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Conserved domains on  [gi|119393893|ref|NP_001073271|]
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lysosomal alpha-glucosidase preproprotein [Homo sapiens]

Protein Classification

glycoside hydrolase family 31 protein( domain architecture ID 12184318)

glycoside hydrolase family 31 protein cleaves a terminal carbohydrate moiety from a substrate that varies in size and may be either a starch or a glycoprotein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
340-824 0e+00

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: 653.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  340 YIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKD 419
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  420 GFRDFPAMVQELHQGGRRYMMIVDPAISSSGPagSYRPYDEGLRRGVFITNETGQPLIGKvWPGSTAFPDFTNPTALAWW 499
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDP--GYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  500 EDMVAEFHDQVPFDGMWIDMNEPSNFirGSEDGCPNNELENPPYVPgvvggtlqaaticasshqflSTHYNLHNLYGLTE 579
Cdd:pfam01055 158 ADQLFKFLLDMGVDGIWNDMNEPSVF--CGSGPEDTVAKDNDPGGG--------------------VEHYDVHNLYGLLM 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  580 AIASHRALVKARG-TRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELC 658
Cdd:pfam01055 216 AKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELY 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  659 VRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTW 738
Cdd:pfam01055 296 VRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTF 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  739 TVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTvpvealgslppppaaprePAIHSEGQWVTLPAPLDTINVHL 818
Cdd:pfam01055 376 DIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWT------------------GERYEGGGTVPVTAPLDRIPLFV 437

                  ....*.
gi 119393893  819 RAGYII 824
Cdd:pfam01055 438 RGGSII 443
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
159-254 4.36e-43

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


:

Pssm-ID: 465286  Cd Length: 113  Bit Score: 152.25  E-value: 4.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  159 FFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLE---TPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTT 235
Cdd:pfam16863  15 LYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPEEllpRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTS 94
                          90
                  ....*....|....*....
gi 119393893  236 VAPLFFADQFLQLSTSLPS 254
Cdd:pfam16863  95 GGPLVFEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
246-359 6.10e-26

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


:

Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 103.42  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 246 LQLSTSLP-SQYITGLAEHLSPLmlSTSWTRITLWNRDLAPTPGA--NLYGSHPFYLALEdggsAHGVFLLNSNAMDVVL 322
Cdd:cd14752   10 LRLSFKLPpDEHFYGLGERFGGL--NKRGKRYRLWNTDQGGYRGStdPLYGSIPFYLSSK----GYGVFLDNPSRTEFDF 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119393893 323 QPS--PALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVG 359
Cdd:cd14752   84 GSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
81-132 1.06e-16

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


:

Pssm-ID: 197472  Cd Length: 46  Bit Score: 74.34  E-value: 1.06e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119393893    81 QCDVPPNSRFDCAPDkAITQEQCEARGCCYIPAKqglqgaqMGQPWCFFPPS 132
Cdd:smart00018   2 QCSVPPSERINCGPP-GITEAECEARGCCFDSSI-------SGVPWCFYPNT 45
 
Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
340-824 0e+00

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: 653.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  340 YIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKD 419
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  420 GFRDFPAMVQELHQGGRRYMMIVDPAISSSGPagSYRPYDEGLRRGVFITNETGQPLIGKvWPGSTAFPDFTNPTALAWW 499
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDP--GYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  500 EDMVAEFHDQVPFDGMWIDMNEPSNFirGSEDGCPNNELENPPYVPgvvggtlqaaticasshqflSTHYNLHNLYGLTE 579
Cdd:pfam01055 158 ADQLFKFLLDMGVDGIWNDMNEPSVF--CGSGPEDTVAKDNDPGGG--------------------VEHYDVHNLYGLLM 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  580 AIASHRALVKARG-TRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELC 658
Cdd:pfam01055 216 AKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELY 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  659 VRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTW 738
Cdd:pfam01055 296 VRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTF 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  739 TVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTvpvealgslppppaaprePAIHSEGQWVTLPAPLDTINVHL 818
Cdd:pfam01055 376 DIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWT------------------GERYEGGGTVPVTAPLDRIPLFV 437

                  ....*.
gi 119393893  819 RAGYII 824
Cdd:pfam01055 438 RGGSII 443
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
359-717 0e+00

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: 649.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06602    1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAISSSgPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWID 518
Cdd:cd06602   81 VPILDPGISAN-ESGGYPPYDRGLEMDVFIKNDDGSPYVGKVWPGYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLWID 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 519 MNEPSNFIRGSED------GCPNNELENPPYVPGVV-GGTLQAATICASSHQF-LSTHYNLHNLYGLTEAIASHRALVKA 590
Cdd:cd06602  160 MNEPSNFCTGSCGnspnapGCPDNKLNNPPYVPNNLgGGSLSDKTICMDAVHYdGGLHYDVHNLYGLSEAIATYKALKEI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 591 -RGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYP 669
Cdd:cd06602  240 fPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAFYP 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 119393893 670 FMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAH 717
Cdd:cd06602  320 FSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
253-866 5.10e-110

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 352.54  E-value: 5.10e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 253 PSQYITGLAEHLSPLmlSTSWTRITLWNRDLAP-TPGANLYGSHPFYLALEDGGsahgvFLLNSNAM---DVVLQPSPAL 328
Cdd:COG1501   60 LGEQIYGLGERFTTL--HKRGRIVVNWNLDHGGhKDNGNTYAPIPFYVSSKGYG-----VFVNSASYvtfDVGSAYSDLV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 329 SWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYM 408
Cdd:COG1501  133 EFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIRWM 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 409 DS--RRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPagsyrPYDEGlrRGVFITNETGQPLIGKVWPGSTA 486
Cdd:COG1501  213 DKyyWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSA-----IFAEG--MANFVKIASGTVFVGKMWPGTTG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 487 FPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEpsnfirgsedGCPNNELENPPYVPgvvggtlqaaticassHQFls 566
Cdd:COG1501  286 LLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNE----------GWPTDVATFPSNVP----------------QQM-- 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 567 thynlHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADV 646
Cdd:COG1501  338 -----RNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDI 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 647 CGFLGNTSEELCVRWTQLGAFYPFMRNHNSllSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARP 726
Cdd:COG1501  413 GGFFGSPSRELWIRWFQVGAFSPFARIHGW--ASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGTPVIRP 490
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 727 LFLEFPKDSSTWTVDHQLLWGEALLITPVLqAGKAEVTGYFPLGTWYDLQTvpvealGSLPpppaaprepaihSEGQWVT 806
Cdd:COG1501  491 LFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWT------GELI------------EGGQWIT 551
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 807 LPAPLDTINVHLRAGYIIPLqGPGLTTTeSRQQPMALAVALTKGGEARGELFWDDGESLE 866
Cdd:COG1501  552 VTAPLDRLPLYVRDGSIIPL-GPVSLRP-SMQKIDGIELRVYGSGETAYTLYDDDGETVS 609
alpha_gluc_MalA NF040948
alpha-glucosidase MalA;
274-777 1.03e-108

alpha-glucosidase MalA;


Pssm-ID: 468879 [Multi-domain]  Cd Length: 626  Bit Score: 349.71  E-value: 1.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 274 TRITLWNRDL-APTPGAN-LYGSHPFYLALeDGGSAHGVFLlNSNA---MDV---------VLQPSPALswrstggilDV 339
Cdd:NF040948  78 GRFIMYNVDAgAYTKYSDpLYVSIPFFISV-KGGKATGYFV-NSPSkliFDIglerydkvkITIPENSV---------EL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 340 YIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKD 419
Cdd:NF040948 147 YVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEVVDELRKEGFPVSAVYLDIDYMDSYKLFTWDKE 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 420 GFRDFPAMVQELHQGGRRYMMIVDPAISSSGpagSYRPYDEGLrrGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWW 499
Cdd:NF040948 227 KFPDPRKFIEELHSRGVKVITIVDPSVKADQ---NYEVFRSGL--GKYCETENGELYVGKLWPGNSVFPDFLNEETREWW 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 500 EDMVAEFHDQVPFDGMWIDMNEPSNFirgsedgcpNNELENPPYVPGVVGGTLQAATICASSHQFLS-----THYNLHNL 574
Cdd:NF040948 302 AELVEEWVKQYGVDGIWLDMNEPTDF---------TEDIERAALGPHQLREDRLLYTFPPGAVHRLDdgkkvKHEKVRNA 372
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 575 YGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLG--- 651
Cdd:NF040948 373 YPYFEAMATYEGLKRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWDDLKLQLQLVLGLSISGVPYVGCDIGGFAGrsf 452
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 652 --NTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFL 729
Cdd:NF040948 453 piDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFLPSKYKEKVKRVIKLRYKFLPYLYSLAWEAHETGHPIIRPLFY 532
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 119393893 730 EFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQT 777
Cdd:NF040948 533 EFQDDEDAYRIEDEYMVGKYLLYAPQIYPKEESRDVYLPRGKWLDFWT 580
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
275-897 1.27e-103

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 345.72  E-value: 1.27e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 275 RITLWNRDlAPTPGAN---LYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVV 351
Cdd:PLN02763  92 RVYTWNTD-AWGYGQNttsLYQSHPWVFVVLPNGEALGVLADTTRRCEIDLRKESIIRIIAPASYPVITFGPFPSPEALL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 352 QQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQEL 431
Cdd:PLN02763 171 TSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDL 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 432 HQGGRRYMMIVDPAISSSGpagSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDqVP 511
Cdd:PLN02763 251 HSIGFKAIWMLDPGIKAEE---GYFVYDSGCENDVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLVKDFVS-NG 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 512 FDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVvggtlqaaticaSSHqflsTHYnlHNLYGLTEAIASHRALVKAR 591
Cdd:PLN02763 327 VDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELGGV------------QNH----SHY--HNVYGMLMARSTYEGMLLAN 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 592 GT-RPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPF 670
Cdd:PLN02763 389 KNkRPFVLTRAGFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPF 468
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 671 MRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEAL 750
Cdd:PLN02763 469 ARGHSEQGTIDHEPWSFGEECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLL 548
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 751 LITPVL-QAGKAEVTGYFPLGTWydlqtvpvealgslppppaaprePAIHSEGQWVTLPApldtinVHLRAGYIIPLQGP 829
Cdd:PLN02763 549 ISASTLpDQGSDNLQHVLPKGIW-----------------------QRFDFDDSHPDLPL------LYLQGGSIIPLGPP 599
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 830 GLTTTE-SRQQPMALAVALTKGGEARGELFWDDGESLEvLERGAYTQVIFLARNNTIVnELVRVTS-EGA 897
Cdd:PLN02763 600 IQHVGEaSLSDDLTLLIALDENGKAEGVLYEDDGDGFG-YTKGDYLLTHYEAELVSSE-VTVRVAStEGS 667
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
159-254 4.36e-43

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


Pssm-ID: 465286  Cd Length: 113  Bit Score: 152.25  E-value: 4.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  159 FFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLE---TPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTT 235
Cdd:pfam16863  15 LYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPEEllpRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTS 94
                          90
                  ....*....|....*....
gi 119393893  236 VAPLFFADQFLQLSTSLPS 254
Cdd:pfam16863  95 GGPLVFEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
246-359 6.10e-26

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 103.42  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 246 LQLSTSLP-SQYITGLAEHLSPLmlSTSWTRITLWNRDLAPTPGA--NLYGSHPFYLALEdggsAHGVFLLNSNAMDVVL 322
Cdd:cd14752   10 LRLSFKLPpDEHFYGLGERFGGL--NKRGKRYRLWNTDQGGYRGStdPLYGSIPFYLSSK----GYGVFLDNPSRTEFDF 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119393893 323 QPS--PALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVG 359
Cdd:cd14752   84 GSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
81-132 1.06e-16

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


Pssm-ID: 197472  Cd Length: 46  Bit Score: 74.34  E-value: 1.06e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119393893    81 QCDVPPNSRFDCAPDkAITQEQCEARGCCYIPAKqglqgaqMGQPWCFFPPS 132
Cdd:smart00018   2 QCSVPPSERINCGPP-GITEAECEARGCCFDSSI-------SGVPWCFYPNT 45
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
81-130 2.98e-16

P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs.


Pssm-ID: 238059  Cd Length: 44  Bit Score: 73.15  E-value: 2.98e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119393893  81 QCDVPPNSRFDCAPDkAITQEQCEARGCCYIPakqglqgAQMGQPWCFFP 130
Cdd:cd00111    2 WCSVPPSERIDCGPP-GITQEECEARGCCFDP-------SISGVPWCFYP 43
Trefoil pfam00088
Trefoil (P-type) domain;
82-130 5.12e-16

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 72.35  E-value: 5.12e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 119393893   82 CD-VPPNSRFDCAPdKAITQEQCEARGCCYIPAkqglqgAQMGQPWCFFP 130
Cdd:pfam00088   1 CSsVPPSDRFDCGY-PGITQEECEARGCCWDPS------VDPGVPWCFYP 43
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
256-315 3.03e-08

Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.


Pssm-ID: 463987 [Multi-domain]  Cd Length: 67  Bit Score: 51.31  E-value: 3.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119393893  256 YITGLAEHLSPLMLSTswTRITLWNRDlAPTPGAN---LYGSHPFYLALEDgGSAHGVFLLNS 315
Cdd:pfam13802   3 HVYGLGERAGPLNKRG--TRYRLWNTD-AFGYELDtdpLYKSIPFYISHNG-GRGYGVFWDNP 61
 
Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
340-824 0e+00

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: 653.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  340 YIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKD 419
Cdd:pfam01055   1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  420 GFRDFPAMVQELHQGGRRYMMIVDPAISSSGPagSYRPYDEGLRRGVFITNETGQPLIGKvWPGSTAFPDFTNPTALAWW 499
Cdd:pfam01055  81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKVDP--GYPPYDEGLEKGYFVKNPDGSLYVGG-WPGMSAFPDFTNPEARDWW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  500 EDMVAEFHDQVPFDGMWIDMNEPSNFirGSEDGCPNNELENPPYVPgvvggtlqaaticasshqflSTHYNLHNLYGLTE 579
Cdd:pfam01055 158 ADQLFKFLLDMGVDGIWNDMNEPSVF--CGSGPEDTVAKDNDPGGG--------------------VEHYDVHNLYGLLM 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  580 AIASHRALVKARG-TRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELC 658
Cdd:pfam01055 216 AKATYEGLREKRPnKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELY 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  659 VRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTW 738
Cdd:pfam01055 296 VRWYQLGAFSPFFRNHSSIDTRRREPWLFGEEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTF 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  739 TVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTvpvealgslppppaaprePAIHSEGQWVTLPAPLDTINVHL 818
Cdd:pfam01055 376 DIDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWT------------------GERYEGGGTVPVTAPLDRIPLFV 437

                  ....*.
gi 119393893  819 RAGYII 824
Cdd:pfam01055 438 RGGSII 443
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
359-717 0e+00

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: 649.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06602    1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAISSSgPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWID 518
Cdd:cd06602   81 VPILDPGISAN-ESGGYPPYDRGLEMDVFIKNDDGSPYVGKVWPGYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLWID 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 519 MNEPSNFIRGSED------GCPNNELENPPYVPGVV-GGTLQAATICASSHQF-LSTHYNLHNLYGLTEAIASHRALVKA 590
Cdd:cd06602  160 MNEPSNFCTGSCGnspnapGCPDNKLNNPPYVPNNLgGGSLSDKTICMDAVHYdGGLHYDVHNLYGLSEAIATYKALKEI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 591 -RGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYP 669
Cdd:cd06602  240 fPGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAFYP 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 119393893 670 FMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAH 717
Cdd:cd06602  320 FSRNHNDIGAIDQEPYVWGPSVADASRKALLIRYSLLPYLYTLFYRAH 367
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
359-864 5.33e-157

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: 470.08  E-value: 5.33e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06603    1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAISSSGpagSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWedmvAEFHDQVPFDGM--- 515
Cdd:cd06603   81 VTIVDPHIKRDD---DYFVYKEAKEKDYFVKDSDGKDFEGWCWPGSSSWPDFLNPEVRDWW----ASLFSYDKYKGSten 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 516 ---WIDMNEPSNFiRGSEdgcpnnelenppyvpgvvgGTLQAATIcassHQFLSTHYNLHNLYGLTEAIASHRALVKARG 592
Cdd:cd06603  154 lyiWNDMNEPSVF-NGPE-------------------ITMPKDAI----HYGGVEHRDVHNIYGLYMHMATFEGLLKRSN 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 593 T--RPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPF 670
Cdd:cd06603  210 GkkRPFVLTRSFFAGSQRYGAVWTGDNMATWEHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPF 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 671 MRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEAL 750
Cdd:cd06603  290 FRAHAHIDTKRREPWLFGEETTEIIREAIRLRYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDSL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 751 LITPVLQAGKAEVTGYFPLGT-WYDLQTvpvealgslppppaaprePAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQG- 828
Cdd:cd06603  370 LVKPVVEEGATSVTVYLPGGEvWYDYFT------------------GQRVTGGGTKTVPVPLDSIPVFQRGGSIIPRKEr 431
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 119393893 829 PGLTTTESRQQPMALAVALTKGGEARGELFWDDGES 864
Cdd:cd06603  432 VRRSSKLMRNDPYTLVVALDENGEAEGELYLDDGES 467
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
359-717 6.77e-137

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: 413.06  E-value: 6.77e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06604    1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDKERFPDPKELIKELHEQGFRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAIS-SSGpagsYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQvPFDGMWI 517
Cdd:cd06604   81 VTIVDPGVKvDPG----YEVYEEGLENDYFVKDPDGELYVGKVWPGKSVFPDFTNPEVREWWGDLYKELVDL-GVDGIWN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 518 DMNEPSNFIRGSEDGCPnnelenPPYVPGVVGGTLqaaticasshqflsTHYNLHNLYGLTEAIASHRALVKAR-GTRPF 596
Cdd:cd06604  156 DMNEPAVFNAPGGTTMP------LDAVHRLDGGKI--------------THEEVHNLYGLLMARATYEGLRRLRpNKRPF 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 597 VISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNS 676
Cdd:cd06604  216 VLSRAGYAGIQRYAAIWTGDNSSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARWYQLGAFFPFFRNHSA 295
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 119393893 677 LLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAH 717
Cdd:cd06604  296 KGTRDQEPWAFGEEVEEIARKAIELRYRLLPYLYTLFYEAH 336
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
253-866 5.10e-110

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 352.54  E-value: 5.10e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 253 PSQYITGLAEHLSPLmlSTSWTRITLWNRDLAP-TPGANLYGSHPFYLALEDGGsahgvFLLNSNAM---DVVLQPSPAL 328
Cdd:COG1501   60 LGEQIYGLGERFTTL--HKRGRIVVNWNLDHGGhKDNGNTYAPIPFYVSSKGYG-----VFVNSASYvtfDVGSAYSDLV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 329 SWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYM 408
Cdd:COG1501  133 EFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHLDIRWM 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 409 DS--RRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPagsyrPYDEGlrRGVFITNETGQPLIGKVWPGSTA 486
Cdd:COG1501  213 DKyyWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDSA-----IFAEG--MANFVKIASGTVFVGKMWPGTTG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 487 FPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEpsnfirgsedGCPNNELENPPYVPgvvggtlqaaticassHQFls 566
Cdd:COG1501  286 LLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNE----------GWPTDVATFPSNVP----------------QQM-- 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 567 thynlHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADV 646
Cdd:COG1501  338 -----RNLYGLLEAKATFEGFRTSRNNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTPDI 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 647 CGFLGNTSEELCVRWTQLGAFYPFMRNHNSllSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARP 726
Cdd:COG1501  413 GGFFGSPSRELWIRWFQVGAFSPFARIHGW--ASSTEPWFFDEEAKQIVKEYAQLRYRLLPYIYSLFAKASTDGTPVIRP 490
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 727 LFLEFPKDSSTWTVDHQLLWGEALLITPVLqAGKAEVTGYFPLGTWYDLQTvpvealGSLPpppaaprepaihSEGQWVT 806
Cdd:COG1501  491 LFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWT------GELI------------EGGQWIT 551
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 807 LPAPLDTINVHLRAGYIIPLqGPGLTTTeSRQQPMALAVALTKGGEARGELFWDDGESLE 866
Cdd:COG1501  552 VTAPLDRLPLYVRDGSIIPL-GPVSLRP-SMQKIDGIELRVYGSGETAYTLYDDDGETVS 609
alpha_gluc_MalA NF040948
alpha-glucosidase MalA;
274-777 1.03e-108

alpha-glucosidase MalA;


Pssm-ID: 468879 [Multi-domain]  Cd Length: 626  Bit Score: 349.71  E-value: 1.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 274 TRITLWNRDL-APTPGAN-LYGSHPFYLALeDGGSAHGVFLlNSNA---MDV---------VLQPSPALswrstggilDV 339
Cdd:NF040948  78 GRFIMYNVDAgAYTKYSDpLYVSIPFFISV-KGGKATGYFV-NSPSkliFDIglerydkvkITIPENSV---------EL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 340 YIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKD 419
Cdd:NF040948 147 YVIEGPTIEEVLETYSELTGKPFLPPKWALGYQISRYSYYPQDAVVEVVDELRKEGFPVSAVYLDIDYMDSYKLFTWDKE 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 420 GFRDFPAMVQELHQGGRRYMMIVDPAISSSGpagSYRPYDEGLrrGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWW 499
Cdd:NF040948 227 KFPDPRKFIEELHSRGVKVITIVDPSVKADQ---NYEVFRSGL--GKYCETENGELYVGKLWPGNSVFPDFLNEETREWW 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 500 EDMVAEFHDQVPFDGMWIDMNEPSNFirgsedgcpNNELENPPYVPGVVGGTLQAATICASSHQFLS-----THYNLHNL 574
Cdd:NF040948 302 AELVEEWVKQYGVDGIWLDMNEPTDF---------TEDIERAALGPHQLREDRLLYTFPPGAVHRLDdgkkvKHEKVRNA 372
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 575 YGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLG--- 651
Cdd:NF040948 373 YPYFEAMATYEGLKRAGKDEPFILSRSGYAGIQRYAAIWTGDNTSSWDDLKLQLQLVLGLSISGVPYVGCDIGGFAGrsf 452
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 652 --NTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFL 729
Cdd:NF040948 453 piDNSPELLVRYYQAALFFPLFRTHKSKDGNDQEPYFLPSKYKEKVKRVIKLRYKFLPYLYSLAWEAHETGHPIIRPLFY 532
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 119393893 730 EFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQT 777
Cdd:NF040948 533 EFQDDEDAYRIEDEYMVGKYLLYAPQIYPKEESRDVYLPRGKWLDFWT 580
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
275-897 1.27e-103

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 345.72  E-value: 1.27e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 275 RITLWNRDlAPTPGAN---LYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVV 351
Cdd:PLN02763  92 RVYTWNTD-AWGYGQNttsLYQSHPWVFVVLPNGEALGVLADTTRRCEIDLRKESIIRIIAPASYPVITFGPFPSPEALL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 352 QQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQEL 431
Cdd:PLN02763 171 TSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDL 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 432 HQGGRRYMMIVDPAISSSGpagSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDqVP 511
Cdd:PLN02763 251 HSIGFKAIWMLDPGIKAEE---GYFVYDSGCENDVWIQTADGKPFVGEVWPGPCVFPDFTNKKTRSWWANLVKDFVS-NG 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 512 FDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVvggtlqaaticaSSHqflsTHYnlHNLYGLTEAIASHRALVKAR 591
Cdd:PLN02763 327 VDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELGGV------------QNH----SHY--HNVYGMLMARSTYEGMLLAN 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 592 GT-RPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPF 670
Cdd:PLN02763 389 KNkRPFVLTRAGFIGSQRYAATWTGDNLSNWEHLHMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPF 468
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 671 MRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEAL 750
Cdd:PLN02763 469 ARGHSEQGTIDHEPWSFGEECEEVCRLALKRRYRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLL 548
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 751 LITPVL-QAGKAEVTGYFPLGTWydlqtvpvealgslppppaaprePAIHSEGQWVTLPApldtinVHLRAGYIIPLQGP 829
Cdd:PLN02763 549 ISASTLpDQGSDNLQHVLPKGIW-----------------------QRFDFDDSHPDLPL------LYLQGGSIIPLGPP 599
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 830 GLTTTE-SRQQPMALAVALTKGGEARGELFWDDGESLEvLERGAYTQVIFLARNNTIVnELVRVTS-EGA 897
Cdd:PLN02763 600 IQHVGEaSLSDDLTLLIALDENGKAEGVLYEDDGDGFG-YTKGDYLLTHYEAELVSSE-VTVRVAStEGS 667
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
359-705 1.01e-98

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: 310.19  E-value: 1.01e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06600    1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWDPVRFPEPKKFVDELHKNGQKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAISSSgpagsyrpydeglrrgvfitnetgqpligkvwpgstafpdftnptalaWWEDMVAEFHDQVPFDGMWID 518
Cdd:cd06600   81 VTIVDPGITRE------------------------------------------------WWAGLISEFLYSQGIDGIWID 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 519 MNEPSNFirgsedgcpnnelenppyvpgvvggtlqaaticasshqflsthYNLHNLYGLTEAIASHRALVKARGTRPFVI 598
Cdd:cd06600  113 MNEPSNF-------------------------------------------YKVHNLYGFYEAMATAEGLRTSHNERPFIL 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 599 SRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLL 678
Cdd:cd06600  150 SRSTFAGSQKYAAHWTGDNTASWDDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLVRWYQLGAFYPFSRSHKATD 229
                        330       340
                 ....*....|....*....|....*..
gi 119393893 679 SLPQEPYSFSEPAQQAMRKALTLRYAL 705
Cdd:cd06600  230 TKDQEPVLFPEYYKESVREILELRYKL 256
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
359-699 1.47e-62

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: 212.98  E-value: 1.47e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMD---SRRDFTFNKDGFRDFPAMVQELHQGG 435
Cdd:cd06589    1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSDWMDwggNWGGFTWNREKFPDPKGMIDELHDKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 436 RRYMMIVDPAISssgpagsyrpydeglrrgvfitnetgqpligkvwpgstafpdftnptalAWWEDMVAEFHDQVPFDGM 515
Cdd:cd06589   81 VKLGLIVKPRLR-------------------------------------------------DWWWENIKKLLLEQGVDGW 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 516 WIDMNEPSNFIRGSedgcpnnelenppyvpgvvggtlqaaticassHQFLSTHYNLHNLYGLTEAIASHRALVKARGT-R 594
Cdd:cd06589  112 WTDMGEPLPFDDAT--------------------------------FHNGGKAQKIHNAYPLNMAEATYEGQKKTFPNkR 159
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 595 PFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNT-SEELCVRWTQLGAFYPFMRN 673
Cdd:cd06589  160 PFILSRSGYAGAQRYPAIWSGDNTTTWDSLAFQIRAGLSASLSGVGYWGHDIGGFTGGDpDKELYTRWVQFGAFSPIFRL 239
                        330       340
                 ....*....|....*....|....*.
gi 119393893 674 HNSLLSLPQEPYSFSEPAQQAMRKAL 699
Cdd:cd06589  240 HGDNSPRDKEPWVYGEEALAIFRKYL 265
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
359-705 3.06e-48

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: 173.91  E-value: 3.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYM--DSRRDFTFNKDGFRDFPAMVQELHQGGR 436
Cdd:cd06593    1 GRPPLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPCDVIHLDCFWMkeDWWCDFEWDEERFPDPEGMIARLKEKGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 437 RYMMIVDPAISSSGPAgsyrpYDEGLRRGVFITNETGQPLIGKV-WPGSTAFPDFTNPTALAWWEDMV------------ 503
Cdd:cd06593   81 KVCLWINPYISQDSPL-----FKEAAEKGYLVKNPDGSPWHQWDgWQPGMGIIDFTNPEAVAWYKEKLkrlldmgvdvik 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 504 AEFHDQVPFDGMWIDmnepsnfirgSEDGcpnnelenppyvpgvvggtlqaaticasshqflsthYNLHNLYGL--TEAI 581
Cdd:cd06593  156 TDFGERIPEDAVYYD----------GSDG------------------------------------RKMHNLYPLlyNKAV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 582 AshRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRW 661
Cdd:cd06593  190 Y--EATKEVKGEEAVLWARSAWAGSQRYPVHWGGDSESTFEGMAASLRGGLSLGLSGFGFWSHDIGGFEGTPSPELYKRW 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 119393893 662 TQLGAFYPFMRNHNsllSLPQEPYSFSEPAQQAMRKALTLRYAL 705
Cdd:cd06593  268 TQFGLLSSHSRLHG---STPREPWEYGEEALDVVRKFAKLRYRL 308
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
359-715 6.33e-47

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: 170.94  E-value: 6.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFP-----LDVQW--NDLDYMDSRR-DFTFNKDGFRDFPAMVQE 430
Cdd:cd06598    1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPldgvvLDLYWfgGIIASPDGPMgDLDWDRKAFPDPAKMIAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 431 LHQGGRRYMMIVDPAISSSGPAgsyrpYDEGLRRGVFITNETGQ--PLIGKVWPGSTAFPDFTNPTALAWWEDMVaEFHD 508
Cdd:cd06598   81 LKQQGVGTILIEEPYVLKNSDE-----YDELVKKGLLAKDKAGKpePTLFNFWFGEGGMIDWSDPEARAWWHDRY-KDLI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 509 QVPFDGMWIDMNEPSNfirgsedgcpnnelenppYVPGVVGGTLQAATIcasshqflsthynlHNLYGLTEAIASHRALV 588
Cdd:cd06598  155 DMGVAGWWTDLGEPEM------------------HPPDMVHADGDAADV--------------HNIYNLLWAKSIYDGYQ 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 589 K-ARGTRPFVISRSTFAGHGRY-AGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGN--TSEELCVRWTQL 664
Cdd:cd06598  203 RnFPEQRPFIMSRSGTAGSQRYgVIPWSGDIGRTWGGLASQINLQLHMSLSGIDYYGSDIGGFARGetLDPELYTRWFQY 282
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119393893 665 GAFYPFMRNHNSLLsLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQ 715
Cdd:cd06598  283 GAFDPPVRPHGQNL-CNPETAPDREGTKAINRENIKLRYQLLPYYYSLAYR 332
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
363-772 1.87e-45

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: 167.78  E-value: 1.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 363 MPPYWGLgfhlcrWGYSSTAITRQVVENMT---RAH-FPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06592    1 RPPIWST------WAEYKYNINQEKVLEYAeeiRANgFPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAISSSGPAgsyrpYDEGLRRGVFIT-NETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWI 517
Cdd:cd06592   75 TLWVHPFINPDSPN-----FRELRDKGYLVKeDSGGPPLIVKWWNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 518 DMNEPSnfirgsedgcpnnelenppYVPGvvggtlqaatiCASSHQFLSTHYNLHNLYGLTEA----IASHRALVKARGT 593
Cdd:cd06592  150 DAGEAS-------------------YLPA-----------DPATFPSGLNPNEYTTLYAELAAefglLNEVRSGWKSQGL 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 594 RPFVisrstfaghgRYAGhwTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGflGN------TSEELCVRWTQLGAF 667
Cdd:cd06592  200 PLFV----------RMSD--KDSHWGYWNGLRSLIPTALTQGLLGYPFVLPDMIG--GNaygnfpPDKELYIRWLQLSAF 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 668 YPFMRnhnslLS-LPQEPYSfsEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLW 746
Cdd:cd06592  266 MPAMQ-----FSvAPWRNYD--EEVVDIARKLAKLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLL 338
                        410       420
                 ....*....|....*....|....*.
gi 119393893 747 GEALLITPVLQAGKAEVTGYFPLGTW 772
Cdd:cd06592  339 GDDILVAPVLEKGARSRDVYLPKGRW 364
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
359-720 4.34e-44

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: 163.35  E-value: 4.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRY 438
Cdd:cd06601    1 GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMFSNLHAQGFKC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 439 MMIVDPAISSsgpagsyrPYDEGLRRGVFITNetgqpligkvwPGStaFPDFTNPTALAWWEDMVAEFHDqVPFDGMWID 518
Cdd:cd06601   81 STNITPIITD--------PYIGGVNYGGGLGS-----------PGF--YPDLGRPEVREWWGQQYKYLFD-MGLEMVWQD 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 519 MNEP---SNFIRGSED--GCPNNELENPPYVPGVVGgtlqaaticasshqfLSTHYNLHNLYGLTEAIASHRALVKARGT 593
Cdd:cd06601  139 MTTPaiaPHKINGYGDmkTFPLRLLVTDDSVKNEHT---------------YKPAATLWNLYAYNLHKATYHGLNRLNAR 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 594 ---RPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGN--------TSEELCVRWT 662
Cdd:cd06601  204 pnrRNFIIGRGGYAGAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPISGSDIGGFASGsdenegkwCDPELLIRWV 283
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119393893 663 QLGAFYPFMRNH------NSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAG 720
Cdd:cd06601  284 QAGAFLPWFRNHydryikKKQQEKLYEPYYYYEPVLPICRKYVELRYRLMQVFYDAMYENTQNG 347
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
159-254 4.36e-43

N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like structure just N-terminal to the catalytic domain of maltase-glucoamylase in eukaryotes. It contributes to the architecture of the substrate-binding site, by donating a loop that comes into close contact with two regions in the catalytic domain thereby creating the site. This family is frequently found at the N-terminus of Glycosyl hydrolase 31, pfam01055.to which it contributes as above.


Pssm-ID: 465286  Cd Length: 113  Bit Score: 152.25  E-value: 4.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893  159 FFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLE---TPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTT 235
Cdd:pfam16863  15 LYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPEEllpRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTS 94
                          90
                  ....*....|....*....
gi 119393893  236 VAPLFFADQFLQLSTSLPS 254
Cdd:pfam16863  95 GGPLVFEDQFLQLSTRLPS 113
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
359-669 1.45e-40

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: 152.37  E-value: 1.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCRWGYSSTAITRQVVENM---TRAH-FPLDVQWNDLDY----MDSRRDFTFNKDGFRDFPAMVQE 430
Cdd:cd06599    1 GRPALPPRWSLGYLGSTMYYTEAPDAQEQILDFidtCREHdIPCDGFHLSSGYtsieDGKRYVFNWNKDKFPDPKAFFRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 431 LHQGGRRYMMIVDPAISSSGPAgsyrpYDEGLRRGVFITN-ETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQ 509
Cdd:cd06599   81 FHERGIRLVANIKPGLLTDHPH-----YDELAEKGAFIKDdDGGEPAVGRFWGGGGSYLDFTNPEGREWWKEGLKEQLLD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 510 VPFDGMWIDmnepsnfirgsedgcpNNELEnppyvpgvvggtLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVK 589
Cdd:cd06599  156 YGIDSVWND----------------NNEYE------------IWDDDAACCGFGKGGPISELRPIQPLLMARASREAQLE 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 590 AR-GTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNT-SEELCVRWTQLGAF 667
Cdd:cd06599  208 HApNKRPFVISRSGCAGIQRYAQTWSGDNRTSWKTLKYNIAMGLGMSLSGVANYGHDIGGFAGPApEPELFVRWVQNGIF 287

                 ..
gi 119393893 668 YP 669
Cdd:cd06599  288 QP 289
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
363-702 3.52e-39

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: 148.47  E-value: 3.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 363 MPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLD--VQ----WNDldymDSRRDFTFNKDGFRDFPAMVQELHQGGR 436
Cdd:cd06591    5 MLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDviVQdwfyWTE----QGWGDMKFDPERFPDPKGMVDELHKMNV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 437 RYMMIVDPAISSSGpagsyRPYDEGLRRGVFITNETGQPLIGkvwpGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMW 516
Cdd:cd06591   81 KLMISVWPTFGPGS-----ENYKELDEKGLLLRTNRGNGGFG----GGTAFYDATNPEAREIYWKQLKDNYFDKGIDAWW 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 517 IDMNEPsnfirgsedgcpnnelENPPYVPGVVGGTLQAATicasshqFLSTHynlhNLYGL--TEAIASH-RALVKARgt 593
Cdd:cd06591  152 LDATEP----------------ELDPYDFDNYDGRTALGP-------GAEVG----NAYPLmhAKGIYEGqRATGPDK-- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 594 RPFVISRSTFAGHGRY-AGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSE---------ELCVRWTQ 663
Cdd:cd06591  203 RVVILTRSAFAGQQRYgAAVWSGDISSSWETLRRQIPAGLNFGASGIPYWTTDIGGFFGGDPEpgeddpayrELYVRWFQ 282
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 119393893 664 LGAFYPFMRNHNSllSLPQEPY---SFSEPAQQAMRKALTLR 702
Cdd:cd06591  283 FGAFCPIFRSHGT--RPPREPNeiwSYGEEAYDILVKYIKLR 322
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
247-777 3.31e-35

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 143.50  E-value: 3.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 247 QLSTSlPSQYITGLAEHLSPLMlsTSWTRITLWNRDlAPTPGANLYGSHPFYLAledgGSAHGVFLLNSN------AMDV 320
Cdd:PRK10658 152 QLDLG-VGETVYGLGERFTAFV--KNGQTVDIWNRD-GGTSSEQAYKNIPFYLT----NRGYGVFVNHPQcvsfevGSEK 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 321 V--LQPSPAlswrstGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLcrwgysSTAITRQ--------VVEN 390
Cdd:PRK10658 224 VskVQFSVE------GEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWL------TTSFTTNydeatvnsFIDG 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 391 MTRAHFPLDV-----------QWNDldymdsrrdFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAgsyrpYD 459
Cdd:PRK10658 292 MAERDLPLHVfhfdcfwmkefQWCD---------FEWDPRTFPDPEGMLKRLKAKGLKICVWINPYIAQKSPL-----FK 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 460 EGLRRGVFITNETGQpligkVW------PGsTAFPDFTNPTALAWWEDMVAE------------FHDQVPFDGMWIDMNE 521
Cdd:PRK10658 358 EGKEKGYLLKRPDGS-----VWqwdkwqPG-MAIVDFTNPDACKWYADKLKGlldmgvdcfktdFGERIPTDVVWFDGSD 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 522 PsnfirgsedgcpnnelenppyvpgvvggtlqaaticasshqflsthYNLHNLYGLTEAIASHRALVKARGTRPFVI-SR 600
Cdd:PRK10658 432 P----------------------------------------------QKMHNYYTYLYNKTVFDVLKETRGEGEAVLfAR 465
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 601 STFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSllSL 680
Cdd:PRK10658 466 SATVGGQQFPVHWGGDCYSNYESMAESLRGGLSLGLSGFGFWSHDIGGFENTATADVYKRWCAFGLLSSHSRLHGS--KS 543
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 681 PQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAgK 760
Cdd:PRK10658 544 YRVPWAYDEEAVDVVRFFTKLKCRLMPYLYREAAEAHERGTPMMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVFSE-A 622
                        570
                 ....*....|....*..
gi 119393893 761 AEVTGYFPLGTWYDLQT 777
Cdd:PRK10658 623 GDVEYYLPEGRWTHLLT 639
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
575-777 6.35e-33

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: 130.54  E-value: 6.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 575 YGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNtS 654
Cdd:cd06596  126 FALNGVEDAADGIENNSNARPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGIFGG-S 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 655 EELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKD 734
Cdd:cd06596  205 PETYTRDLQWKAFTPVLMNMSGWAANDKQPWVFGEPYTSINRKYLKLKMRLMPYIYTYAREASVTGLPMVRAMFLEYPND 284
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119393893 735 SSTWT--VDHQLLWGEALLITPVLQAGKAEVTG----YFPLGTWYDLQT 777
Cdd:cd06596  285 PTAYGtaTQYQFMWGPDFLVAPVYQNTAAGNDVrngiYLPAGTWIDYWT 333
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
359-675 3.74e-31

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: 125.12  E-value: 3.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGlgFHLCRW---GYSSTAITRQVvENMTRAHFP-----LDVQWndldymDSRRDFTFNKDGFR--DFPAMV 428
Cdd:cd06597    1 GRAALPPKWA--FGHWVSaneWNSQAEVLELV-EEYLAYDIPvgavvIEAWS------DEATFYIFNDATGKwpDPKGMI 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 429 QELHQGGRRYMMIVDPAISSSG-PAGSYRP-YDEGLRRGVFITNETGQPLI-GKVWPGSTAFPDFTNPTALAWWedmvae 505
Cdd:cd06597   72 DSLHEQGIKVILWQTPVVKTDGtDHAQKSNdYAEAIAKGYYVKNGDGTPYIpEGWWFGGGSLIDFTNPEAVAWW------ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 506 fHDQVP--FDGMWIDmnepsnfirG-SEDGCPNNELENPPYVPGvvggtlqaaticasshqflSTHYNLHNLYGlTEAIA 582
Cdd:cd06597  146 -HDQRDylLDELGID---------GfKTDGGEPYWGEDLIFSDG-------------------KKGREMRNEYP-NLYYK 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 583 SHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNT-SEELCVRW 661
Cdd:cd06597  196 AYFDYIREIGNDGVLFSRAGDSGAQRYPIGWVGDQDSTFEGLQSALKAGLSAAWSGYPFWGWDIGGFSGPLpTAELYLRW 275
                        330
                 ....*....|....
gi 119393893 662 TQLGAFYPFMRNHN 675
Cdd:cd06597  276 TQLAAFSPIMQNHS 289
PRK10426 PRK10426
alpha-glucosidase; Provisional
417-821 2.54e-30

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 127.80  E-value: 2.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 417 NKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAgsyrpYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTAL 496
Cdd:PRK10426 264 DSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGDL-----CEEAAEKGYLAKDADGGDYLVEFGEFYAGVVDLTNPEAY 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 497 AWWEDMVAEFHDQVPFDGMWIDMNEpsnfirgsedgcpnnelenppYVP-------GVvggtlqAATIcasshqflsthy 569
Cdd:PRK10426 339 EWFKEVIKKNMIGLGCSGWMADFGE---------------------YLPtdaylhnGV------SAEI------------ 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 570 nLHNLYGLTEAIASHRAlVKARGTRPFVI--SRSTFAGHGRYAG-HWTGDV---WSSWEQLASSVPEILQFNLLGVPLVG 643
Cdd:PRK10426 380 -MHNAWPALWAKCNYEA-LEETGKLGEILffMRAGYTGSQKYSTlFWAGDQnvdWSLDDGLASVVPAALSLGMSGHGLHH 457
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 644 ADVCGF---LGNT-SEELCVRWTQLGAFYPFMRNHNSllSLPQEPYSF--SEPAQQAMRKALTLRYALLPHLYTLFHQAH 717
Cdd:PRK10426 458 SDIGGYttlFGMKrTKELLLRWCEFSAFTPVMRTHEG--NRPGDNWQFdsDAETIAHFARMTRVFTTLKPYLKELVAEAA 535
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 718 VAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTvpvealgslppppaaprePA 797
Cdd:PRK10426 536 KTGLPVMRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEEGRTDWTVYLPEDKWVHLWT------------------GE 597
                        410       420
                 ....*....|....*....|....
gi 119393893 798 IHSeGQWVTLPAPLDTINVHLRAG 821
Cdd:PRK10426 598 AFA-GGEITVEAPIGKPPVFYRAG 620
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
359-709 5.89e-27

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: 112.29  E-value: 5.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 359 GYPFMPPYWGLGFHLCR-WGYSSTAItRQVVENMTRAHFPLDV-----QW--NDLDYMDSRRDFTFNKDGFRDFPAMVQE 430
Cdd:cd06595    2 GKPPLIPRYALGNWWSRyWAYSDDDI-LDLVDNFKRNEIPLSVlvldmDWhiTDKKYKNGWTGYTWNKELFPDPKGFLDW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 431 LHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLrrGVFITNETGQPLigkvwpgstafpDFTNPTALAWWEDMVAEFHDQV 510
Cdd:cd06595   81 LHERGLRVGLNLHPAEGIRPHEEAYAEFAKYL--GIDPAKIIPIPF------------DVTDPKFLDAYFKLLIHPLEKQ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 511 PFDGMWIDmnepsnfirgsedgCPNNELENPPYVpgvvggtlqaaticasSHQFLSTHYNLHNLYglteaiashralvKA 590
Cdd:cd06595  147 GVDFWWLD--------------WQQGKDSPLAGL----------------DPLWWLNHYHYLDSG-------------RN 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 591 RGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLAssvpEILQFNL----LGVPLVGADVCGFLGNTSE-ELCVRWTQLG 665
Cdd:cd06595  184 GKRRPLILSRWGGLGSHRYPIGFSGDTEVSWETLA----FQPYFTAtaanVGYSWWSHDIGGHKGGIEDpELYLRWVQFG 259
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 119393893 666 AFYPFMRNH-NSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHL 709
Cdd:cd06595  260 VFSPILRLHsDKGPYYKREPWLWDAKTFEIAKDYLRLRHRLIPYL 304
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
246-359 6.10e-26

N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). 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 of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.


Pssm-ID: 270212 [Multi-domain]  Cd Length: 122  Bit Score: 103.42  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 246 LQLSTSLP-SQYITGLAEHLSPLmlSTSWTRITLWNRDLAPTPGA--NLYGSHPFYLALEdggsAHGVFLLNSNAMDVVL 322
Cdd:cd14752   10 LRLSFKLPpDEHFYGLGERFGGL--NKRGKRYRLWNTDQGGYRGStdPLYGSIPFYLSSK----GYGVFLDNPSRTEFDF 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119393893 323 QPS--PALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVG 359
Cdd:cd14752   84 GSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
423-674 1.12e-17

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: 85.33  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 423 DFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRpydEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDM 502
Cdd:cd06594   72 GWDELVKELKEQGIRVLGYINPFLANVGPLYSYK---EAEEKGYLVKNKTGEPYLVDFGEFDAGLVDLTNPEARRWFKEV 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 503 VAEFHDQVPFDGMWIDMNEpsnfirgsedgcpnnelenppYVPgvVGGTLqaaticASShqflSTHYNLHNLYGLTEAiA 582
Cdd:cd06594  149 IKENMIDFGLSGWMADFGE---------------------YLP--FDAVL------HSG----EDAALYHNRYPELWA-R 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393893 583 SHRALVKARGTRPFVI--SRSTFAGHGRYAG-HWTGD--V-WSSWEQLASSVPEILQFNLLGVPLVGADVCGF------- 649
Cdd:cd06594  195 LNREAVEEAGKEGEIVffMRSGYTGSPRYSTlFWAGDqnVdWSRDDGLKSVIPGALSSGLSGFSLTHSDIGGYttlfnpl 274
                        250       260
                 ....*....|....*....|....*.
gi 119393893 650 LGNT-SEELCVRWTQLGAFYPFMRNH 674
Cdd:cd06594  275 VGYKrSKELLMRWAEMAAFTPVMRTH 300
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
81-132 1.06e-16

P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.


Pssm-ID: 197472  Cd Length: 46  Bit Score: 74.34  E-value: 1.06e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 119393893    81 QCDVPPNSRFDCAPDkAITQEQCEARGCCYIPAKqglqgaqMGQPWCFFPPS 132
Cdd:smart00018   2 QCSVPPSERINCGPP-GITEAECEARGCCFDSSI-------SGVPWCFYPNT 45
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
81-130 2.98e-16

P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated molecules, largely found in epithelia of gastrointestinal tissues. Function is not known but it was originally identified from mucosal tissues, where it may have a regulatory or structural role and has also been implicated as a growth fractor in other tissues.The domain is found in 1 to 6 copies where it occurs.


Pssm-ID: 238059  Cd Length: 44  Bit Score: 73.15  E-value: 2.98e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119393893  81 QCDVPPNSRFDCAPDkAITQEQCEARGCCYIPakqglqgAQMGQPWCFFP 130
Cdd:cd00111    2 WCSVPPSERIDCGPP-GITQEECEARGCCFDP-------SISGVPWCFYP 43
Trefoil pfam00088
Trefoil (P-type) domain;
82-130 5.12e-16

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 72.35  E-value: 5.12e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 119393893   82 CD-VPPNSRFDCAPdKAITQEQCEARGCCYIPAkqglqgAQMGQPWCFFP 130
Cdd:pfam00088   1 CSsVPPSDRFDCGY-PGITQEECEARGCCWDPS------VDPGVPWCFYP 43
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
256-315 3.03e-08

Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and appears to be similar to the galactose mutarotase superfamily.


Pssm-ID: 463987 [Multi-domain]  Cd Length: 67  Bit Score: 51.31  E-value: 3.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119393893  256 YITGLAEHLSPLMLSTswTRITLWNRDlAPTPGAN---LYGSHPFYLALEDgGSAHGVFLLNS 315
Cdd:pfam13802   3 HVYGLGERAGPLNKRG--TRYRLWNTD-AFGYELDtdpLYKSIPFYISHNG-GRGYGVFWDNP 61
 
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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