| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000307326 |
| Family | AA5 |
| Protein Properties | Length: 1090 Molecular Weight: 122157 Isoelectric Point: 9.3381 |
| Chromosome | Chromosome/Scaffold: 017057193 Start: 7262 End: 12748 |
| Description | RING domain ligase2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA5 | 409 | 1087 | 0 |
| STSDNNVCPICLTDPKNMAFGCGHQELSPLYISSLLLDEGCRHLEILVGLGXPQLELLLWRLLCLNFCFMSLFSRLLITTFVQLNSTYNXLYASYMYTRH FVISKXLLISYGMSFRDQLMNRRHVVSMSNTNIKMTCRAPTDAGICGTVAGSRKGQWQQLLNNTGVVAMHMALTHHNTVIMFDQTEAGPSGYRLRTRHNG NRCTDNRDDVADSSCYAHSVEYDISSNKVRPLRLYTDTWCSSGSFLSNGTLLQTGGYGSGTRRIRYYRPCGNGKCNWRQSERSLSKDRWYASNQLLPEHD RVIVVGGRRTFTYEFVPKMSSNEGSHELSFLHQTYDPNEGGNNLYPFLHLSSDGNLFIFANRNSILFDYERNRVIKTFPRIPGDGSRNYPGSGSSVILPL DHANRFEKVEVMVCGGAASGAYRATRQNRFLKGLSSCGRMVITGNRHKWNMENMPGPRLLNDMLILPTGNVLIINGAKRGSGGWNNARNASLRPYLYKPN XKLGKRFSVLKSTKIARMYHSSAVLLPDGRVLVGGGNPHDRYTFSNVAYPTELRLQAFVPHYMRRKYHTHRPTNVTIQYGQNNYNGVRYGEEFNVTFLLE RKPSDVVEFTAYSPPFTTHSISMNQRLLKLRCKSLVRAQXGLVHAVVEAPPSANVAPSGYYMLTVVNGGTPSMSEWVRF | |||
| Full Sequence |
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| Protein Sequence Length: 1090 Download |
| MGGKSSKRST SRHPSFGTAS RSWSHQSYQE APYAQPPLIP SYAPPSQDYR PQQYYAPPPQ 60 SHGSAWPTGS NTGSGTKFGR INDDYNSLDQ VTDALARAGL ESSNLIVGID FTKSNEWTGA 120 RSFHRKSLHH IGEEQNPYEQ GIAIIGKTLS SFDEDNLIPC FGFGDASTHD QEVFSFYPDE 180 GSYCNGFEEV LRRYRELVPQ LRLAGPTSFA PIIEMGITIV EQSGGQYHVL VIIADGQVTR 240 SVDTGRGQLS PQERKTVEAI VKASEYPLSI ILVGVGDGPW DMMKEFDDNI PARTFDNFQA 300 SIFRDRGYHL DRFVNFTEIM AKNMDRSRKE AEFALAALME IPSQYKATLE LNILGATRGK 360 AIDRVPLPPP HYGSSSFSSP KTSRSSSFRP SAPSRQRDEF VSTAHPAGST SDNNVCPICL 420 TDPKNMAFGC GHQELSPLYI SSLLLDEGCR HLEILVGLGX PQLELLLWRL LCLNFCFMSL 480 FSRLLITTFV QLNSTYNXLY ASYMYTRHFV ISKXLLISYG MSFRDQLMNR RHVVSMSNTN 540 IKMTCRAPTD AGICGTVAGS RKGQWQQLLN NTGVVAMHMA LTHHNTVIMF DQTEAGPSGY 600 RLRTRHNGNR CTDNRDDVAD SSCYAHSVEY DISSNKVRPL RLYTDTWCSS GSFLSNGTLL 660 QTGGYGSGTR RIRYYRPCGN GKCNWRQSER SLSKDRWYAS NQLLPEHDRV IVVGGRRTFT 720 YEFVPKMSSN EGSHELSFLH QTYDPNEGGN NLYPFLHLSS DGNLFIFANR NSILFDYERN 780 RVIKTFPRIP GDGSRNYPGS GSSVILPLDH ANRFEKVEVM VCGGAASGAY RATRQNRFLK 840 GLSSCGRMVI TGNRHKWNME NMPGPRLLND MLILPTGNVL IINGAKRGSG GWNNARNASL 900 RPYLYKPNXK LGKRFSVLKS TKIARMYHSS AVLLPDGRVL VGGGNPHDRY TFSNVAYPTE 960 LRLQAFVPHY MRRKYHTHRP TNVTIQYGQN NYNGVRYGEE FNVTFLLERK PSDVVEFTAY 1020 SPPFTTHSIS MNQRLLKLRC KSLVRAQXGL VHAVVEAPPS ANVAPSGYYM LTVVNGGTPS 1080 MSEWVRFMHH 1140 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam09118 | DUF1929 | 5.0e-20 | 979 | 1086 | 109 | + Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase. | ||
| cd02851 | E_set_GO_C | 8.0e-27 | 979 | 1086 | 109 | + C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. | ||
| pfam07002 | Copine | 5.0e-62 | 127 | 276 | 159 | + Copine. This family represents a conserved region approximately 180 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth. | ||
| cd01459 | vWA_copine_like | 6.0e-96 | 81 | 345 | 287 | + VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding. | ||
| pfam07250 | Glyoxal_oxid_N | 1.0e-99 | 577 | 824 | 250 | + Glyoxal oxidase N-terminus. This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACU22839.1 | 0 | 1 | 443 | 1 | 420 | unknown [Glycine max] |
| RefSeq | XP_002276473.1 | 0 | 552 | 1089 | 31 | 571 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279018.1 | 0 | 1 | 433 | 1 | 407 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002318092.1 | 0 | 28 | 433 | 34 | 416 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002511290.1 | 0 | 1 | 433 | 1 | 407 | copine, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1k3i_A | 0.0000002 | 866 | 1089 | 456 | 656 | A Chain A, Crystal Structure Of The Precursor Of Galactose Oxidase |
| PDB | 2eid_A | 0.0000002 | 866 | 1089 | 439 | 639 | A Chain A, Galactose Oxidase W290g Mutant |
| PDB | 2eic_A | 0.0000002 | 866 | 1089 | 439 | 639 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vz3_A | 0.0000002 | 866 | 1089 | 439 | 639 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vz1_A | 0.0000002 | 866 | 1089 | 439 | 639 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CK272515 | 297 | 77 | 373 | 0 |
| DY264397 | 339 | 1 | 330 | 0 |
| BM112278 | 259 | 98 | 356 | 0 |
| EB110104 | 213 | 661 | 873 | 0 |
| DY264397 | 45 | 329 | 373 | 3.3 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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