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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna20103.1-v1.0-hybrid |
Family | GH31 |
Protein Properties | Length: 1727 Molecular Weight: 192614 Isoelectric Point: 5.049 |
Chromosome | Chromosome/Scaffold: 3 Start: 8119624 End: 8127842 |
Description | Glycosyl hydrolases family 31 protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH31 | 273 | 739 | 0 |
YFFAGPTPESVMDQYTELIGRPAPMPYWSFGFHQCKYGYKNVSDLEGVVAGYANASIPLDVMWTDIDYMDAYKDFTLDPVNFPLDKMQNFTNTLHQNGQK YVVILDPGISINDSYGSYTRGKEADIYIKRDGIPYQGNVWPGDVYFPDFVHPQSEPYWENEIKLFIDQLPVDGLWIDMNEVSNFQTSAPTPNSTLDDPPY KINDSGGHRPILSKTIPGSALHYGNVTEYNVHNLYGMLQAKATNKALTNVTGKRPFVLSRSTFVSSGKYAAHWTGDNGARWNDLAYSIPGILNFGLFGVP MVGADICGFIGDTNEELCRRWIQVGAFYPFSRDHSDKNSIRQELYVWESVAASAKKVLGLRYRLLPLYYTSMYQAHKNGTPIARPLFFSFPEDTNTYDIS SQFLIGKGVMVSPVLQQGATSVEAYFPAGNWYDLFNYTSLSVDTGKNVTLDAPPDHINVHVHEGNIL | |||
GH31 | 1102 | 1569 | 0 |
YFFSGPTPELVMEQYTELIGRPAPMPYWSFGFHQCRYGYKDVADLEGVVAGYANARIPLEVMWTDIDYMDAYKDFTLDPINFPLDKMQNFTNTLHQNGQK YVLILDPGISINESYATYIRGKAADIYIKRDGIPYQGNVWPGDVYYPDFVHPQSEQFWANEIKLFQDQLPFDGLWLDMNEVSNFITSPPTLNSTLDDPPY KINDSGVQRPIISKTVPASALHFGNLTEYNVHNLYGFLESRATHQGLINVTGKRPFILTRSTFVSSGKYAAHWTGDNAARWSDLAYTIPGILNFGIFGVP MVGADICGFSLNTTEELCRRWIQLGAFYPFSRDHSEKFTIRQELYVWDSVAASARKVLGLRYRLLPLFYTSMYQAHKKGTPIARPLFFSFPEDTNTYDIS SQFLIGRGVMVSPVLQQGANSVDAYFPTGNWFDLFNYSRSVSVHSGEYVTLDAPPDHINVHIREGNIL |
Full Sequence |
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Protein Sequence Length: 1727 Download |
MERNRSKHTA KATFHHLLPV FFFYVFFSLD CLFAQELVGY GYKVQSVNSS DSSGKTLTVN 60 LGLINSSSVY GPDISNLTLY VSYETKDRLR VRITDSTQQR WEIPQEIIPR QNQTSQNFSV 120 TDNDLVFTLR NTTPFGFTIT RRSTNDTVFD TTPNPSDPNT TFIFKDQYIQ LSSSLPNNRS 180 SLYGLGEHTK STFKILANQM LTLWAADIAS VNPDLNLYGS HPFYMDVRSP SGDGRVKAGT 240 THGVLLLNSN GMDVNYTGDR VTYNVIGGVV DLYFFAGPTP ESVMDQYTEL IGRPAPMPYW 300 SFGFHQCKYG YKNVSDLEGV VAGYANASIP LDVMWTDIDY MDAYKDFTLD PVNFPLDKMQ 360 NFTNTLHQNG QKYVVILDPG ISINDSYGSY TRGKEADIYI KRDGIPYQGN VWPGDVYFPD 420 FVHPQSEPYW ENEIKLFIDQ LPVDGLWIDM NEVSNFQTSA PTPNSTLDDP PYKINDSGGH 480 RPILSKTIPG SALHYGNVTE YNVHNLYGML QAKATNKALT NVTGKRPFVL SRSTFVSSGK 540 YAAHWTGDNG ARWNDLAYSI PGILNFGLFG VPMVGADICG FIGDTNEELC RRWIQVGAFY 600 PFSRDHSDKN SIRQELYVWE SVAASAKKVL GLRYRLLPLY YTSMYQAHKN GTPIARPLFF 660 SFPEDTNTYD ISSQFLIGKG VMVSPVLQQG ATSVEAYFPA GNWYDLFNYT SLSVDTGKNV 720 TLDAPPDHIN VHVHEGNILA LQGEALTTQA ARNTSFELLV VIGSSNESAG EVFLDDGEEL 780 EMGGEGGKWS FVRFHSARAQ NGSLILSSNV ENGDFALSQG WIIDKITVLG LDKDHAKVES 840 SVSLPIGKEF ELELKPNQTC FVAEEPVGYG YRVESVNSDP SGKTVTASLG LINSSLVYGP 900 DIPNLKLYAS YETKERLRIR IIDSDNQRWE IPQDILPHQT PQTSHHSISE NDFIFTLHNT 960 TPFGFTVTRR SSSEVVFDTT PNPSDPSSIF VFKDQYIQLS SSLPETRSSL YGLGEHTKPS 1020 FKLQPNQTLT LWTADIGSAN PDVNLYGSHP FYMDVRSPSG DNGKVTAGAT HGVLLLNSNG 1080 MDVNYGGDRV TYKVIGGVVD LYFFSGPTPE LVMEQYTELI GRPAPMPYWS FGFHQCRYGY 1140 KDVADLEGVV AGYANARIPL EVMWTDIDYM DAYKDFTLDP INFPLDKMQN FTNTLHQNGQ 1200 KYVLILDPGI SINESYATYI RGKAADIYIK RDGIPYQGNV WPGDVYYPDF VHPQSEQFWA 1260 NEIKLFQDQL PFDGLWLDMN EVSNFITSPP TLNSTLDDPP YKINDSGVQR PIISKTVPAS 1320 ALHFGNLTEY NVHNLYGFLE SRATHQGLIN VTGKRPFILT RSTFVSSGKY AAHWTGDNAA 1380 RWSDLAYTIP GILNFGIFGV PMVGADICGF SLNTTEELCR RWIQLGAFYP FSRDHSEKFT 1440 IRQELYVWDS VAASARKVLG LRYRLLPLFY TSMYQAHKKG TPIARPLFFS FPEDTNTYDI 1500 SSQFLIGRGV MVSPVLQQGA NSVDAYFPTG NWFDLFNYSR SVSVHSGEYV TLDAPPDHIN 1560 VHIREGNILA LQGEALTTQA ARKTAFELLV VISSSGESSG EVFLDDGEEV EMGGEGGKWS 1620 VVKFYCGAAN GSVFLRSMLE NGGFALSQKW IIDKITLIGL ENVDGLEGFA VNITEGTNLK 1680 GKSVVKANFH SDKRFFMVEI SSVSILIGKE FELELRLKHD TGEDTL* 1740 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG1501 | COG1501 | 3.0e-119 | 903 | 1591 | 701 | + Alpha-glucosidases, family 31 of glycosyl hydrolases [Carbohydrate transport and metabolism] | ||
pfam01055 | Glyco_hydro_31 | 0 | 1102 | 1569 | 472 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
pfam01055 | Glyco_hydro_31 | 0 | 273 | 739 | 472 | + Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases. | ||
cd06602 | GH31_MGAM_SI_GAA | 0 | 1121 | 1498 | 383 | + This family 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). | ||
cd06602 | GH31_MGAM_SI_GAA | 0 | 292 | 669 | 383 | + This family 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). |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3w38_A | 0 | 865 | 1721 | 39 | 912 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3w38_A | 0 | 1 | 833 | 1 | 853 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3w37_A | 0 | 865 | 1721 | 39 | 912 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3w37_A | 0 | 1 | 833 | 1 | 853 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 3ctt_A | 0 | 886 | 1608 | 66 | 774 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |