEYGVQSFYLDlGT---GYNLPHYYQCRQTLDNPDT-----YARLFTASLEG 695
Cdd:cd06591 123 --------YDATNPEAREIYWKQLKDNYFDKGIDAWWLD-ATepeLDPYDFDNYDGRTALGPGAevgnaYPLMHAKGIYE 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 696 aGLMAVSTAsvvpKPPTFLsTPPA----------------NATWEGLRETLGAVLNYGVIGYP---------FVLPGVIG 750
Cdd:cd06591 194 -GQRATGPD----KRVVIL-TRSAfagqqrygaavwsgdiSSSWETLRRQIPAGLNFGASGIPywttdiggfFGGDPEPG 267
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 28571438 751 GDYllqrplskmvsfyslsqpplPD-PELFIRWLQLATFMPAM 792
Cdd:cd06591 268 EDD--------------------PAyRELYVRWFQFGAFCPIF 290
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
559-790 4.54e-09

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: 59.15  E-value: 4.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 559 FTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSANFKDAVKRKLLIyeRHSERSIPALTRYKSSSSAgVLDITNNA 638
Cdd:cd06599  64 FNWNKDKFPDPKAFFRKFHERGIRLVANIKPGLLTDHPHYDELAEKGAFI--KDDDGGEPAVGRFWGGGGS-YLDFTNPE 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 639 SVPWLLEklqRLKE---EYGVQSFYLDlgtgyNlphyyqCRQTLDNPDTYARLFTASLEGAG-------LMA-VSTASVV 707
Cdd:cd06599 141 GREWWKE---GLKEqllDYGIDSVWND-----N------NEYEIWDDDAACCGFGKGGPISElrpiqplLMArASREAQL 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 708 PKPPT---FL---STPPA-----------NAT-WEGLRETLGAVLNYGVIGYPFVlpGV-IGGdyllqrplskmvsFYSl 768
Cdd:cd06599 207 EHAPNkrpFVisrSGCAGiqryaqtwsgdNRTsWKTLKYNIAMGLGMSLSGVANY--GHdIGG-------------FAG- 270
                       250       260
                ....*....|....*....|..
gi 28571438 769 sqpPLPDPELFIRWLQLATFMP 790
Cdd:cd06599 271 ---PAPEPELFVRWVQNGIFQP 289
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
558-790 1.21e-07

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: 54.82  E-value: 1.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 558 DFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSAN--FKDAVKRKLLIyeRHSERSI------PALTRYkssssa 629
Cdd:cd06604  55 VFTWDKERFPDPKELIKELHEQGFRLVTIVDPGVKVDPGYevYEEGLENDYFV--KDPDGELyvgkvwPGKSVF------ 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 630 gvLDITNNASVPWLLEKLQRLKEeYGVQSFYLDLgtgyNLPH-YYQCRQTLDNPDTYARLftaslEG------------A 696
Cdd:cd06604 127 --PDFTNPEVREWWGDLYKELVD-LGVDGIWNDM----NEPAvFNAPGGTTMPLDAVHRL-----DGgkitheevhnlyG 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 697 GLMAVST----ASVVPKPPTFLSTPPA---------------NATWEGLRETLGAVLNYGVIGYPFVlpGV-IGGdyllq 756
Cdd:cd06604 195 LLMARATyeglRRLRPNKRPFVLSRAGyagiqryaaiwtgdnSSSWEHLRLSIPMLLNLGLSGVPFV--GAdIGG----- 267
                       250       260       270
                ....*....|....*....|....*....|....
gi 28571438 757 rplskmvsFYSLsqpplPDPELFIRWLQLATFMP 790
Cdd:cd06604 268 --------FAGD-----PSPELLARWYQLGAFFP 288
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
546-795 1.57e-07

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: 54.13  E-value: 1.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 546 IVINEFWQENIGD-------FTVDKARFPTLKDTIDVLHRRGFKVVLTIQPF--ISTDSANFKDAVKRkLLIYERHSERs 616
Cdd:cd06595  44 LVLDMDWHITDKKykngwtgYTWNKELFPDPKGFLDWLHERGLRVGLNLHPAegIRPHEEAYAEFAKY-LGIDPAKIIP- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 617 IPaltrykssssagvLDITNNASVPWLLEKLQRLKEEYGVQSFYLDLGTGYNLP-----------HYY---QCRQTLDNP 682
Cdd:cd06595 122 IP-------------FDVTDPKFLDAYFKLLIHPLEKQGVDFWWLDWQQGKDSPlagldplwwlnHYHyldSGRNGKRRP 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 683 DTYARlfTASLEGAGLmavstasvvpkppTFLSTPPANATWEGLRE----TLGAvlnyGVIGYPFV---LPGVIGGDYll 755
Cdd:cd06595 189 LILSR--WGGLGSHRY-------------PIGFSGDTEVSWETLAFqpyfTATA----ANVGYSWWshdIGGHKGGIE-- 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 28571438 756 qrplskmvsfyslsqpplpDPELFIRWLQLATFMPAMQFS 795
Cdd:cd06595 248 -------------------DPELYLRWVQFGVFSPILRLH 268
GalA COG3345
Alpha-galactosidase [Carbohydrate transport and metabolism];
526-674 3.51e-07

Alpha-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442574 [Multi-domain]  Cd Length: 219  Bit Score: 51.90  E-value: 3.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 526 LNESAICDYSESAIAMGLGHIVINEFWQEN-------IGDFTVDKARFP-TLKDTIDVLHRRGFKVVLTIQPF-ISTDSA 596
Cdd:COG3345  48 FTEEKLLALADAAAELGVELFVLDDGWFGGrrddtagLGDWLVDPEKFPnGLKPLADRIHALGMKFGLWVEPEmVNPDSD 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 597 NFKdAVKRKLLiyerHSERSIPALTRYkssssAGVLDITNNASVPWLLEKLQRLKEEYGVQSFYLD----LGTGYNLPHY 672
Cdd:COG3345 128 LYR-EHPDWVL----KDPDGEPVEGRN-----QYVLDLSNPEVRDYLFEVLDRLLAEWGIDYIKWDfnrdLTEAGSLPGE 197

                ..
gi 28571438 673 YQ 674
Cdd:COG3345 198 RQ 199
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
775-894 1.23e-06

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: 51.58  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 775 DPELFIRWLQLATFMPAM-----------QFSHLPSEYRSdlVTRVAQELKEvrQLIviPLLKKYLNPSMNEGLPLVRPL 843
Cdd:cd06596 204 SPETYTRDLQWKAFTPVLmnmsgwaandkQPWVFGEPYTS--INRKYLKLKM--RLM--PYIYTYAREASVTGLPMVRAM 277
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28571438 844 WMMDPHDPACL--IVSDEFSVGEELIVAPILHANREEREV----YLPQGVWKDGIDG 894
Cdd:cd06596 278 FLEYPNDPTAYgtATQYQFMWGPDFLVAPVYQNTAAGNDVrngiYLPAGTWIDYWTG 334
GH36 cd14791
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
526-656 1.26e-06

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: 51.07  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 526 LNESAICDYSESAIAMGLGHIVINEFWQEN-------IGDFTVDKARFP-TLKDTIDVLHRRGFKVVLTIQPF-ISTDS- 595
Cdd:cd14791  16 ITEEKLLELADAAAELGVELFVIDDGWFGArnddyagLGDWLVDPEKFPdGLKALADRIHALGMKFGLWLEPEmVGPDSe 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571438 596 --ANFKDavkrkLLIYERHSERSipaltrykSSSSAGVLDITNNASVPWLLEKLQRLKEEYGV 656
Cdd:cd14791  96 lyREHPD-----WLLKDPGGPPV--------TGRNQYVLDLSNPEVRDYLREVIDRLLREWGI 145
GH_D cd14790
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
541-751 4.68e-06

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: 49.16  E-value: 4.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 541 MGLGHIVINEFW--QENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFIstdsanfkdavkrklliyerhsersip 618
Cdd:cd14790  32 LPYKVFNIDDCWakKDAEGDFVPDPERFPRGEAMARRLHARGLKLGIWGDPFR--------------------------- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 619 altrykssssagvLDitnnasvpWLLEKLQRLKeEYGVQSFYLDLG-TGYNLPHYYQCRQTLDNPDTYARLFTASLEGAG 697
Cdd:cd14790  85 -------------LD--------WVEDDLQTLA-EWGVDMFKLDFGeSSGTPVQWFPQKMPNKEQAQGYEQMARALNATG 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571438 698 LMAV---STASVVPKPPTFL-------STPPANATWEGLRETLGAVLNYGVIGYPFVLPGVIGG 751
Cdd:cd14790 143 EPIVysgSWSAYQGGGEICNlwrnyddIQDSWDAVLSIVDWFFTNQDVLQAGGFHFNDPDMLII 206
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
552-794 1.13e-05

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: 48.12  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 552 WQENIGDFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFIStdsANFKDAVKRKLLiyerhsersipaltryksssSAGV 631
Cdd:cd06589  52 WGGNWGGFTWNREKFPDPKGMIDELHDKGVKLGLIVKPRLR---DWWWENIKKLLL--------------------EQGV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 632 LDITNNASVPWLLEKLQRLKEEYGVQSfyldlgtgYNLPHYYQCRQTLD---NPDTYARLFTASLEG-AGL---MAVSTA 704
Cdd:cd06589 109 DGWWTDMGEPLPFDDATFHNGGKAQKI--------HNAYPLNMAEATYEgqkKTFPNKRPFILSRSGyAGAqryPAIWSG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 705 SVvpkpptflstppaNATWEGLRETLGAVLNYGVIGYPFV---LPGVIGGDyllqrplskmvsfyslsqpplPDPELFIR 781
Cdd:cd06589 181 DN-------------TTTWDSLAFQIRAGLSASLSGVGYWghdIGGFTGGD---------------------PDKELYTR 226
                       250
                ....*....|...
gi 28571438 782 WLQLATFMPAMQF 794
Cdd:cd06589 227 WVQFGAFSPIFRL 239
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
558-795 1.88e-03

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: 41.73  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 558 DFTVDKARFPTLKDTIDVLHRRGFKVVLTIQPFISTDSAN----FKDAVKRKLLIYERHSERSI----PALTRYKssssa 629
Cdd:cd06602  55 DFTLDPVNFPGLPAFVDDLHANGQHYVPILDPGISANESGgyppYDRGLEMDVFIKNDDGSPYVgkvwPGYTVFP----- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 630 gvlDITNNASVPWLLEKLQRLKEEYGVQSFYLDL--------GTGYNLPHYYQCRQT-LDNPDtYA-------RLFTASL 693
Cdd:cd06602 130 ---DFTNPNTQEWWTEEIKDFHDQVPFDGLWIDMnepsnfctGSCGNSPNAPGCPDNkLNNPP-YVpnnlgggSLSDKTI 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 694 ------EGAGL-----------MAVSTA----SVVPKPPTFL---STPPA------------NATWEGLRETLGAVLNYG 737
Cdd:cd06602 206 cmdavhYDGGLhydvhnlyglsEAIATYkalkEIFPGKRPFIisrSTFPGsgkyaghwlgdnYSTWEDMRYSIPGMLEFN 285
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571438 738 VIGYPFVLPGVIG--GDyllqrplskmvsfyslsqpplPDPELFIRWLQLATFMPamqFS 795
Cdd:cd06602 286 LFGIPMVGADICGfnGN---------------------TTEELCARWMQLGAFYP---FS 321
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH