Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna14589.1-v1.0-hybrid |
Family | CE8 |
Protein Properties | Length: 1356 Molecular Weight: 149767 Isoelectric Point: 5.7152 |
Chromosome | Chromosome/Scaffold: 1 Start: 7807262 End: 7816333 |
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 | 71 | 344 | 0 |
NVHLVAHSHDDVGWLKTVDQYYVGSNNSIQGACVENTLDSVVESLVRDPNRKFVFAEMAFFQRWWLTQSVEVQERVWKLVDAGQLEFVNGGWCMHDEAAV HYIDMIDQTTLGHLAIKQQFNKTPRAGWQIDPFGHSAVQGYLLGAELGFDSVHFARIDYQDRAQRKGDKSLEVIWHGSKTFGSSSQIFANAFPRHYSPPE GFHFEVFDDFVPVQDNPLIFDYNVEQRVNDFITAAITQDGRVNALYSTPSLYTDAKNAANQSWPLKTEDYFPYA | |||
CE8 | 1061 | 1342 | 0 |
VMANGGDFKKISEAIDSIPASNTKRVIIYVGGGVYNEKITIPKNKPFVTLMGDSKNMPNLTFNGDSAKYGTLYSATLSVESDYFVGVNLNIINSSPRPDG KKEGAQALALKLSGNKAALYNCQMFGFQDTLCDDQGNHFIKDSYVEGTVDFIFGSGKSLYLNTHINVLGDSGMTVITANAREGDEDKGYSFVHCSITGTG SGTFLGRAWRAAPKVTFAYTEMGEVVKPEGWTDNNHPEYDKSVSFGEYKNTGPGSSMSKRVSFTKELSDADAKPFISLGFID |
Full Sequence |
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Protein Sequence Length: 1356 Download |
MEPHMVACTD VPFSLYKADP ASGETECAEM LKLAVFFECV IGLIWFLGVV SVDGVYVKYQ 60 TGSGVVEGKL NVHLVAHSHD DVGWLKTVDQ YYVGSNNSIQ GACVENTLDS VVESLVRDPN 120 RKFVFAEMAF FQRWWLTQSV EVQERVWKLV DAGQLEFVNG GWCMHDEAAV HYIDMIDQTT 180 LGHLAIKQQF NKTPRAGWQI DPFGHSAVQG YLLGAELGFD SVHFARIDYQ DRAQRKGDKS 240 LEVIWHGSKT FGSSSQIFAN AFPRHYSPPE GFHFEVFDDF VPVQDNPLIF DYNVEQRVND 300 FITAAITQDG RVNALYSTPS LYTDAKNAAN QSWPLKTEDY FPYADQINAY WTGYFTSRPG 360 LKRYIRSLSG YYLAARELEF LVGKRANGSN TFSLGDALGI AQHHDAATGT AKQHTTNDYV 420 KRLSIGVSEA EAVVSSALLC LTTNKSGDQC KDPAVTFSQC RLLNISFCPP TEEDIPAGKS 480 LVVVAYNPLG WNRTEIVRIP VNDANLVVQD SSGNTLETQY ASVDNVTSNL RTFYTEAYLG 540 KSSKEIPKYW LIFQASVPPL GWDTYFISRG ATGKRRVGLL AVKDSSQNET IDIGPGDLKM 600 SFSSASGQLK RMYNSKTGVD VPIQQSYLWY GSSTAAQASG AYIFRPNGAP PTIVSRSVPF 660 KVFRGPLFDE IHQEFSSWIY QVTRVYRDKE HAEVEYTIGP IPTDDGLGKE VITRMTANMQ 720 TNKVFYTDSN GRDFIERVRD YRADWNLSVN QPVAGNYYPL NLGIFTSDNK SEFSVLVDRA 780 TGGSSIQDGQ VEMMLHRRLL VDDRRGVGEA LDETVCISNN TCQGLTVRGN YYMSINQYGD 840 GAQWRRTTGQ EVYSPLLLAF THENMENWNA SHVTKGSVMD SSYSLPHNVA LITLQELDGG 900 SALLRLAHLY EAGEAPQYST LAKVELKKML TGKTIKELKE MSLSANQEKS GMKKMKWHVE 960 GSTGEEPTPV RGGPVDSSTL VVELGPMEIQ KRMSIHAALM MITTVLLAAT VSMADDPVIP 1020 SDKSAVDKWF QDNVKPLADR KSSLDPDLVK AEDGDPKIVK VMANGGDFKK ISEAIDSIPA 1080 SNTKRVIIYV GGGVYNEKIT IPKNKPFVTL MGDSKNMPNL TFNGDSAKYG TLYSATLSVE 1140 SDYFVGVNLN IINSSPRPDG KKEGAQALAL KLSGNKAALY NCQMFGFQDT LCDDQGNHFI 1200 KDSYVEGTVD FIFGSGKSLY LNTHINVLGD SGMTVITANA REGDEDKGYS FVHCSITGTG 1260 SGTFLGRAWR AAPKVTFAYT EMGEVVKPEG WTDNNHPEYD KSVSFGEYKN TGPGSSMSKR 1320 VSFTKELSDA DAKPFISLGF IDGSKWLLPP PTPKV* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02304 | PLN02304 | 2.0e-79 | 1067 | 1349 | 293 | + probable pectinesterase | ||
cd00451 | GH38N_AMII_euk | 2.0e-85 | 70 | 302 | 233 | + 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. | ||
PLN02682 | PLN02682 | 6.0e-87 | 1066 | 1349 | 293 | + pectinesterase family protein | ||
cd10810 | GH38N_AMII_LAM_like | 7.0e-137 | 70 | 305 | 238 | + 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. | ||
PLN02665 | PLN02665 | 0 | 994 | 1351 | 360 | + pectinesterase family protein |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004559 | alpha-mannosidase activity |
GO:0005618 | cell wall |
GO:0005975 | carbohydrate metabolic process |
GO:0006013 | mannose 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 | 1hxk_A | 0 | 28 | 811 | 13 | 852 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hww_A | 0 | 28 | 811 | 13 | 852 | A Chain A, Golgi Alpha-Mannosidase Ii In Complex With Deoxymannojirimicin |
PDB | 1hty_A | 0 | 28 | 811 | 13 | 852 | A Chain A, Golgi Alpha-Mannosidase Ii |
PDB | 1ps3_A | 0 | 28 | 811 | 43 | 882 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
PDB | 3eju_A | 0 | 28 | 811 | 43 | 882 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |