| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000163211 |
| Family | GH38 |
| Protein Properties | Length: 2429 Molecular Weight: 272816 Isoelectric Point: 7.7171 |
| Chromosome | Chromosome/Scaffold: 000909246 Start: 6849 End: 26811 |
| Description | ARF-GAP domain 1 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH38 | 200 | 361 | 0 |
| NWSGVVFFQRWWRDQTEATQNTVKQLVSSGQLELINGGMCMHDEAAAHYIDMIDQTTLGHRFIKQEFNVTPRIGWQIDPFGHSAVQAYLLGAEVGFDSLF FARIDYQDRAKRKNEKSLEVVWRGSKSLGSSAQIFAGAFPENYGPPTNDFYFEVDDISPIVQ | |||
| Full Sequence |
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| Protein Sequence Length: 2429 Download |
| MALSMTHQIS ALSRTPIRTT EASSSSVELV TVSPMWKSLA AGLTCKIQKL EGFDGLSPPL 60 SSCRSLFLRS SQPDLSMACR AFATKAKSPV LEHQVRGTHD KGMGVPIYVM MPLDSVTMHN 120 LVNRKKAMNT SLQALKNAGV EGVMMDKIRT HRYTIFTYQG LERWQQAPFE SGTIFTYQGL 180 ERKRVGNKHH LKVGEEELMN WSGVVFFQRW WRDQTEATQN TVKQLVSSGQ LELINGGMCM 240 HDEAAAHYID MIDQTTLGHR FIKQEFNVTP RIGWQIDPFG HSAVQAYLLG AEVGFDSLFF 300 ARIDYQDRAK RKNEKSLEVV WRGSKSLGSS AQIFAGAFPE NYGPPTNDFY FEVDDISPIV 360 QDDTDLSDYN VLERVNDFVS AAISQAARQL EFFKGMSKSG SKTDSLADAL AIAQHHDAVS 420 GTERQHVADD YAKRLSIGYN ECPLLNISYC PPSEADLSTG KSLVIVVYNS LGWKRKDVIK 480 IPVINANVAV RDSTGKEIES QLIPLLNASA TIRNYHVKAY LGKSLGETPY YWLAFSATVP 540 PLGFSTYFIS SATRKATTSE VYRSEAGRND TIEVGRGNLR LIYSGNEGQL TKYMNSRSLV 600 KKQIKQSFSY YAGDNGYVDL QAEGAYVFRP NGSYPIKSGG KVTRVYKEKE HAEIEFIIGP 660 IPIDNGVGKD IVSKITTGMK TNKRFYTDSN GRDFIERIRD YRKDWDLEVN QPVAGNYYPI 720 NLGIYTKDNN TELSVLVDRS VGGSSIVDGQ LELMLHRRLL SDDDKGIFEA LNETVCIRDD 780 CEGLIEIYSP FLLAFTEQDE DSWTSSYVTT FSGMDPSYTL PDNVAIITLQ ELEDEKLLFR 840 LAHLYEIDED KDLSVMASVE LKKVFADKKI RKVTEMSLSA NQERAEMEKK RLVWKAEGSS 900 DKEAKVLRGG PVDPTKLVVD LAPMEIRTLI IDLARAVAAP RRPSTKVVRA TERDTESTAT 960 ARPPPPEQSI ELHYPRHHLI PGRIFQMRKE SQASAMEIED PKPNSSDQIS PKFSINGSFS 1020 NPFVSEIIIS VVGFFRLDFD LISIFTVLLL LKSAQMQHGL RHGDYTRYRR YCTARLRRLY 1080 KSLKFTHGRG KYNRRAITES TVTEVRYLHV VLYTAERAWS HAMEKRQVLD GPNARQRIYL 1140 IGRLRKAVKW ATLFAQLCAI KGDSRTSLEA EAYASFMKGS LLFEQDQNWD TALMNFKSAR 1200 AVXEELAKYG DLENQVLCRE RVEELEPSIR YCLHKVGESN LQASELLQIG EMEGPALDLF 1260 KAKLEVGLVT FKAVMAEARS QQAASMTEFH WLGHRFPISN PKTRVSILKA QELEKDLLGS 1320 STNSLPPEKK LGIFDKIFTA YHEARGSIRS DLASAGNSEN VKDDLNGLDK AVSAVLGERT 1380 IERNQMLVTI AKSKLTKRRD DKNEKATKPE ELVRLYDLLL QNTSDLSDLV SSGRDKKPEE 1440 VAFADECELK SLAFRAERCF FLGKSYSLAG KRVEAYVLYC HARSLAENAL AKFQSVNNGD 1500 EAIIKELKTL CDECRSNSCI EHATGIMEEL KAPENLSKKI SSINLSGIDK KVEFLLEKLN 1560 VYESAVGDAN VKSAPRIEAF PPPFQSIPRN PIVLDLAYNH IDFPSLQHRL RKDKSGGFLK 1620 RHLRPPTAQT SLHFRSLPLK QKPKTATQEE EIQDEGHLCI LPNMHFAKLD DSPMFRQQIQ 1680 GLEESAESLR GRCYKFYKGC RKYTEGLGEA YDGEIAFITA LESFGGGHND PIFSALGGQV 1740 MSRFTIALRE IATYKEVLRS QIEHMVNDRL VNIVHVDLHE VKAREKFLSL RKSTRMDIAA 1800 SIEEELQNAR SSFEQARFSL VAVLSDIEAK KRFEFLEAVS GVMDAHLRYF KQSYELLHAM 1860 EPYIHQVLAY AQQTRESCNQ EQMCLNERIQ EYKKQIDRES TQSLSGIHGS TKGDGPQPFS 1920 RKSHKVIEEV MQSAAKGKVQ TIRQGYLSKR SSNLRGDWKR RYFILDSRGM LYYYRKPWSW 1980 PSYGSPSSPQ KNNSSENGSG LLSRWLSSHY HGGVHDEKSV ASHTVNLLTS TIKVDADQTD 2040 LRFCFRIISP AKIYTLQAEN ALDQMDWIEK ITGVIASLLS FQTPERRLST SPTGSDDQFS 2100 GNEGNLLESA SDAEQTAIQE LSPKITAYNY LRISKSMQPH KLKEKSEKPI DILRRVCGND 2160 KCADCGAPEP DWASLNLGIL ICIECSGVHR NLGVHVRSLT LDVKVWEPSV LTLFQSLGNA 2220 FANSIWEEML YSRSSLQADN MPIGFSKADR NEPFLMIKPC NDDLNSTKER YIQAKLCKSV 2280 RANDKKAVYR YIIGYEADVN SRSVQALDDI SGDKPSSSNL NSVTQTEIQP AEDTAEGCSL 2340 LHLACQSADI GMVELLLQYG ANVKATDSKG QTPLHYSVIR GNIAIAKLLL TRGADPKATD 2400 REGKTPSELV SDSASKDNGM LALLTNSGR 2460 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01412 | ArfGap | 6.0e-37 | 2147 | 2275 | 132 | + Putative GTPase activating protein for Arf. Putative zinc fingers with GTPase activating proteins (GAPs) towards the small GTPase, Arf. The GAP of ARD1 stimulates GTPase hydrolysis for ARD1 but not ARFs. | ||
| pfam01074 | Glyco_hydro_38 | 8.0e-51 | 201 | 356 | 156 | + Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. | ||
| cd00451 | GH38N_AMII_euk | 5.0e-62 | 190 | 386 | 197 | + 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. | ||
| cd07606 | BAR_SFC_plant | 1.0e-78 | 1678 | 1863 | 201 | + The Bin/Amphiphysin/Rvs (BAR) domain of the plant protein SCARFACE (SFC). BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. The plant protein SCARFACE (SFC), also called VAscular Network 3 (VAN3), is a plant ACAP (ArfGAP with Coiled-coil, ANK repeat and PH domain containing protein), an Arf GTPase Activating Protein (GAP) that plays a role in the trafficking of auxin efflux regulators from the plasma membrane to the endosome. It is required for the normal vein patterning in leaves. SCF contains an N-terminal BAR domain, followed by a Pleckstrin Homology (PH) domain, an Arf GAP domain, and C-terminal ankyrin (ANK) repeats. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. | ||
| cd10810 | GH38N_AMII_LAM_like | 4.0e-97 | 204 | 388 | 187 | + 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:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004559 | alpha-mannosidase activity |
| GO:0005515 | protein binding |
| GO:0005543 | phospholipid 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 |
| EMBL | CBI29251.1 | 0 | 1664 | 2427 | 1 | 830 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002299350.1 | 0 | 1664 | 2427 | 1 | 838 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002303749.1 | 0 | 1664 | 2427 | 1 | 828 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002511098.1 | 0 | 1664 | 2425 | 1 | 817 | gcn4-complementing protein, putative [Ricinus communis] |
| RefSeq | XP_002512662.1 | 0 | 1664 | 2427 | 1 | 828 | ATP binding protein, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1o7d_D | 0 | 579 | 773 | 10 | 229 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
| PDB | 1o7d_A | 3.00018e-42 | 204 | 386 | 72 | 255 | C Chain C, The Structure Of The Bovine Lysosomal A-Mannosidase Suggests A Novel Mechanism For Low Ph Activation |
| PDB | 3t9k_B | 3e-26 | 2153 | 2417 | 39 | 315 | A Chain A, Crystal Structure Of Acap1 C-portion Mutant S554d Fused With Integrin Beta1 Peptide |
| PDB | 3t9k_A | 3e-26 | 2153 | 2417 | 39 | 315 | A Chain A, Crystal Structure Of Acap1 C-portion Mutant S554d Fused With Integrin Beta1 Peptide |
| PDB | 1ps3_A | 5e-26 | 393 | 771 | 448 | 882 | A Chain A, Golgi Alpha-mannosidase Ii In Complex With Kifunensine |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO780062 | 552 | 386 | 855 | 0 |
| GR715419 | 306 | 1196 | 1501 | 0 |
| CO125721 | 287 | 1219 | 1505 | 0 |
| HO780062 | 40 | 347 | 386 | 0.001 |
| HO780062 | 24 | 416 | 439 | 0.052 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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