| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G046436_T01 |
| Family | GT75 |
| Protein Properties | Length: 311 Molecular Weight: 34442.3 Isoelectric Point: 6.6297 |
| Chromosome | Chromosome/Scaffold: 3 Start: 179804578 End: 179807286 |
| Description | reversibly glycosylated polypeptide 1 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT75 | 143 | 263 | 0 |
| EVAKDPSGKDINALEQHIKNLLSPSTPFFFNTLYDPYRVGADFVRGYPYSLREGVPTVVSHGLWLNIPDYDAPTQLLKPLERNTRYVDAILTIPKGTLFP MCGMNLAFDRELIGPAMYFGL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 311 Download |
| MSPTGPPFDS DAPRTTPPKP SSKSALCKWW HSLAPALLAA ALAVTVAALR PTTEHADAKG 60 RPPLWFGPGG VFKVALFADL HYGEDAWTDW GPAQDAASDR VMAAVLDAEN PAIDVQTSLL 120 EEDLNKNYQE DKRQYTPLVK NGEVAKDPSG KDINALEQHI KNLLSPSTPF FFNTLYDPYR 180 VGADFVRGYP YSLREGVPTV VSHGLWLNIP DYDAPTQLLK PLERNTRYVD AILTIPKGTL 240 FPMCGMNLAF DRELIGPAMY FGLWVMASLL DLFCSHLTGL RKLSSRNPNQ RHKRLASLQL 300 WYITFVWDGS * 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd07383 | MPP_Dcr2 | 9.0e-10 | 70 | 111 | 42 | + Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain. DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. | ||
| pfam03214 | RGP | 1.0e-73 | 144 | 263 | 120 | + Reversibly glycosylated polypeptide. | ||
| PLN03180 | PLN03180 | 2.0e-92 | 144 | 263 | 120 | + reversibly glycosylated polypeptide; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005618 | cell wall |
| GO:0007047 | : GO:0044234 |
| GO:0008466 | glycogenin glucosyltransferase activity |
| GO:0016758 | transferase activity, transferring hexosyl groups |
| GO:0030054 | cell junction |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACN27755.1 | 0 | 128 | 263 | 92 | 228 | unknown [Zea mays] |
| GenBank | ACU23018.1 | 0 | 128 | 263 | 94 | 230 | unknown [Glycine max] |
| RefSeq | NP_001148994.1 | 0 | 128 | 263 | 92 | 228 | LOC100282614 [Zea mays] |
| RefSeq | XP_002460988.1 | 0 | 128 | 263 | 92 | 228 | hypothetical protein SORBIDRAFT_02g038770 [Sorghum bicolor] |
| RefSeq | XP_002514626.1 | 0 | 128 | 263 | 93 | 229 | Alpha-1,4-glucan-protein synthase [UDP-forming], putative [Ricinus communis] |
| Hydropathy |
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