NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370511246|ref|XP_024302765|]
View 

probable maltase-glucoamylase 2 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
 304-769 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: 587.22  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  304 YVFLGNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEV 383
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  384 AYSGLPDFVKELHDNGQKYLIIMNPGISK-NSNYEPYNNGSLKRVWILGSNGFAVGEGYPGPTVFPDYTNPVCTEWWTDQ 462
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKvDPGYPPYDEGLEKGYFVKNPDGSLYVGGWPGMSAFPDFTNPEARDWWADQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  463 VAKFHDHLEFDGVWIEMNEVSsllqasnnqcesnnlNFPPFLPRVLDHLLFartlcmdTEFHGGLHYDIHSLYGHSMART 542
Cdd:pfam01055  161 LFKFLLDMGVDGIWNDMNEPS---------------VFCGSGPEDTVAKDN-------DPGGGVEHYDVHNLYGLLMAKA 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  543 TNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRW 622
Cdd:pfam01055  219 TYEGLREKRPNKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRW 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  623 MQLGAFYPLPRNHNGPGFRDQDPAAFGvdSLLLKSSRHYLNIRYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWD 702
Cdd:pfam01055  299 YQLGAFSPFFRNHSSIDTRRREPWLFG--EEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFD 376

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511246  703 VHEQFLWGPGLLITPVLYEGVDEVKAYIPDATWYDYETGVAISwRKQLVNMLLPGDKIGLHLRGGYI 769
Cdd:pfam01055  377 IDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYE-GGGTVPVTAPLDRIPLFVRGGSI 442
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 104-215 1.12e-47

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: 165.73  E-value: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  104 GFTAQLKRLPSP-SLFGNDVATTLFTAEYQTSNRFHFKITDFNNIRYEVSHENINLVDGIADASNLSYYVEVTDKPFSIK 182
Cdd:pfam16863    1 GLTADLTLAGSPcNLYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1370511246  183 IMRTSNRRVLLDTSIGPLQFAQQYLQLSFRLPS 215
Cdd:pfam16863   81 VTRKSTGEVLFDTSGGPLVFEDQFLQLSTRLPS 113
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 991-1084 2.96e-34

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: 127.21  E-value: 2.96e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  991 ISFLHLKVIYHTATMLQVKIYDPTNKRYEVPVPLNTPPQPVGDPENRLYDVRIQNNPFGIQIQRKNSSTVIWDSQLPGFI 1070
Cdd:pfam16863   20 IETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTSGGPLV 99

                           90
                   ....*....|....
gi 1370511246 1071 FNDMFLSISTRLPS 1084
Cdd:pfam16863  100 FEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 207-323 7.54e-25

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: 100.72  E-value: 7.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  207 LQLSFRLP-SANVYGLGEHVHqqyRHNMTWKTWPIFTRDA-TPTEGMINLYGAHTFFLCLEdargsSFGVFLMNSNAMEV 284
Cdd:cd14752     10 LRLSFKLPpDEHFYGLGERFG---GLNKRGKRYRLWNTDQgGYRGSTDPLYGSIPFYLSSK-----GYGVFLDNPSRTEF 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370511246  285 TLQPA--PAITYRTIGGILDFYVFLGNTPEQVVQEYLELVG 323
Cdd:cd14752     82 DFGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 1076-1190 3.59e-23

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: 95.72  E-value: 3.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1076 LSISTRLP-SQYIYGFGEteHTTfRRNMNWNTWGMFAHD--EPPAYKKNSYGVHPYYMALEedgsAHGVLLLNSNAMDVT 1152
Cdd:cd14752     10 LRLSFKLPpDEHFYGLGE--RFG-GLNKRGKRYRLWNTDqgGYRGSTDPLYGSIPFYLSSK----GYGVFLDNPSRTEFD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1153 LQPT--PALTYRTTGGILDFYIVLGPTPELVTQQYTELIG 1190
Cdd:cd14752     83 FGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
Glyco_hydro_31 super family cl47624
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 1171-1229 9.46e-21

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


The actual alignment was detected with superfamily member pfam01055:

Pssm-ID: 460044 [Multi-domain]  Cd Length: 443  Bit Score: 96.86  E-value: 9.46e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511246 1171 YIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPL 59
Trefoil pfam00088
Trefoil (P-type) domain;
43-87 7.04e-12

Trefoil (P-type) domain;


:

Pssm-ID: 459666  Cd Length: 43  Bit Score: 61.18  E-value: 7.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370511246   43 CPEIPQSERIDCTPdQEVTEDICRWQyKCCWSPVADANVPRCFFP 87
Cdd:pfam00088    1 CSSVPPSDRFDCGY-PGITQEECEAR-GCCWDPSVDPGVPWCFYP 43
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 908-948 2.27e-10

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


:

Pssm-ID: 197472  Cd Length: 46  Bit Score: 57.01  E-value: 2.27e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370511246   908 VSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 948
Cdd:smart00018    5 VPPSERINCGPPGITEAE--CEARGCCF-DSSISGVPWCFY 42
 
Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 304-769 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: 587.22  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  304 YVFLGNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEV 383
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  384 AYSGLPDFVKELHDNGQKYLIIMNPGISK-NSNYEPYNNGSLKRVWILGSNGFAVGEGYPGPTVFPDYTNPVCTEWWTDQ 462
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKvDPGYPPYDEGLEKGYFVKNPDGSLYVGGWPGMSAFPDFTNPEARDWWADQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  463 VAKFHDHLEFDGVWIEMNEVSsllqasnnqcesnnlNFPPFLPRVLDHLLFartlcmdTEFHGGLHYDIHSLYGHSMART 542
Cdd:pfam01055  161 LFKFLLDMGVDGIWNDMNEPS---------------VFCGSGPEDTVAKDN-------DPGGGVEHYDVHNLYGLLMAKA 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  543 TNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRW 622
Cdd:pfam01055  219 TYEGLREKRPNKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRW 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  623 MQLGAFYPLPRNHNGPGFRDQDPAAFGvdSLLLKSSRHYLNIRYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWD 702
Cdd:pfam01055  299 YQLGAFSPFFRNHSSIDTRRREPWLFG--EEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFD 376

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511246  703 VHEQFLWGPGLLITPVLYEGVDEVKAYIPDATWYDYETGVAISwRKQLVNMLLPGDKIGLHLRGGYI 769
Cdd:pfam01055  377 IDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYE-GGGTVPVTAPLDRIPLFVRGGSI 442
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 323-680 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: 564.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKY 402
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  403 LIIMNPGISKN--SNYEPYNNGSLKRVWILGSNG-FAVGEGYPGPTVFPDYTNPVCTEWWTDQVAKFHDHLEFDGVWIEM 479
Cdd:cd06602     81 VPILDPGISANesGGYPPYDRGLEMDVFIKNDDGsPYVGKVWPGYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLWIDM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  480 NEVSSLLQAS------NNQCESNNLNFPPFLPRVL-DHLLFARTLCMD-TEFHGGLHYDIHSLYGHSMARTTNLALETIF 551
Cdd:cd06602    161 NEPSNFCTGScgnspnAPGCPDNKLNNPPYVPNNLgGGSLSDKTICMDaVHYDGGLHYDVHNLYGLSEAIATYKALKEIF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  552 MNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPL 631
Cdd:cd06602    241 PGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAFYPF 320

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1370511246  632 PRNHNGPGFRDQDPAAFGVDslLLKSSRHYLNIRYTLLPYLYTLFYHAH 680
Cdd:cd06602    321 SRNHNDIGAIDQEPYVWGPS--VADASRKALLIRYSLLPYLYTLFYRAH 367
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 203-808 5.87e-96

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 329.93  E-value: 5.87e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  203 AQQYLQLSFrLPSANVYGLGEHVHQQYRHN---MTWKTwpiftrDA-TPTEGMINLYGAHTF-FLCLEDarGSSFGVFLM 277
Cdd:PLN02763    62 DQQIVTFEL-PSGTSFYGTGEVSGPLERTGkrvYTWNT------DAwGYGQNTTSLYQSHPWvFVVLPN--GEALGVLAD 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  278 NSNAMEVTLQ-----------PAPAITyrtiggildFYVFlgNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGIN 346
Cdd:PLN02763   133 TTRRCEIDLRkesiiriiapaSYPVIT---------FGPF--PSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAK 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  347 KLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKYLIIMNPGISKNSNYEPYNNGSLKR 426
Cdd:PLN02763   202 RVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCEND 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  427 VWILGSNGFA-VGEGYPGPTVFPDYTNPVCTEWWTDQVAKFHDHlEFDGVWIEMNEVSSLLQASNNQCESNNLNFPPFLP 505
Cdd:PLN02763   282 VWIQTADGKPfVGEVWPGPCVFPDFTNKKTRSWWANLVKDFVSN-GVDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELG 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  506 RVLDHLlfartlcmdtefhgglHYdiHSLYGHSMARTTNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDL 585
Cdd:PLN02763   361 GVQNHS----------------HY--HNVYGMLMARSTYEGMLLANKNKRPFVLTRAGFIGSQRYAATWTGDNLSNWEHL 422

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  586 RWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLPRNHNGPGFRDQDPAAFGVDSLLLksSRHYLNIR 665
Cdd:PLN02763   423 HMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGEECEEV--CRLALKRR 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  666 YTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWDVHEQFLWGPGLLITPVLY-EGVDEVKAYIPDATW--YDYETGv 742
Cdd:PLN02763   501 YRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISASTLPdQGSDNLQHVLPKGIWqrFDFDDS- 579

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511246  743 aiswrkqlvNMLLPgdkiGLHLRGGYIFPTQKP-NTTTEASRRNSLGLIIALDYKREAKGELYWDDG 808
Cdd:PLN02763   580 ---------HPDLP----LLYLQGGSIIPLGPPiQHVGEASLSDDLTLLIALDENGKAEGVLYEDDG 633
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
214-810 2.67e-87

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 295.92  E-value: 2.67e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  214 PSANVYGLGEH---VHQQYRHNMTWktwpifTRDATPTEGMINLYGAHTFFLCLEDargssFGVFLmNSNAM---EVTLQ 287
Cdd:COG1501     60 LGEQIYGLGERfttLHKRGRIVVNW------NLDHGGHKDNGNTYAPIPFYVSSKG-----YGVFV-NSASYvtfDVGSA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  288 PAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYS 367
Cdd:COG1501    128 YSDLVEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  368 DIDYMD--GKKDFTVDEVAYSGLPDFVKELHDNGQKYLIIMNPGISKNSnyEPYNNGSLKRVWIlGSNGFAVGEGYPGPT 445
Cdd:COG1501    208 DIRWMDkyYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDS--AIFAEGMANFVKI-ASGTVFVGKMWPGTT 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  446 VFPDYTNPVCTEWWTDQVAKFHDHLEFDGVWIEMNEVssllqasnnqcesnnlnfppfLPRVLdhllfartlcmdTEFHG 525
Cdd:COG1501    285 GLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNEG---------------------WPTDV------------ATFPS 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  526 GLHYDIHSLYGHSMARTTNLALETIFmNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGA 605
Cdd:COG1501    332 NVPQQMRNLYGLLEAKATFEGFRTSR-NNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTP 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  606 NICGYNNNVTEELCRRWMQLGAFYPLPRNHNgpGFRDQDPAAFGVDSllLKSSRHYLNIRYTLLPYLYTLFYHAHTRGET 685
Cdd:COG1501    411 DIGGFFGSPSRELWIRWFQVGAFSPFARIHG--WASSTEPWFFDEEA--KQIVKEYAQLRYRLLPYIYSLFAKASTDGTP 486

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  686 VARPLVHEFYQDSATWDVHEQFLWGPGLLITPVLyEGVDEVKAYIPDATWYDYETGVAISwRKQLVNMLLPGDKIGLHLR 765
Cdd:COG1501    487 VIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIE-GGQWITVTAPLDRLPLYVR 564

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1370511246  766 GGYIFPTQKPNTTTEASRRNSLGLIIALDykREAKGELYWDDGVS 810
Cdd:COG1501    565 DGSIIPLGPVSLRPSMQKIDGIELRVYGS--GETAYTLYDDDGET 607
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 104-215 1.12e-47

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: 165.73  E-value: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  104 GFTAQLKRLPSP-SLFGNDVATTLFTAEYQTSNRFHFKITDFNNIRYEVSHENINLVDGIADASNLSYYVEVTDKPFSIK 182
Cdd:pfam16863    1 GLTADLTLAGSPcNLYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1370511246  183 IMRTSNRRVLLDTSIGPLQFAQQYLQLSFRLPS 215
Cdd:pfam16863   81 VTRKSTGEVLFDTSGGPLVFEDQFLQLSTRLPS 113
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 991-1084 2.96e-34

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: 127.21  E-value: 2.96e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  991 ISFLHLKVIYHTATMLQVKIYDPTNKRYEVPVPLNTPPQPVGDPENRLYDVRIQNNPFGIQIQRKNSSTVIWDSQLPGFI 1070
Cdd:pfam16863   20 IETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTSGGPLV 99

                           90
                   ....*....|....
gi 1370511246 1071 FNDMFLSISTRLPS 1084
Cdd:pfam16863  100 FEDQFLQLSTRLPS 113
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 207-323 7.54e-25

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: 100.72  E-value: 7.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  207 LQLSFRLP-SANVYGLGEHVHqqyRHNMTWKTWPIFTRDA-TPTEGMINLYGAHTFFLCLEdargsSFGVFLMNSNAMEV 284
Cdd:cd14752     10 LRLSFKLPpDEHFYGLGERFG---GLNKRGKRYRLWNTDQgGYRGSTDPLYGSIPFYLSSK-----GYGVFLDNPSRTEF 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370511246  285 TLQPA--PAITYRTIGGILDFYVFLGNTPEQVVQEYLELVG 323
Cdd:cd14752     82 DFGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 1076-1190 3.59e-23

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: 95.72  E-value: 3.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1076 LSISTRLP-SQYIYGFGEteHTTfRRNMNWNTWGMFAHD--EPPAYKKNSYGVHPYYMALEedgsAHGVLLLNSNAMDVT 1152
Cdd:cd14752     10 LRLSFKLPpDEHFYGLGE--RFG-GLNKRGKRYRLWNTDqgGYRGSTDPLYGSIPFYLSSK----GYGVFLDNPSRTEFD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1153 LQPT--PALTYRTTGGILDFYIVLGPTPELVTQQYTELIG 1190
Cdd:cd14752     83 FGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 1171-1229 9.46e-21

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: 96.86  E-value: 9.46e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511246 1171 YIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPL 59
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
1083-1229 1.57e-18

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 90.99  E-value: 1.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1083 PSQYIYGFGE---TEHTTFRRNMNWNTWGMFAHDEPPAYKknsygVHPYYMALEEDGsahgvLLLNSNAM---DVTLQPT 1156
Cdd:COG1501     60 LGEQIYGLGErftTLHKRGRIVVNWNLDHGGHKDNGNTYA-----PIPFYVSSKGYG-----VFVNSASYvtfDVGSAYS 129

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511246 1157 PALTYRTTGGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:COG1501    130 DLVEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPL 202
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 1190-1229 2.75e-13

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: 72.93  E-value: 2.75e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPL 40
Trefoil pfam00088
Trefoil (P-type) domain;
43-87 7.04e-12

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 61.18  E-value: 7.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370511246   43 CPEIPQSERIDCTPdQEVTEDICRWQyKCCWSPVADANVPRCFFP 87
Cdd:pfam00088    1 CSSVPPSDRFDCGY-PGITQEECEAR-GCCWDPSVDPGVPWCFYP 43
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 908-948 2.27e-10

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


Pssm-ID: 197472  Cd Length: 46  Bit Score: 57.01  E-value: 2.27e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370511246   908 VSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 948
Cdd:smart00018    5 VPPSERINCGPPGITEAE--CEARGCCF-DSSISGVPWCFY 42
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 907-948 7.73e-10

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: 55.43  E-value: 7.73e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370511246  907 PVSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 948
Cdd:cd00111      4 SVPPSERIDCGPPGITQEE--CEARGCCF-DPSISGVPWCFY 42
Trefoil pfam00088
Trefoil (P-type) domain;
908-948 1.32e-09

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 54.63  E-value: 1.32e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1370511246  908 VSDLEKFNCYPddPTASEESCRQRGCLWEDTSTPGVPTCYY 948
Cdd:pfam00088    4 VPPSDRFDCGY--PGITQEECEARGCCWDPSVDPGVPWCFY 42
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 1088-1228 2.60e-08

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 58.36  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1088 YGFGETE---HTTFRRNMNWNT--WGmfahdeppaYKKNS---YGVHPYYMALEEDGSAHGVLLLNSNAMDVTLQPTPAL 1159
Cdd:PLN02763    77 YGTGEVSgplERTGKRVYTWNTdaWG---------YGQNTtslYQSHPWVFVVLPNGEALGVLADTTRRCEIDLRKESII 147

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511246 1160 TYRTTGgildFY--IVLGP--TPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIP 1228
Cdd:PLN02763   148 RIIAPA----SYpvITFGPfpSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIP 216
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 42-89 8.50e-07

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


Pssm-ID: 197472  Cd Length: 46  Bit Score: 46.61  E-value: 8.50e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1370511246    42 ECpEIPQSERIDCTPDqEVTEDICRwQYKCCWSPvADANVPRCFFPWN 89
Cdd:smart00018    2 QC-SVPPSERINCGPP-GITEAECE-ARGCCFDS-SISGVPWCFYPNT 45
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 42-88 2.73e-06

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: 45.41  E-value: 2.73e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1370511246   42 ECPeIPQSERIDCTPdQEVTEDICRwQYKCCWSPvADANVPRCFFPW 88
Cdd:cd00111      2 WCS-VPPSERIDCGP-PGITQEECE-ARGCCFDP-SISGVPWCFYPK 44
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
 1165-1228 5.36e-05

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 47.58  E-value: 5.36e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511246 1165 GGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLS-----RYgyqNDAEISSLYDAMVAAQIP 1228
Cdd:PRK10658   233 GEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWLTtsfttNY---DEATVNSFIDGMAERDLP 298
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
 217-284 6.49e-04

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: 39.37  E-value: 6.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511246  217 NVYGLGEHV------HQQYRhnmtwktwpIFTRDA-TPTEGMINLYGAHTFFLCLEDarGSSFGVFLMNSNAMEV 284
Cdd:pfam13802    3 HVYGLGERAgplnkrGTRYR---------LWNTDAfGYELDTDPLYKSIPFYISHNG--GRGYGVFWDNPAETWF 66
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
 1086-1146 3.56e-03

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: 37.06  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511246 1086 YIYGFGetEHTT-FRRNM----NWNTWGMfahdEPPAYKKNSYGVHPYYMALeEDGSAHGVLLLNS 1146
Cdd:pfam13802    3 HVYGLG--ERAGpLNKRGtryrLWNTDAF----GYELDTDPLYKSIPFYISH-NGGRGYGVFWDNP 61
 
Name Accession Description Interval E-value
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 304-769 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: 587.22  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  304 YVFLGNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEV 383
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPLDVIWLDIDYMDGYRDFTWDPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  384 AYSGLPDFVKELHDNGQKYLIIMNPGISK-NSNYEPYNNGSLKRVWILGSNGFAVGEGYPGPTVFPDYTNPVCTEWWTDQ 462
Cdd:pfam01055   81 RFPDPKGMVDELHAKGQKLVVIIDPGIKKvDPGYPPYDEGLEKGYFVKNPDGSLYVGGWPGMSAFPDFTNPEARDWWADQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  463 VAKFHDHLEFDGVWIEMNEVSsllqasnnqcesnnlNFPPFLPRVLDHLLFartlcmdTEFHGGLHYDIHSLYGHSMART 542
Cdd:pfam01055  161 LFKFLLDMGVDGIWNDMNEPS---------------VFCGSGPEDTVAKDN-------DPGGGVEHYDVHNLYGLLMAKA 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  543 TNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRW 622
Cdd:pfam01055  219 TYEGLREKRPNKRPFVLTRSGFAGSQRYAAHWSGDNTSTWEHLRFSIPGGLSLGLSGIPFWGADIGGFFNPTTPELYVRW 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  623 MQLGAFYPLPRNHNGPGFRDQDPAAFGvdSLLLKSSRHYLNIRYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWD 702
Cdd:pfam01055  299 YQLGAFSPFFRNHSSIDTRRREPWLFG--EEVEEIIRKAIRLRYRLLPYLYTLFYEAHETGLPVMRPLFLEFPDDPNTFD 376

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511246  703 VHEQFLWGPGLLITPVLYEGVDEVKAYIPDATWYDYETGVAISwRKQLVNMLLPGDKIGLHLRGGYI 769
Cdd:pfam01055  377 IDDQFMFGPSLLVAPVLEEGATSVDVYLPGGRWYDFWTGERYE-GGGTVPVTAPLDRIPLFVRGGSI 442
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 323-680 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: 564.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKY 402
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPLDVQWNDIDYMDRYRDFTLDPVNFPGLPAFVDDLHANGQHY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  403 LIIMNPGISKN--SNYEPYNNGSLKRVWILGSNG-FAVGEGYPGPTVFPDYTNPVCTEWWTDQVAKFHDHLEFDGVWIEM 479
Cdd:cd06602     81 VPILDPGISANesGGYPPYDRGLEMDVFIKNDDGsPYVGKVWPGYTVFPDFTNPNTQEWWTEEIKDFHDQVPFDGLWIDM 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  480 NEVSSLLQAS------NNQCESNNLNFPPFLPRVL-DHLLFARTLCMD-TEFHGGLHYDIHSLYGHSMARTTNLALETIF 551
Cdd:cd06602    161 NEPSNFCTGScgnspnAPGCPDNKLNNPPYVPNNLgGGSLSDKTICMDaVHYDGGLHYDVHNLYGLSEAIATYKALKEIF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  552 MNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPL 631
Cdd:cd06602    241 PGKRPFIISRSTFPGSGKYAGHWLGDNYSTWEDMRYSIPGMLEFNLFGIPMVGADICGFNGNTTEELCARWMQLGAFYPF 320

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1370511246  632 PRNHNGPGFRDQDPAAFGVDslLLKSSRHYLNIRYTLLPYLYTLFYHAH 680
Cdd:cd06602    321 SRNHNDIGAIDQEPYVWGPS--VADASRKALLIRYSLLPYLYTLFYRAH 367
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
 323-683 2.38e-109

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: 346.80  E-value: 2.38e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKY 402
Cdd:cd06604      1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIPCDAIYLDIDYMDGYRVFTWDKERFPDPKELIKELHEQGFRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  403 LIIMNPGISKNSNYEPYNNGSLKRVWILGSNG-FAVGEGYPGPTVFPDYTNPVCTEWWTDQVAKFHDhLEFDGVWIEMNE 481
Cdd:cd06604     81 VTIVDPGVKVDPGYEVYEEGLENDYFVKDPDGeLYVGKVWPGKSVFPDFTNPEVREWWGDLYKELVD-LGVDGIWNDMNE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  482 VSSLlqasnnqcesnNLNFPPFLPRVLDHllfartlcmDTEFHGGLHYDIHSLYGHSMARTTNLALETIFMNNRSFILSR 561
Cdd:cd06604    160 PAVF-----------NAPGGTTMPLDAVH---------RLDGGKITHEEVHNLYGLLMARATYEGLRRLRPNKRPFVLSR 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  562 STFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLPRNHNGPGFR 641
Cdd:cd06604    220 AGYAGIQRYAAIWTGDNSSSWEHLRLSIPMLLNLGLSGVPFVGADIGGFAGDPSPELLARWYQLGAFFPFFRNHSAKGTR 299

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1370511246  642 DQDPAAFGVDSllLKSSRHYLNIRYTLLPYLYTLFYHAHTRG 683
Cdd:cd06604    300 DQEPWAFGEEV--EEIARKAIELRYRLLPYLYTLFYEAHETG 339
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
 323-668 6.18e-104

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: 328.68  E-value: 6.18e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKY 402
Cdd:cd06600      1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPYDVMWLDIDYMDSYKDFTWDPVRFPEPKKFVDELHKNGQKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  403 LIIMNPGIsknsnyepynngslkrvwilgsngfavgegypgptvfpdytnpvCTEWWTDQVAKFHDHLEFDGVWIEMNEV 482
Cdd:cd06600     81 VTIVDPGI--------------------------------------------TREWWAGLISEFLYSQGIDGIWIDMNEP 116

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  483 SsllqasnnqcesnnlNFppflprvldhllfartlcmdtefhgglhYDIHSLYGHSMARTTNLALETIfMNNRSFILSRS 562
Cdd:cd06600    117 S---------------NF----------------------------YKVHNLYGFYEAMATAEGLRTS-HNERPFILSRS 152

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  563 TFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLPRNHNGPGFRD 642
Cdd:cd06600    153 TFAGSQKYAAHWTGDNTASWDDLKLSIPLVLGLSLSGIPFVGADIGGFAGDTSEELLVRWYQLGAFYPFSRSHKATDTKD 232

                          330       340
                   ....*....|....*....|....*.
gi 1370511246  643 QDPAAFgvDSLLLKSSRHYLNIRYTL 668
Cdd:cd06600    233 QEPVLF--PEYYKESVREILELRYKL 256
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
 323-810 4.09e-103

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: 334.49  E-value: 4.09e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKY 402
Cdd:cd06603      1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPYDVIWLDIEHTDGKRYFTWDKKKFPDPKKMQEKLASKGRKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  403 LIIMNPGISKNSNYEPYNNGSLKRVWILGSNG--FaVGEGYPGPTVFPDYTNPVCTEWWtdqvAKFHDHLEFDG------ 474
Cdd:cd06603     81 VTIVDPHIKRDDDYFVYKEAKEKDYFVKDSDGkdF-EGWCWPGSSSWPDFLNPEVRDWW----ASLFSYDKYKGstenly 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  475 VWIEMNEVSSLlqasNNQCESnnlnfppfLPRvldhllfartlcmDTEFHGGL-HYDIHSLYGHSMARTTNLALETI-FM 552
Cdd:cd06603    156 IWNDMNEPSVF----NGPEIT--------MPK-------------DAIHYGGVeHRDVHNIYGLYMHMATFEGLLKRsNG 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  553 NNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLP 632
Cdd:cd06603    211 KKRPFVLTRSFFAGSQRYGAVWTGDNMATWEHLKISIPMLLSLSIAGIPFVGADVGGFFGNPDEELLVRWYQAGAFYPFF 290

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  633 RNHNGPGFRDQDPAAFGVDSllLKSSRHYLNIRYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWDVHEQFLWGPG 712
Cdd:cd06603    291 RAHAHIDTKRREPWLFGEET--TEIIREAIRLRYRLLPYWYTLFYEASRTGLPIMRPLWYEFPEDESTFDIDDQFMLGDS 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  713 LLITPVLYEGVDEVKAYIPDAT-WYDYETGVAISwRKQLVNMLLPGDKIGLHLRGGYIFPTQ-KPNTTTEASRRNSLGLI 790
Cdd:cd06603    369 LLVKPVVEEGATSVTVYLPGGEvWYDYFTGQRVT-GGGTKTVPVPLDSIPVFQRGGSIIPRKeRVRRSSKLMRNDPYTLV 447

                          490       500
                   ....*....|....*....|
gi 1370511246  791 IALDYKREAKGELYWDDGVS 810
Cdd:cd06603    448 VALDENGEAEGELYLDDGES 467
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 203-808 5.87e-96

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 329.93  E-value: 5.87e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  203 AQQYLQLSFrLPSANVYGLGEHVHQQYRHN---MTWKTwpiftrDA-TPTEGMINLYGAHTF-FLCLEDarGSSFGVFLM 277
Cdd:PLN02763    62 DQQIVTFEL-PSGTSFYGTGEVSGPLERTGkrvYTWNT------DAwGYGQNTTSLYQSHPWvFVVLPN--GEALGVLAD 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  278 NSNAMEVTLQ-----------PAPAITyrtiggildFYVFlgNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGIN 346
Cdd:PLN02763   133 TTRRCEIDLRkesiiriiapaSYPVIT---------FGPF--PSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAK 201

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  347 KLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKYLIIMNPGISKNSNYEPYNNGSLKR 426
Cdd:PLN02763   202 RVAEIARTFREKKIPCDVVWMDIDYMDGFRCFTFDKERFPDPKGLADDLHSIGFKAIWMLDPGIKAEEGYFVYDSGCEND 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  427 VWILGSNGFA-VGEGYPGPTVFPDYTNPVCTEWWTDQVAKFHDHlEFDGVWIEMNEVSSLLQASNNQCESNNLNFPPFLP 505
Cdd:PLN02763   282 VWIQTADGKPfVGEVWPGPCVFPDFTNKKTRSWWANLVKDFVSN-GVDGIWNDMNEPAVFKTVTKTMPETNIHRGDEELG 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  506 RVLDHLlfartlcmdtefhgglHYdiHSLYGHSMARTTNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDL 585
Cdd:PLN02763   361 GVQNHS----------------HY--HNVYGMLMARSTYEGMLLANKNKRPFVLTRAGFIGSQRYAATWTGDNLSNWEHL 422

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  586 RWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLPRNHNGPGFRDQDPAAFGVDSLLLksSRHYLNIR 665
Cdd:PLN02763   423 HMSIPMVLQLGLSGQPLSGPDIGGFAGDATPKLFGRWMGVGAMFPFARGHSEQGTIDHEPWSFGEECEEV--CRLALKRR 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  666 YTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWDVHEQFLWGPGLLITPVLY-EGVDEVKAYIPDATW--YDYETGv 742
Cdd:PLN02763   501 YRLLPHFYTLFYKAHTTGLPVMTPIFFADPKDPSLRKVENSFLLGPLLISASTLPdQGSDNLQHVLPKGIWqrFDFDDS- 579

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511246  743 aiswrkqlvNMLLPgdkiGLHLRGGYIFPTQKP-NTTTEASRRNSLGLIIALDYKREAKGELYWDDG 808
Cdd:PLN02763   580 ---------HPDLP----LLYLQGGSIIPLGPPiQHVGEASLSDDLTLLIALDENGKAEGVLYEDDG 633
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
214-810 2.67e-87

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 295.92  E-value: 2.67e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  214 PSANVYGLGEH---VHQQYRHNMTWktwpifTRDATPTEGMINLYGAHTFFLCLEDargssFGVFLmNSNAM---EVTLQ 287
Cdd:COG1501     60 LGEQIYGLGERfttLHKRGRIVVNW------NLDHGGHKDNGNTYAPIPFYVSSKG-----YGVFV-NSASYvtfDVGSA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  288 PAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYS 367
Cdd:COG1501    128 YSDLVEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPLDVIHL 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  368 DIDYMD--GKKDFTVDEVAYSGLPDFVKELHDNGQKYLIIMNPGISKNSnyEPYNNGSLKRVWIlGSNGFAVGEGYPGPT 445
Cdd:COG1501    208 DIRWMDkyYWGDFEWDPRRFPDPKAMVKELHDRGVKLVLWINPYVAPDS--AIFAEGMANFVKI-ASGTVFVGKMWPGTT 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  446 VFPDYTNPVCTEWWTDQVAKFHDHLEFDGVWIEMNEVssllqasnnqcesnnlnfppfLPRVLdhllfartlcmdTEFHG 525
Cdd:COG1501    285 GLLDFTRPDAREWFWAGLEKELLSIGVDGIKLDMNEG---------------------WPTDV------------ATFPS 331

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  526 GLHYDIHSLYGHSMARTTNLALETIFmNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGA 605
Cdd:COG1501    332 NVPQQMRNLYGLLEAKATFEGFRTSR-NNRTFILTRSGFAGGQRYPVIWTGDNTSSWESLEDQLTQGLNLSLSGVPFWTP 410

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  606 NICGYNNNVTEELCRRWMQLGAFYPLPRNHNgpGFRDQDPAAFGVDSllLKSSRHYLNIRYTLLPYLYTLFYHAHTRGET 685
Cdd:COG1501    411 DIGGFFGSPSRELWIRWFQVGAFSPFARIHG--WASSTEPWFFDEEA--KQIVKEYAQLRYRLLPYIYSLFAKASTDGTP 486

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  686 VARPLVHEFYQDSATWDVHEQFLWGPGLLITPVLyEGVDEVKAYIPDATWYDYETGVAISwRKQLVNMLLPGDKIGLHLR 765
Cdd:COG1501    487 VIRPLFLEFPDDPTTRFIDDQYMFGEYLLVAPIF-AGTESRLVYLPKGKWYDFWTGELIE-GGQWITVTAPLDRLPLYVR 564

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1370511246  766 GGYIFPTQKPNTTTEASRRNSLGLIIALDykREAKGELYWDDGVS 810
Cdd:COG1501    565 DGSIIPLGPVSLRPSMQKIDGIELRVYGS--GETAYTLYDDDGET 607
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
 323-662 2.37e-59

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: 204.89  E-value: 2.37e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMD---GKKDFTVDEVAYSGLPDFVKELHDNG 399
Cdd:cd06589      1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPLDGFVLDSDWMDwggNWGGFTWNREKFPDPKGMIDELHDKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  400 QKYLIIMNPGIsknsnyepynngslkrvwilgsngfavgegypgptvfpdytnpvcTEWWTDQVAKFHDHLEFDGVWIEM 479
Cdd:cd06589     81 VKLGLIVKPRL---------------------------------------------RDWWWENIKKLLLEQGVDGWWTDM 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  480 NEvssllqasnnqcesnnlnfppflPRVLDHLLFArtlcmdtefHGGLHYDIHSLYGHSMARTTNLALETIFMNNRSFIL 559
Cdd:cd06589    116 GE-----------------------PLPFDDATFH---------NGGKAQKIHNAYPLNMAEATYEGQKKTFPNKRPFIL 163

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  560 SRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYN-NNVTEELCRRWMQLGAFYPLPRNHNGP 638
Cdd:cd06589    164 SRSGYAGAQRYPAIWSGDNTTTWDSLAFQIRAGLSASLSGVGYWGHDIGGFTgGDPDKELYTRWVQFGAFSPIFRLHGDN 243

                          330       340
                   ....*....|....*....|....
gi 1370511246  639 GFRDQDPAAFgvDSLLLKSSRHYL 662
Cdd:cd06589    244 SPRDKEPWVY--GEEALAIFRKYL 265
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 104-215 1.12e-47

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: 165.73  E-value: 1.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  104 GFTAQLKRLPSP-SLFGNDVATTLFTAEYQTSNRFHFKITDFNNIRYEVSHENINLVDGIADASNLSYYVEVTDKPFSIK 182
Cdd:pfam16863    1 GLTADLTLAGSPcNLYGNDIETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFK 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1370511246  183 IMRTSNRRVLLDTSIGPLQFAQQYLQLSFRLPS 215
Cdd:pfam16863   81 VTRKSTGEVLFDTSGGPLVFEDQFLQLSTRLPS 113
GH31_lyase_GLase cd06601
alpha-1,4-glucan lyase; GLases (alpha-1,4-glucan lyases) are glycosyl hydrolase family 31 ...
 323-677 9.04e-39

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: 148.33  E-value: 9.04e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKY 402
Cdd:cd06601      1 GRSRMKPRYVFGYHQGCYGYSSRESLEVVVQSYRDANIPLDGLHIDVDFQDNYRTFTTSKDKFPNPKEMFSNLHAQGFKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  403 LIIMNPGISknsnyEPYnngslkrvwiLGSNGFAVGEGYPGptVFPDYTNPVCTEWWTDQVAKFHD-HLEFdgVWIEMNE 481
Cdd:cd06601     81 STNITPIIT-----DPY----------IGGVNYGGGLGSPG--FYPDLGRPEVREWWGQQYKYLFDmGLEM--VWQDMTT 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  482 VSSLLQASNNQCESNNL------------NFPPFLPRVLDHLLFARTLCMDTeFHGGLHydihslyghsmarttnlalET 549
Cdd:cd06601    142 PAIAPHKINGYGDMKTFplrllvtddsvkNEHTYKPAATLWNLYAYNLHKAT-YHGLNR-------------------LN 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  550 IFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNN--------VTEELCRR 621
Cdd:cd06601    202 ARPNRRNFIIGRGGYAGAQRFAGLWTGDNASTWDFLQINIPQVLNLGLSGVPISGSDIGGFASGsdenegkwCDPELLIR 281

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  622 WMQLGAFYPLPRNH----NGPGFRDQDPAAFGVDSLLLKSSRHYLNIRYTLLPYLYTLFY 677
Cdd:cd06601    282 WVQAGAFLPWFRNHydryIKKKQQEKLYEPYYYYEPVLPICRKYVELRYRLMQVFYDAMY 341
NtCtMGAM_N pfam16863
N-terminal barrel of NtMGAM and CtMGAM, maltase-glucoamylase; NtCtMGAM_N is a beta-barrel-like ...
 991-1084 2.96e-34

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: 127.21  E-value: 2.96e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  991 ISFLHLKVIYHTATMLQVKIYDPTNKRYEVPVPLNTPPQPVGDPENRLYDVRIQNNPFGIQIQRKNSSTVIWDSQLPGFI 1070
Cdd:pfam16863   20 IETLKLTVEYQTDNRLHVKITDPNNKRYEVPEELLPRPSPSSSASDSLYEFEYTNEPFGFKVTRKSTGEVLFDTSGGPLV 99

                           90
                   ....*....|....
gi 1370511246 1071 FNDMFLSISTRLPS 1084
Cdd:pfam16863  100 FEDQFLQLSTRLPS 113
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
 323-677 4.52e-33

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: 131.27  E-value: 4.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIP-----YDVQ-YSDIDYMDGKK--DFTVDEVAYSGLPDFVKE 394
Cdd:cd06598      1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFPldgvvLDLYwFGGIIASPDGPmgDLDWDRKAFPDPAKMIAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  395 LHDNGQKYLIIMNPGISKNSN--YEPYNNGSLKRVwILGSNGFAVGEGYPGPTVFPDYTNPVCTEWWTDQVaKFHDHLEF 472
Cdd:cd06598     81 LKQQGVGTILIEEPYVLKNSDeyDELVKKGLLAKD-KAGKPEPTLFNFWFGEGGMIDWSDPEARAWWHDRY-KDLIDMGV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  473 DGVWIEMNEvssllqasnnqcesnnlnfPPFLPRvldhllfartlcmDTEFHGGLHYDIHSLYGHSMARTTNLALETIFM 552
Cdd:cd06598    159 AGWWTDLGE-------------------PEMHPP-------------DMVHADGDAADVHNIYNLLWAKSIYDGYQRNFP 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  553 NNRSFILSRSTFAGSGKF-AAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVT--EELCRRWMQLGAFY 629
Cdd:cd06598    207 EQRPFIMSRSGTAGSQRYgVIPWSGDIGRTWGGLASQINLQLHMSLSGIDYYGSDIGGFARGETldPELYTRWFQYGAFD 286

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1370511246  630 PLPRNHNGPGFRDQdPAAFGVDSllLKSSRHYLNIRYTLLPYLYTLFY 677
Cdd:cd06598    287 PPVRPHGQNLCNPE-TAPDREGT--KAINRENIKLRYQLLPYYYSLAY 331
PRK10426 PRK10426
alpha-glucosidase; Provisional
 214-735 1.54e-29

alpha-glucosidase; Provisional


Pssm-ID: 236691 [Multi-domain]  Cd Length: 635  Bit Score: 125.88  E-value: 1.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  214 PSANVYGLGEhvhqQYRH-NMTWKTWPIFT------RDATP--TEGMInlygahtfflCLEDARGS---------SF--- 272
Cdd:PRK10426    80 PDEHIYGCGE----QFSYfDLRGKPFPLWTseqgvgRNKQTyvTWQAD----------CKENAGGDyywtyfpqpTFvss 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  273 ---GVFLMNSNAMEVTLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELVGRPFFPPYWS-----LGFQlsrrdyGG 344
Cdd:PRK10426   146 qkyYCHVDNSAYMNFDFSAPEYHELELWEDKATLRFECADTYISLLEKLTALFGRQPELPDWAydgvtLGIQ------GG 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  345 INKLKEVVSRNRLAEIPYD---VQ-YSDIDYMD-GKK---DFTVDEVAYSGLPDFVKELHDNGQKYLIIMNPGISKNSNY 416
Cdd:PRK10426   220 TEVVQKKLDTMRNAGVKVNgiwAQdWSGIRMTSfGKRlmwNWKWDSERYPQLDSRIKQLNEEGIQFLGYINPYLASDGDL 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  417 epYNNGSLKRVWILGSNG--FAV--GEGYPGptvFPDYTNPVCTEWWTDQVAKFHDHLEFDGvWIEmnevssllqasnnq 492
Cdd:PRK10426   300 --CEEAAEKGYLAKDADGgdYLVefGEFYAG---VVDLTNPEAYEWFKEVIKKNMIGLGCSG-WMA-------------- 359

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  493 cesnnlNFPPFLPrvldhllfartlcMDTEFHGGLHYDI-HSLYGHSMARTTNLALETIFMNNRSFILSRSTFAGSGKFA 571
Cdd:PRK10426   360 ------DFGEYLP-------------TDAYLHNGVSAEImHNAWPALWAKCNYEALEETGKLGEILFFMRAGYTGSQKYS 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  572 -AHWLGDNAATW---DDLRWSIPTILEFNLFGIPMVGANICGY----NNNVTEELCRRWMQLGAFYPLPRNHNG--Pgfr 641
Cdd:PRK10426   421 tLFWAGDQNVDWsldDGLASVVPAALSLGMSGHGLHHSDIGGYttlfGMKRTKELLLRWCEFSAFTPVMRTHEGnrP--- 497

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  642 DQDPAAFGVDSLLLKSSRhYLNIRYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWDVHEQFLWGPGLLITPVLYE 721
Cdd:PRK10426   498 GDNWQFDSDAETIAHFAR-MTRVFTTLKPYLKELVAEAAKTGLPVMRPLFLHYEDDAATYTLKYQYLLGRDLLVAPVHEE 576

                          570
                   ....*....|....
gi 1370511246  722 GVDEVKAYIPDATW 735
Cdd:PRK10426   577 GRTDWTVYLPEDKW 590
GH31_CPE1046 cd06596
Clostridium CPE1046-like; CPE1046 is an uncharacterized Clostridium perfringens protein with a ...
 535-741 1.61e-29

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: 120.91  E-value: 1.61e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  535 YGHSMARTTNLALETIFMNN---RSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICG-Y 610
Cdd:cd06596    122 AGYSFALNGVEDAADGIENNsnaRPFIWTVDGWAGTQRYAVIWTGDQSGSWEYIRFHIPTYIGSGLSGQAYATSDVDGiF 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  611 NNNvtEELCRRWMQLGAFYPLPRNHNGPGFRDQDPAAFGVDSLLLksSRHYLNIRYTLLPYLYTLFYHAHTRGETVARPL 690
Cdd:cd06596    202 GGS--PETYTRDLQWKAFTPVLMNMSGWAANDKQPWVFGEPYTSI--NRKYLKLKMRLMPYIYTYAREASVTGLPMVRAM 277

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370511246  691 VHEFYQDSATW--DVHEQFLWGPGLLITPVlYEGVDEVKA-----YIPDATWYDYETG 741
Cdd:cd06596    278 FLEYPNDPTAYgtATQYQFMWGPDFLVAPV-YQNTAAGNDvrngiYLPAGTWIDYWTG 334
GH31_xylosidase_YicI cd06593
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
 323-668 5.05e-28

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: 115.74  E-value: 5.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYMDGKK--DFTVDEVAYSGLPDFVKELHDNGQ 400
Cdd:cd06593      1 GRPPLPPAWSFGLWLSRSFYYSEEEVLEVADGMRERGIPCDVIHLDCFWMKEDWwcDFEWDEERFPDPEGMIARLKEKGF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  401 KYLIIMNPGISKNSnyEPYNNGSLKRVWILGSNG--FAVGEGYPGPTVFPDYTNPVCTEWWTDQVAKFHDhlefDGVwie 478
Cdd:cd06593     81 KVCLWINPYISQDS--PLFKEAAEKGYLVKNPDGspWHQWDGWQPGMGIIDFTNPEAVAWYKEKLKRLLD----MGV--- 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  479 mnevssllqasnnqcesnnlnfppflpRVL--DhllFARTLCMDTEFHGGLHYD-IHSLYGHSMARTTNLALETIFmNNR 555
Cdd:cd06593    152 ---------------------------DVIktD---FGERIPEDAVYYDGSDGRkMHNLYPLLYNKAVYEATKEVK-GEE 200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  556 SFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLPRNH 635
Cdd:cd06593    201 AVLWARSAWAGSQRYPVHWGGDSESTFEGMAASLRGGLSLGLSGFGFWSHDIGGFEGTPSPELYKRWTQFGLLSSHSRLH 280

                          330       340       350
                   ....*....|....*....|....*....|...
gi 1370511246  636 nGPGFRdqDPAAFGVDSllLKSSRHYLNIRYTL 668
Cdd:cd06593    281 -GSTPR--EPWEYGEEA--LDVVRKFAKLRYRL 308
GH31_NET37 cd06592
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
 328-735 1.60e-27

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: 115.78  E-value: 1.60e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  328 PPYWSLGFQLsRRDYGG--INKLKEVVSRNRlaeIPYDVQYSDIDYMDGKKDFTVDEVAYSGLPDFVKELHDNGQKYLII 405
Cdd:cd06592      2 PPIWSTWAEY-KYNINQekVLEYAEEIRANG---FPPSVIEIDDGWQTYYGDFEFDPEKFPDPKGMIDKLHEMGFRVTLW 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  406 MNPGISKNSnyEPYNNGSLKRVWILGSNGFAVGEGY--PGPTVFPDYTNPVCTEWWTDQVAKFHDHLEFDGVWIEMNEVS 483
Cdd:cd06592     78 VHPFINPDS--PNFRELRDKGYLVKEDSGGPPLIVKwwNGYGAVLDFTNPEARDWFKERLRELQEDYGIDGFKFDAGEAS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  484 sllqasnnqcesnnlnfppFLPRvldhllfartlcMDTEFHGGLH-YDIHSLYGHSMARTTNLA-LETIFMNNRSFILSR 561
Cdd:cd06592    156 -------------------YLPA------------DPATFPSGLNpNEYTTLYAELAAEFGLLNeVRSGWKSQGLPLFVR 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  562 STFAGSgkfaaHWlgdnaATWDDLRWSIPTILEFNLFGIP-----MVGANicGYNNNVTE-ELCRRWMQLGAFYPLPRNH 635
Cdd:cd06592    205 MSDKDS-----HW-----GYWNGLRSLIPTALTQGLLGYPfvlpdMIGGN--AYGNFPPDkELYIRWLQLSAFMPAMQFS 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  636 NGP-GFRDQDpaafgvdslLLKSSRHYLNIRYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWDVHEQFLWGPGLL 714
Cdd:cd06592    273 VAPwRNYDEE---------VVDIARKLAKLREKLLPYIYELAAEAVDTGEPIIRPLWWIAPEDEEALTIDDQFLLGDDIL 343

                          410       420
                   ....*....|....*....|.
gi 1370511246  715 ITPVLYEGVDEVKAYIPDATW 735
Cdd:cd06592    344 VAPVLEKGARSRDVYLPKGRW 364
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 207-323 7.54e-25

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: 100.72  E-value: 7.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  207 LQLSFRLP-SANVYGLGEHVHqqyRHNMTWKTWPIFTRDA-TPTEGMINLYGAHTFFLCLEdargsSFGVFLMNSNAMEV 284
Cdd:cd14752     10 LRLSFKLPpDEHFYGLGERFG---GLNKRGKRYRLWNTDQgGYRGSTDPLYGSIPFYLSSK-----GYGVFLDNPSRTEF 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1370511246  285 TLQPA--PAITYRTIGGILDFYVFLGNTPEQVVQEYLELVG 323
Cdd:cd14752     82 DFGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
GH31_glycosidase_Aec37 cd06599
E.coli Aec37-like; Glycosyl hydrolase family 31 (GH31) domain of a bacterial protein family ...
 323-630 2.49e-24

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: 105.37  E-value: 2.49e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYG----GINKLKEVVSRNRLAEIPYDV-----QYSDIDymDGKKD-FTVDEVAYSGLPDFV 392
Cdd:cd06599      1 GRPALPPRWSLGYLGSTMYYTeapdAQEQILDFIDTCREHDIPCDGfhlssGYTSIE--DGKRYvFNWNKDKFPDPKAFF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  393 KELHDNGqkYLIIMN--PGISKNSNYepYNNGSLKRVWILGSNG-------FAVGEGYpgptvFPDYTNPVCTEWWTDQV 463
Cdd:cd06599     79 RKFHERG--IRLVANikPGLLTDHPH--YDELAEKGAFIKDDDGgepavgrFWGGGGS-----YLDFTNPEGREWWKEGL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  464 AkfHDHLEF--DGVWiemNEvssllqasNNQCESNNLNfppflprvldhllfartLCMDTEFHGGLHYDIHSLYGHSMAR 541
Cdd:cd06599    150 K--EQLLDYgiDSVW---ND--------NNEYEIWDDD-----------------AACCGFGKGGPISELRPIQPLLMAR 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  542 TTNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANICG-YNNNVTEELCR 620
Cdd:cd06599    200 ASREAQLEHAPNKRPFVISRSGCAGIQRYAQTWSGDNRTSWKTLKYNIAMGLGMSLSGVANYGHDIGGfAGPAPEPELFV 279

                          330
                   ....*....|
gi 1370511246  621 RWMQLGAFYP 630
Cdd:cd06599    280 RWVQNGIFQP 289
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
 298-749 6.89e-24

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 108.45  E-value: 6.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  298 GGILDFYVFLGNTPEQVVQEYLELVGRPFFPPYWSLGFQLSRR---DY------GGINKLKEvvsRNrlaeIPYDVQYSD 368
Cdd:PRK10658   233 GEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWLTTSfttNYdeatvnSFIDGMAE---RD----LPLHVFHFD 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  369 IDYMDGKK--DFTVDEVAYsglPD---FVKELHDNGQKYLIIMNPGISKNSNY--EPYNNGSL-KR----VWI--LGSNG 434
Cdd:PRK10658   306 CFWMKEFQwcDFEWDPRTF---PDpegMLKRLKAKGLKICVWINPYIAQKSPLfkEGKEKGYLlKRpdgsVWQwdKWQPG 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  435 FAVgegypgptVfpDYTNPVCTEWwtdqvakFHDHLEfdgvwiemnevssllqasnnqcesnnlnfppflpRVLDHLL-- 512
Cdd:PRK10658   383 MAI--------V--DFTNPDACKW-------YADKLK----------------------------------GLLDMGVdc 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  513 ----FARTLCMDTEFHGGLH-YDIHSLYGHSMARTTNLALETIFMNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRW 587
Cdd:PRK10658   412 fktdFGERIPTDVVWFDGSDpQKMHNYYTYLYNKTVFDVLKETRGEGEAVLFARSATVGGQQFPVHWGGDCYSNYESMAE 491

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  588 SIPTILEFNLFGIPMVGANICGYNNNVTEELCRRWMQLGAFYPLPRNHNGPGFRDqdPAAFG---VDSLllkssRHYLNI 664
Cdd:PRK10658   492 SLRGGLSLGLSGFGFWSHDIGGFENTATADVYKRWCAFGLLSSHSRLHGSKSYRV--PWAYDeeaVDVV-----RFFTKL 564

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  665 RYTLLPYLYTLFYHAHTRGETVARPLVHEFYQDSATWDVHEQFLWGPGLLITPVLYEgVDEVKAYIPDATWYDYETGVAI 744
Cdd:PRK10658   565 KCRLMPYLYREAAEAHERGTPMMRAMVLEFPDDPACDYLDRQYMLGDSLLVAPVFSE-AGDVEYYLPEGRWTHLLTGEEV 643


                   ....*...
gi 1370511246  745 ---SWRKQ 749
Cdd:PRK10658   644 eggRWHKE 651
GH31_N cd14752
N-terminal domain of glycosyl hydrolase family 31 (GH31); This family is found N-terminal to ...
 1076-1190 3.59e-23

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: 95.72  E-value: 3.59e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1076 LSISTRLP-SQYIYGFGEteHTTfRRNMNWNTWGMFAHD--EPPAYKKNSYGVHPYYMALEedgsAHGVLLLNSNAMDVT 1152
Cdd:cd14752     10 LRLSFKLPpDEHFYGLGE--RFG-GLNKRGKRYRLWNTDqgGYRGSTDPLYGSIPFYLSSK----GYGVFLDNPSRTEFD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1153 LQPT--PALTYRTTGGILDFYIVLGPTPELVTQQYTELIG 1190
Cdd:cd14752     83 FGSEdsDELTFSSEGGDLDYYFFAGPTPKEVIEQYTELTG 122
GH31_xylosidase_XylS cd06591
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
 323-635 4.88e-23

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: 101.48  E-value: 4.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDVQYSDIDYM--DGKKDFTVDEVAYsglPD---FVKELHD 397
Cdd:cd06591      1 GKAPMLPKWALGFWQSKERYKTQEELLEVAREYRERGIPLDVIVQDWFYWteQGWGDMKFDPERF---PDpkgMVDELHK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  398 NGQKYLIIMNPGISKNS-NYEPYnngsLKRVWILGSNGFAVGegYPGPTVFPDYTNPVCTEWWTDQVAKFHDHLEFDGVW 476
Cdd:cd06591     78 MNVKLMISVWPTFGPGSeNYKEL----DEKGLLLRTNRGNGG--FGGGTAFYDATNPEAREIYWKQLKDNYFDKGIDAWW 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  477 IEmnevssllqasnnQCEsnnlnfppflPRVLDHLLFARtlcmDTEFHGGLHYDIHSLYGHSMARTTNLALETIFMNNRS 556
Cdd:cd06591    152 LD-------------ATE----------PELDPYDFDNY----DGRTALGPGAEVGNAYPLMHAKGIYEGQRATGPDKRV 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  557 FILSRSTFAGSGKF-AAHWLGDNAATWDDLRWSIPTILEFNLFGIP---------MVGANICGYNNNVTEELCRRWMQLG 626
Cdd:cd06591    205 VILTRSAFAGQQRYgAAVWSGDISSSWETLRRQIPAGLNFGASGIPywttdiggfFGGDPEPGEDDPAYRELYVRWFQFG 284


                   ....*....
gi 1370511246  627 AFYPLPRNH 635
Cdd:cd06591    285 AFCPIFRSH 293
Glyco_hydro_31 pfam01055
Glycosyl hydrolases family 31; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. ...
 1171-1229 9.46e-21

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: 96.86  E-value: 9.46e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511246 1171 YIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:pfam01055    1 YFFLGPTPKDVVKQYTELTGRPPLPPYWALGYHQSRWGYKSEEEVLEVVDGFRERDIPL 59
YicI COG1501
Alpha-glucosidase/xylosidase, GH31 family [Carbohydrate transport and metabolism];
1083-1229 1.57e-18

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


Pssm-ID: 441110 [Multi-domain]  Cd Length: 609  Bit Score: 90.99  E-value: 1.57e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1083 PSQYIYGFGE---TEHTTFRRNMNWNTWGMFAHDEPPAYKknsygVHPYYMALEEDGsahgvLLLNSNAM---DVTLQPT 1156
Cdd:COG1501     60 LGEQIYGLGErftTLHKRGRIVVNWNLDHGGHKDNGNTYA-----PIPFYVSSKGYG-----VFVNSASYvtfDVGSAYS 129

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511246 1157 PALTYRTTGGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:COG1501    130 DLVEFTVPGDSLEFYVIEGPSPEDVLEKYTELTGKPPLPPRWAFGYWQSRKSYYDQDQVLAFADEFRDRGFPL 202
GH31_transferase_CtsY cd06597
CtsY (cyclic tetrasaccharide-synthesizing enzyme Y)-like; CtsY is a bacterial ...
 323-666 1.78e-18

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: 88.14  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  323 GRPFFPPYWSLGFQLSRRDYGGINKLKEVVSRNRLAEIPYDV----QYSD------IDYMDGKkdftvdevaYSGLPDFV 392
Cdd:cd06597      1 GRAALPPKWAFGHWVSANEWNSQAEVLELVEEYLAYDIPVGAvvieAWSDeatfyiFNDATGK---------WPDPKGMI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  393 KELHDNGQKYLIIMNPGISKNSNYEP-----YNNGSlkrvwilgSNGFAVGEGYPGPTV----------FPDYTNPVCTE 457
Cdd:cd06597     72 DSLHEQGIKVILWQTPVVKTDGTDHAqksndYAEAI--------AKGYYVKNGDGTPYIpegwwfgggsLIDFTNPEAVA 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  458 WWTDQVAKFHDHLEFDG--------VWIEmnevssllqasnnqcesnnlnfppflprvldhllfartlcmDTEFHGGLHY 529
Cdd:cd06597    144 WWHDQRDYLLDELGIDGfktdggepYWGE-----------------------------------------DLIFSDGKKG 182

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  530 DI-HSLYGHSMARTTNLALETIfmNNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWSIPTILEFNLFGIPMVGANIC 608
Cdd:cd06597    183 REmRNEYPNLYYKAYFDYIREI--GNDGVLFSRAGDSGAQRYPIGWVGDQDSTFEGLQSALKAGLSAAWSGYPFWGWDIG 260

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511246  609 GYNNNV-TEELCRRWMQLGAFYPLPRNH---NGPGFRDQDP---AAFGVDSLLLKSSRHYLNIRY 666
Cdd:cd06597    261 GFSGPLpTAELYLRWTQLAAFSPIMQNHsekNHRPWSEERRwnvAERTGDPEVLDIYRKYVKLRM 325
GH31_MGAM_SI_GAA cd06602
maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase; This subgroup ...
 1190-1229 2.75e-13

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: 72.93  E-value: 2.75e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:cd06602      1 GRPAMPPYWSLGFHLCRWGYKNLDELKEVVERYRAAGIPL 40
Trefoil pfam00088
Trefoil (P-type) domain;
43-87 7.04e-12

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 61.18  E-value: 7.04e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1370511246   43 CPEIPQSERIDCTPdQEVTEDICRWQyKCCWSPVADANVPRCFFP 87
Cdd:pfam00088    1 CSSVPPSDRFDCGY-PGITQEECEAR-GCCWDPSVDPGVPWCFYP 43
GH31_glucosidase_YihQ cd06594
alpha-glucosidase YihQ-like; YihQ is a bacterial alpha-glucosidase with a conserved glycosyl ...
 380-637 2.31e-11

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: 66.45  E-value: 2.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  380 VDEVAYSGLPDFVKELHDNGQKYLIIMNPGISknsnyepyNNGSLKRVWILGSNGFAV----GEGY-----PGPTVFPDY 450
Cdd:cd06594     65 WDEELYPGWDELVKELKEQGIRVLGYINPFLA--------NVGPLYSYKEAEEKGYLVknktGEPYlvdfgEFDAGLVDL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  451 TNPVCTEWWTDQVAKFHDHLEFDGvWieMNEvssllqasnnqcesnnlnFPPFLPrvldhllfartlcMDTEFHGG-LHY 529
Cdd:cd06594    137 TNPEARRWFKEVIKENMIDFGLSG-W--MAD------------------FGEYLP-------------FDAVLHSGeDAA 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  530 DIHSLYGHSMARTTNLALETIFMNNRSFILSRSTFAGSGKFAA-HWLGDNAATW---DDLRWSIPTILEFNLFGIPMVGA 605
Cdd:cd06594    183 LYHNRYPELWARLNREAVEEAGKEGEIVFFMRSGYTGSPRYSTlFWAGDQNVDWsrdDGLKSVIPGALSSGLSGFSLTHS 262

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1370511246  606 NICGY--------NNNVTEELCRRWMQLGAFYPLPRNHNG 637
Cdd:cd06594    263 DIGGYttlfnplvGYKRSKELLMRWAEMAAFTPVMRTHEG 302
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 908-948 2.27e-10

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


Pssm-ID: 197472  Cd Length: 46  Bit Score: 57.01  E-value: 2.27e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370511246   908 VSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 948
Cdd:smart00018    5 VPPSERINCGPPGITEAE--CEARGCCF-DSSISGVPWCFY 42
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 907-948 7.73e-10

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: 55.43  E-value: 7.73e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370511246  907 PVSDLEKFNCYPDDPTASEesCRQRGCLWeDTSTPGVPTCYY 948
Cdd:cd00111      4 SVPPSERIDCGPPGITQEE--CEARGCCF-DPSISGVPWCFY 42
GH31_u1 cd06595
glycosyl hydrolase family 31 (GH31); uncharacterized subgroup; This family represents an ...
 553-672 8.72e-10

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: 61.45  E-value: 8.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246  553 NNRSFILSRSTFAGSGKFAAHWLGDNAATWDDLRWsIP--TILEFNLfGIPMVGANICGYNNNVTE-ELCRRWMQLGAFY 629
Cdd:cd06595    185 KRRPLILSRWGGLGSHRYPIGFSGDTEVSWETLAF-QPyfTATAANV-GYSWWSHDIGGHKGGIEDpELYLRWVQFGVFS 262

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1370511246  630 PLPRNH--NGPgFRDQDPAAFGVDSllLKSSRHYLNIRYTLLPYL 672
Cdd:cd06595    263 PILRLHsdKGP-YYKREPWLWDAKT--FEIAKDYLRLRHRLIPYL 304
Trefoil pfam00088
Trefoil (P-type) domain;
908-948 1.32e-09

Trefoil (P-type) domain;


Pssm-ID: 459666  Cd Length: 43  Bit Score: 54.63  E-value: 1.32e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1370511246  908 VSDLEKFNCYPddPTASEESCRQRGCLWEDTSTPGVPTCYY 948
Cdd:pfam00088    4 VPPSDRFDCGY--PGITQEECEARGCCWDPSVDPGVPWCFY 42
GH31_MGAM-like cd06600
maltase-glucoamylase (MGAM)-like; This family includes the following closely related glycosyl ...
 1190-1229 5.59e-09

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: 58.27  E-value: 5.59e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:cd06600      1 GRPALPPYWAFGYHQSRYSYYDQDKVVEVVDIMQEAGIPY 40
PLN02763 PLN02763
hydrolase, hydrolyzing O-glycosyl compounds
 1088-1228 2.60e-08

hydrolase, hydrolyzing O-glycosyl compounds


Pssm-ID: 215408 [Multi-domain]  Cd Length: 978  Bit Score: 58.36  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511246 1088 YGFGETE---HTTFRRNMNWNT--WGmfahdeppaYKKNS---YGVHPYYMALEEDGSAHGVLLLNSNAMDVTLQPTPAL 1159
Cdd:PLN02763    77 YGTGEVSgplERTGKRVYTWNTdaWG---------YGQNTtslYQSHPWVFVVLPNGEALGVLADTTRRCEIDLRKESII 147

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370511246 1160 TYRTTGgildFY--IVLGP--TPELVTQQYTELIGRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIP 1228
Cdd:PLN02763   148 RIIAPA----SYpvITFGPfpSPEALLTSLSHAIGTVFMPPKWALGYQQCRWSYESAKRVAEIARTFREKKIP 216
GH31 cd06589
glycosyl hydrolase family 31 (GH31); GH31 enzymes occur in prokaryotes, eukaryotes, and ...
 1190-1229 4.25e-08

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: 55.82  E-value: 4.25e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:cd06589      1 GRPPLLPKWALGFWNSRYGYYSEDEVEELVDRYREEGIPL 40
PD smart00018
P or trefoil or TFF domain; Proposed role in renewal and pathology of mucous epithelia.
 42-89 8.50e-07

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


Pssm-ID: 197472  Cd Length: 46  Bit Score: 46.61  E-value: 8.50e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1370511246    42 ECpEIPQSERIDCTPDqEVTEDICRwQYKCCWSPvADANVPRCFFPWN 89
Cdd:smart00018    2 QC-SVPPSERINCGPP-GITEAECE-ARGCCFDS-SISGVPWCFYPNT 45
Trefoil cd00111
P or trefoil or TFF domain; Trefoil factor family domain peptides are mucin-associated ...
 42-88 2.73e-06

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: 45.41  E-value: 2.73e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1370511246   42 ECPeIPQSERIDCTPdQEVTEDICRwQYKCCWSPvADANVPRCFFPW 88
Cdd:cd00111      2 WCS-VPPSERIDCGP-PGITQEECE-ARGCCFDP-SISGVPWCFYPK 44
GH31_glucosidase_II_MalA cd06604
Alpha-glucosidase II-like; Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a ...
 1190-1228 5.34e-06

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: 50.20  E-value: 5.34e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIP 1228
Cdd:cd06604      1 GRPPLPPKWALGYQQSRWSYYPEEEVREVAKGFRERDIP 39
PRK10658 PRK10658
putative alpha-glucosidase; Provisional
 1165-1228 5.36e-05

putative alpha-glucosidase; Provisional


Pssm-ID: 236731 [Multi-domain]  Cd Length: 665  Bit Score: 47.58  E-value: 5.36e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370511246 1165 GGILDFYIVLGPTPELVTQQYTELIGRPAMIPYWALGFHLS-----RYgyqNDAEISSLYDAMVAAQIP 1228
Cdd:PRK10658   233 GEYLEYFVIDGPTPKEVLDRYTALTGRPALPPAWSFGLWLTtsfttNY---DEATVNSFIDGMAERDLP 298
GH31_GANC_GANAB_alpha cd06603
neutral alpha-glucosidase C, neutral alpha-glucosidase AB; This subgroup includes the closely ...
 1190-1229 1.86e-04

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: 45.59  E-value: 1.86e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIPY 1229
Cdd:cd06603      1 GTPPLPPLFALGYHQCRWNYNDQEDVLEVDANFDEHDIPY 40
GH31_transferase_CtsZ cd06598
CtsZ (cyclic tetrasaccharide-synthesizing enzyme Z)-like; CtsZ is a bacterial ...
 1190-1228 5.31e-04

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: 43.83  E-value: 5.31e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1370511246 1190 GRPAMIPYWALGFHLSRYGYQNDAEISSLYDAMVAAQIP 1228
Cdd:cd06598      1 GRPPLPPKWAFGLWQSEFGYDNWAEVDELVDTLRQKDFP 39
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
 217-284 6.49e-04

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: 39.37  E-value: 6.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370511246  217 NVYGLGEHV------HQQYRhnmtwktwpIFTRDA-TPTEGMINLYGAHTFFLCLEDarGSSFGVFLMNSNAMEV 284
Cdd:pfam13802    3 HVYGLGERAgplnkrGTRYR---------LWNTDAfGYELDTDPLYKSIPFYISHNG--GRGYGVFWDNPAETWF 66
Gal_mutarotas_2 pfam13802
Galactose mutarotase-like; This family is found N-terminal to glycosyl-hydrolase domains, and ...
 1086-1146 3.56e-03

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: 37.06  E-value: 3.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370511246 1086 YIYGFGetEHTT-FRRNM----NWNTWGMfahdEPPAYKKNSYGVHPYYMALeEDGSAHGVLLLNS 1146
Cdd:pfam13802    3 HVYGLG--ERAGpLNKRGtryrLWNTDAF----GYELDTDPLYKSIPFYISH-NGGRGYGVFWDNP 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH