Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna06416.1-v1.0-hybrid |
Family | GH38 |
Protein Properties | Length: 2031 Molecular Weight: 228878 Isoelectric Point: 6.2752 |
Chromosome | Chromosome/Scaffold: 5 Start: 4077966 End: 4091772 |
Description | Glycosyl hydrolase family 38 protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH38 | 39 | 351 | 0 |
NVHLVPHTHDDVGWLKTVDQYYVGSNNSIQGACVQNVLDSLIPALLADKNRKFVYVEQAFFQRWWRDQSEEVQDTVKELVSSGQLELINGGMCMHDEAAP HYIDMIDQTTLGHRFIKQEFNVTPRIGWQIDPFGHSAVQAYLLGAEVGFDSLFFGRIDYQDRAKRKVDKSLEVVWRGSKSLGSSAQIFAGAFPANYEPPS DNFYFEVNDASPIVQDDMDLFDYNVPDRVNDFVSAAMLQANITRTNHIMWTMGTDFKYQYAHTWFRQMDKFINYVNQDGRVNALYSTPSIYTDAKYAADE SWPIKSDDFFPYA | |||
GH38 | 1075 | 1389 | 0 |
NVHLVPHTHDDVGWVKTVDQYYTGANNSLLGSPASVRNVLDSLVPALLADKNRKFIYAEQAFFQLWWREQSEAIQDTVKQLVSSGQLEFINGGMCMHDEA ATHYIDMIDQTTLGHRFIKQEFNVTPRVGWQIDTFGHSSVQAYLLGAEVGFDSLFFGRIDYQDKAKRKDDKSLEVVWRGSKSLGSSAQIFAGAFPGLYVP PSDNFYFETDDPAPLVQDDMNLGDYNMPERVNDFVSEAISQANITRTNHIMWTMGKDFAYQYANSWFRQMDKFIHHVNQDGRVNALYSTPSMYTNAKYAT NESWPIKSDDFFPYA |
Full Sequence |
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Protein Sequence Length: 2031 Download |
MAVVAYFPVV LVFTVFLYAA EAKYIQYNTT SVLVPGKLNV HLVPHTHDDV GWLKTVDQYY 60 VGSNNSIQGA CVQNVLDSLI PALLADKNRK FVYVEQAFFQ RWWRDQSEEV QDTVKELVSS 120 GQLELINGGM CMHDEAAPHY IDMIDQTTLG HRFIKQEFNV TPRIGWQIDP FGHSAVQAYL 180 LGAEVGFDSL FFGRIDYQDR AKRKVDKSLE VVWRGSKSLG SSAQIFAGAF PANYEPPSDN 240 FYFEVNDASP IVQDDMDLFD YNVPDRVNDF VSAAMLQANI TRTNHIMWTM GTDFKYQYAH 300 TWFRQMDKFI NYVNQDGRVN ALYSTPSIYT DAKYAADESW PIKSDDFFPY ADNINAYWTG 360 YFTSRPALKG YVRVMGGYYL AARQLEFFKG RSKSGPNTEY LADALAIAQH HDAVSGTSKQ 420 HVADDYAKRL SIGYVETEKV VAKSLACMTE PSQAGCKSVC PLLNISYCPS SEVHLSKGKD 480 LVIVVYNSLG WKRKDVIKIP VVSEHVTVKD SAGKEIELQI LPLLNESLSI RNNLVKAYLG 540 ISPSVTPSYW LAFSATVPPL GFSTYIVSSA KQTATTERLT LHKTELSQNN EIKVGPGNLK 600 LIYSGNDGKL IEYTNSRSSV KELVDQSFSY YPGDDGTHAN KTDLQASGAY IFRPNGTYPI 660 NSEGEVPLTV LRGPLLDEVH QKINSWIYQV TRVYKEKEHA EIEFTVGPIP IDDGIGKEIV 720 TKITTSMKTN KQFYTDSNGR DFIERIRDYR KDWTLEVNQP VAGNYYPINL GIYAKDNNTE 780 MSVLVDRSVG GSSIVDGQLE LMIHRRLLYD DARGVGEALN ETVCIQDDCK GLTVTGKYYL 840 RLDPIGEGAK WRRSFGQEIY SPFLLAFTEQ DGHRWTKSHV TTFSGMDPSY SLPDNVAIIT 900 IQELEDGKVL FRLAHLYEIE EDKDLSVMAS VELKKVFANK KIKQITEMSL SANQGRAEME 960 KKRLVWKVEG SSEEPKALRG GPVDPTKLVF FRCHWSSAQP LLNCRAFMPL IVRGTNIGLE 1020 VSIVSAFLNI QVLGTSMAVE ACCLRLLMVL VVFLFAESKF IAYNTTSQIV PGKLNVHLVP 1080 HTHDDVGWVK TVDQYYTGAN NSLLGSPASV RNVLDSLVPA LLADKNRKFI YAEQAFFQLW 1140 WREQSEAIQD TVKQLVSSGQ LEFINGGMCM HDEAATHYID MIDQTTLGHR FIKQEFNVTP 1200 RVGWQIDTFG HSSVQAYLLG AEVGFDSLFF GRIDYQDKAK RKDDKSLEVV WRGSKSLGSS 1260 AQIFAGAFPG LYVPPSDNFY FETDDPAPLV QDDMNLGDYN MPERVNDFVS EAISQANITR 1320 TNHIMWTMGK DFAYQYANSW FRQMDKFIHH VNQDGRVNAL YSTPSMYTNA KYATNESWPI 1380 KSDDFFPYAS DVNAYWTGYF TSRPALKRYV RMMSSYYLAA RQLEFFKGIR KSGPNTDSLA 1440 DALAVAQHHD AVSGTSRQHV ADDYTKRLYI GYKEAEKCPL LNISYCPPSE VDLTKGKDLV 1500 IVVYNPLGWR RKDVIRIPVV NENVTVKDST GKKVESQILP LLNASVSIRD YHVKAYLGIA 1560 PSVTPSYWLA FSATVPPLGF STYIVSNDLN IAATTSKRHT VYKTETSQDE TIKVGPGNLK 1620 LIYSGNDGEL IQYTNSRSLV KESVKQSFSY YPGDDGSVVD SYGEDGNPRF QASGAYIFRP 1680 NGTYPIKSKE QVSLTVLRGP LLDEVHQRIN SWIYQVTRVY KEKEHAEIEF IIGPIPADDG 1740 IGKEIVTKIT TSMRTNKQFY TDSNGRDFIQ RIRDYRKDWN LEVNQPVAGN YHPINLGIYM 1800 KDNNTELSVL VDRSVGGSSI VDGQLELMLH RRLLADDDKG IAEQLNETVC IQDDCKGLTI 1860 TGKYHMRIDP LGEGAKWRRS FGQEIYSPFL LAFTEKDGDN WTSSHVTTFS GMDPSYALPD 1920 NIALLTLQEL EDGKVLLRLA HLYEIEEDKD LSVMASVELK KVFANKKIKH ITEMSLTANQ 1980 DRREMERKRL VWNVEGSNKE PKALRGGAVD PTKLVVDLAP MEIRTFIVNF * 2040 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02701 | PLN02701 | 3.0e-94 | 37 | 817 | 878 | + alpha-mannosidase | ||
cd00451 | GH38N_AMII_euk | 3.0e-99 | 1074 | 1352 | 279 | + N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. | ||
cd00451 | GH38N_AMII_euk | 4.0e-100 | 38 | 314 | 277 | + N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. | ||
cd10810 | GH38N_AMII_LAM_like | 1.0e-157 | 1074 | 1353 | 282 | + N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base. | ||
cd10810 | GH38N_AMII_LAM_like | 3.0e-167 | 38 | 315 | 280 | + N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004559 | alpha-mannosidase activity |
GO:0005975 | carbohydrate metabolic process |
GO:0006013 | mannose metabolic process |
GO:0008270 | zinc ion binding |
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 | 1o7d_A | 0 | 27 | 321 | 3 | 298 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 1o7d_A | 0 | 1062 | 1359 | 2 | 298 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
PDB | 1hxk_A | 0 | 25 | 819 | 38 | 852 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hxk_A | 0 | 1073 | 1843 | 50 | 850 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 0 | 25 | 819 | 38 | 852 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |