Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna03056.1-v1.0-hybrid |
Family | GT57 |
Protein Properties | Length: 869 Molecular Weight: 97019.7 Isoelectric Point: 9.3308 |
Chromosome | Chromosome/Scaffold: 3 Start: 10134253 End: 10145274 |
Description | ALG6, ALG8 glycosyltransferase family |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT57 | 31 | 515 | 0 |
ATCLKLLLIPAYRSTDFEVHRHWLAITNSLPLSQWYSDETSLWTLDYPPFFAYFERLLSLFANLIDPQIVHLHNGLNYSSDTVVYFQRVSVCVSDLCLLF GVYRLTRRLDHVRRRVMWVLVVWSPMLLIVDHLHFQYNGLLLGVLLVSVSYLEEGRDLMGGFVFAVLLCFKHLFAVAAPVYFVYLLRHYCWKGLVKGFGR LLVMGSVVVAVFTVAYGPFVYHGQMKQVIHRMFPFGRGLCHAYWAPNFWVFYILLDKVIAFLLGRLGFNIQAPAASFTGGLVGDSSPFAVLPQITPAITF IMVLLALSPCLIKAWRDPRPVMITRWVAYAYTCGFLFGWHVHEKASLQFVIPLAIVAVQDLDTARHYFFLSIVSCYSLFPLLYESQEYPIKVLLLLLHSM LMWLGFSAQFTKDKTLEMAPSGKRKDNHIGSNRSTAAAQKGGFVIGWEIWSYLVGLVLVEIWGQFLHPMFLGDKLPFLPLMLIST |
Full Sequence |
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Protein Sequence Length: 869 Download |
MEPQTTKKIL KNPSKPNNPK LSELWWFFAA ATCLKLLLIP AYRSTDFEVH RHWLAITNSL 60 PLSQWYSDET SLWTLDYPPF FAYFERLLSL FANLIDPQIV HLHNGLNYSS DTVVYFQRVS 120 VCVSDLCLLF GVYRLTRRLD HVRRRVMWVL VVWSPMLLIV DHLHFQYNGL LLGVLLVSVS 180 YLEEGRDLMG GFVFAVLLCF KHLFAVAAPV YFVYLLRHYC WKGLVKGFGR LLVMGSVVVA 240 VFTVAYGPFV YHGQMKQVIH RMFPFGRGLC HAYWAPNFWV FYILLDKVIA FLLGRLGFNI 300 QAPAASFTGG LVGDSSPFAV LPQITPAITF IMVLLALSPC LIKAWRDPRP VMITRWVAYA 360 YTCGFLFGWH VHEKASLQFV IPLAIVAVQD LDTARHYFFL SIVSCYSLFP LLYESQEYPI 420 KVLLLLLHSM LMWLGFSAQF TKDKTLEMAP SGKRKDNHIG SNRSTAAAQK GGFVIGWEIW 480 SYLVGLVLVE IWGQFLHPMF LGDKLPFLPL MLISTAYERV GKSRAVIFDY LMERLSKNLS 540 AGKQKFLVLQ ETLIKTSGDI CKSEGSAEDS AHVLCKRPTA SNVLSSLNLG NSLLPKFTLE 600 TVDAGTFFAS ESLDKLRKPK IRKKAMWKRA ANWGWKLNVD DSFLAPILLL VDILEPERPP 660 LSATMLRRAT ALLTRPASSS LRAARAFSTE VAEAGDAPAN PAFNEAWKKV VPHIEPPKTP 720 LSFMKPRPAV PSSIPTKLTV NFVLPYASEL SAKEVDMVII PASTGQMGVL PGHVATIAEL 780 KPGILSVHEG NDVTKYFVSS GFAFIHANSY ADIIAVEAVP IDRVDASLVQ KGLAEFTQKL 840 NSASTDLEKA EAQIGVDVHS ALNAALTG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK00571 | atpC | 2.0e-17 | 738 | 854 | 118 | + F0F1 ATP synthase subunit epsilon; Validated | ||
pfam02823 | ATP-synt_DE_N | 2.0e-19 | 738 | 818 | 82 | + ATP synthase, Delta/Epsilon chain, beta-sandwich domain. Part of the ATP synthase CF(1). These subunits are part of the head unit of the ATP synthase. The subunit is called epsilon in bacteria and delta in mitochondria. In bacteria the delta (D) subunit is equivalent to the mitochondrial Oligomycin sensitive subunit, OSCP (pfam00213). | ||
COG0355 | AtpC | 5.0e-20 | 738 | 858 | 123 | + F0F1-type ATP synthase, epsilon subunit (mitochondrial delta subunit) [Energy production and conversion] | ||
cd12152 | F1-ATPase_delta | 2.0e-31 | 738 | 861 | 125 | + mitochondrial ATP synthase delta subunit. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit. | ||
pfam03155 | Alg6_Alg8 | 3.0e-100 | 30 | 515 | 502 | + ALG6, ALG8 glycosyltransferase family. N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147. |
Gene Ontology | |
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GO Term | Description |
GO:0005789 | endoplasmic reticulum membrane |
GO:0015986 | ATP synthesis coupled proton transport |
GO:0016758 | transferase activity, transferring hexosyl groups |
GO:0045261 | proton-transporting ATP synthase complex, catalytic core F(1) |
GO:0046933 | proton-transporting ATP synthase activity, rotational mechanism |
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 | 4b2q_h | 2e-19 | 738 | 866 | 4 | 131 | V Chain V, Model Of The Yeast F1fo-Atp Synthase Dimer Based On Subtomogram Average |
PDB | 4b2q_H | 2e-19 | 738 | 866 | 4 | 131 | V Chain V, Model Of The Yeast F1fo-Atp Synthase Dimer Based On Subtomogram Average |
PDB | 3zry_H | 2e-19 | 729 | 866 | 1 | 137 | V Chain V, Model Of The Yeast F1fo-Atp Synthase Dimer Based On Subtomogram Average |
PDB | 3zia_R | 2e-19 | 729 | 866 | 1 | 137 | J Chain J, The Structure Of F1-atpase From Saccharomyces Cerevisiae Inhibited By Its Regulatory Protein If1 |
PDB | 3zia_H | 2e-19 | 729 | 866 | 1 | 137 | J Chain J, The Structure Of F1-atpase From Saccharomyces Cerevisiae Inhibited By Its Regulatory Protein If1 |