| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10025960 |
| Family | GH38 |
| Protein Properties | Length: 1425 Molecular Weight: 160344 Isoelectric Point: 6.3295 |
| Chromosome | Chromosome/Scaffold: 319 Start: 71836 End: 82266 |
| Description | Glycosyl hydrolase family 38 protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH38 | 485 | 807 | 0 |
| NVHLVPHSHDDVGWLKNIDQYYVGSNNSIQNACVQNVLDSVVAALLKDPNRKFVFAEMCILVVKMGSHEIFFLTFGCKAQSFFNRWWEEQSKETQEIVRK LDHGGQLEFVNGGWCMHDEAATHYIDMIDQTTLGHRMIKNEFNTTPRAAWQIDSFGHSAVQAYLLGAESGFDSVHFATVDYQDRAKRKADKSLEVVWRGS RTFGSSSQGFHFEVGDEDDQGVIVQDDPRIFDYNVDQRVKEFVLAAKTRANVTRANHVMWTMGDDFQYQFAESWFRQMDKLIHHVNKGGEINVLYSTPSI YTDAKNAANQSWPLKTDDFFPYA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1425 Download |
| MGETRDNDYE EELLDYEEEE EKAPDSITAK VNGEAPKKGY VGIHSSGFRD FLLKPELLRA 60 IVDSGFEHPS EVQHECIPQA ILGMDVIFQA KSGMGKTAVF VLSTLQQIEP TPGQVIALVL 120 CHTRELAYQI CHEFERFSTY LPDTKVAVFY GGVNIKTHRD LLKNECPHVV VGTPGRILAL 180 ARDKELSLKN VRHFILDECD KMLESLDMRR DVQEIFKMTP HDKQVMMFSA TLSKEIRPVC 240 KKFMQDPMEI YVDDEAKLTL HGLVQHYIKL TELEKNRKLN DLLDALDFNQ VVIFVKSVSR 300 AAELNKLLIE CNFPSICIHS GMSQEERLTR YKGFKEGHKR ILVATDLVGR GIDIERVNIV 360 INYDMPDSAD TYLHRVGRAG RFGTKGLAIT FVSSASDSDV LNQVQERFEV DIKELPEQID 420 TSTYSKFSTT SMKCKKHEKA DVAVCLVHRH IYSLRNSCRR RSFVDGSPLN YHYDTGSGVV 480 DGKLNVHLVP HSHDDVGWLK NIDQYYVGSN NSIQNACVQN VLDSVVAALL KDPNRKFVFA 540 EMCILVVKMG SHEIFFLTFG CKAQSFFNRW WEEQSKETQE IVRKLDHGGQ LEFVNGGWCM 600 HDEAATHYID MIDQTTLGHR MIKNEFNTTP RAAWQIDSFG HSAVQAYLLG AESGFDSVHF 660 ATVDYQDRAK RKADKSLEVV WRGSRTFGSS SQGFHFEVGD EDDQGVIVQD DPRIFDYNVD 720 QRVKEFVLAA KTRANVTRAN HVMWTMGDDF QYQFAESWFR QMDKLIHHVN KGGEINVLYS 780 TPSIYTDAKN AANQSWPLKT DDFFPYADGE DAYSRFVFQN LRFGLASEEA EMTVSAALTC 840 LVSKKTRGQC GSLAKTSSQL TRKMQFSQTK SLLVQCQLLN ISYCEPTTEA GSGKPLVVVV 900 YNPLGWNRTD IVRIPVNDSS LVVSDSSGKA IESQYISMDN LTNNLRKFYL KAYTGKSSDQ 960 VPKSWLVFQL SLPPLGWSTY FLSTAPDIAK TRNSYSVKGT AVDDVVEIGP GNLKMSFSST 1020 SGQLTRMYNN VTGVDVPIQQ SYVWYASSTE AAQSSGAYIF RPDSNTPNIV ARKVAMEVIR 1080 GPIVDEIHQQ FGQWIYQVTR LYKDKQHAEI EYTIGPIPTD DGAGKEVVSQ LTANMVTDKV 1140 FYTDSNGRDF LKRVRNVRND WNLSVNQPVA GNYYPVMHRK SDEIRLNLGA YITDSKAELS 1200 VLVDRATGGG SIKDGQLELM LHRRILQDDG RGVGEPLDEQ VCVDNSLTCQ GLTVRGNYYV 1260 SIDKLGGGAM WRRTTGQEIY SPLLLAFTHE EDKLWKATHL TTSTLLDTGY SLPLNVALIT 1320 LEELEDGSVL LRLAHLYEAG EDAKYSSLAK VELKKMFPGK QIKGVKEMSL SGNQEKSNMK 1380 RMSWTVEGDK GNEGKPLRGG PFDPSAQIVE LAPMEIRTFL LTFS* 1440 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01074 | Glyco_hydro_38 | 7.0e-82 | 485 | 807 | 329 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
| PTZ00424 | PTZ00424 | 1.0e-82 | 48 | 419 | 373 | + helicase 45; Provisional | ||
| cd00451 | GH38N_AMII_euk | 3.0e-94 | 484 | 771 | 294 | + 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. | ||
| COG0513 | SrmB | 9.0e-126 | 45 | 414 | 374 | + Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis] | ||
| cd10810 | GH38N_AMII_LAM_like | 5.0e-146 | 484 | 771 | 304 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0003676 | nucleic acid binding |
| GO:0004386 | helicase activity |
| GO:0004559 | alpha-mannosidase activity |
| GO:0005524 | ATP binding |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEC66555.1 | 0 | 473 | 1423 | 27 | 1004 | hypothetical protein OsI_32713 [Oryza sativa Indica Group] |
| RefSeq | NP_001064140.1 | 0 | 473 | 1423 | 27 | 1004 | Os10g0140200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002265360.1 | 0 | 473 | 1423 | 29 | 1006 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002303405.1 | 0 | 451 | 1423 | 22 | 1011 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002464752.1 | 0 | 479 | 1423 | 35 | 1007 | hypothetical protein SORBIDRAFT_01g026390 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1xti_A | 0 | 39 | 424 | 1 | 386 | A Chain A, Structure Of Wildtype Human Uap56 |
| PDB | 1xtj_A | 0 | 39 | 424 | 1 | 386 | A Chain A, Structure Of Human Uap56 In Complex With Adp |
| PDB | 1xtk_A | 0 | 44 | 424 | 5 | 385 | A Chain A, Structure Of Decd To Dead Mutation Of Human Uap56 |
| PDB | 1t6n_B | 0 | 33 | 252 | 1 | 220 | A Chain A, Crystal Structure Of The N-Terminal Domain Of Human Uap56 |
| PDB | 1t6n_A | 0 | 33 | 252 | 1 | 220 | A Chain A, Crystal Structure Of The N-Terminal Domain Of Human Uap56 |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO778661 | 424 | 1 | 424 | 0 |
| HO636717 | 401 | 24 | 424 | 0 |
| HO575046 | 401 | 24 | 424 | 0 |
| HO403659 | 404 | 23 | 424 | 0 |
| HO779729 | 369 | 30 | 398 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
