Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000399053 |
Family | CBM43 |
Protein Properties | Length: 582 Molecular Weight: 63138.2 Isoelectric Point: 8.2118 |
Chromosome | Chromosome/Scaffold: 019115100 Start: 342 End: 4667 |
Description | O-Glycosyl hydrolases family 17 protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM43 | 489 | 567 | 1.4e-26 |
WCLPKKGADPEALQKNIDYVCGLGLNCGPIKQGGLCFMPNTVRAHAAYAMNVYFQAMGRKDSDCDFEQTGATTAAMESA | |||
GH17 | 138 | 452 | 0 |
IGVNYGTMASDLPPPAKVAHFLLESTIINRVRLFDTNPDILRAFAHTGIAVTITIPNDQIPHLTKIRSAQQWLKTNVQPHIPATNIVRILVGNEVLSTTN KLFITGLVPAMQALHNALVDASWDRQIKVSTPHSLGILSSSTPPSSGKFRQGYDIHVLKPLLTFLQSTNSPFMVNPYPYFGYSPETLDFALFRPNPGVLD GNTKMLYTNMLDAQLDAVFSAMKLVGFEDLEIVIAETGWPSQGDPAQVGVDAQSAEDYNRNLIQHVTSGYGTPLMPNRTFETFVFSLFNENLKPGPTPER NFGLFRPDMTPTYNV |
Full Sequence |
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Protein Sequence Length: 582 Download |
MDVCYHFVRE IVGEXEIILQ KIPTKDNPAD MLTKVVVAGG VCKSRLKKVK ALSRHVHLTS 60 AARNRTLPSP DSKAKNPKVT SSKPAHQRST LASICTTALQ NTSLLLLMGN FALNFASSRR 120 CILLLLVSIF VQGGEGSIGV NYGTMASDLP PPAKVAHFLL ESTIINRVRL FDTNPDILRA 180 FAHTGIAVTI TIPNDQIPHL TKIRSAQQWL KTNVQPHIPA TNIVRILVGN EVLSTTNKLF 240 ITGLVPAMQA LHNALVDASW DRQIKVSTPH SLGILSSSTP PSSGKFRQGY DIHVLKPLLT 300 FLQSTNSPFM VNPYPYFGYS PETLDFALFR PNPGVLDGNT KMLYTNMLDA QLDAVFSAMK 360 LVGFEDLEIV IAETGWPSQG DPAQVGVDAQ SAEDYNRNLI QHVTSGYGTP LMPNRTFETF 420 VFSLFNENLK PGPTPERNFG LFRPDMTPTY NVGVLRHTAS STTPKNSGPG PVPVLAPASP 480 PQSRGGKLWC LPKKGADPEA LQKNIDYVCG LGLNCGPIKQ GGLCFMPNTV RAHAAYAMNV 540 YFQAMGRKDS DCDFEQTGAT TAAMESASID DEECCNGGED P* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd09272 | RNase_HI_RT_Ty1 | 9.0e-11 | 1 | 36 | 36 | + Ty1/Copia family of RNase HI in long-term repeat retroelements. Ribonuclease H (RNase H) enzymes are divided into two major families, Type 1 and Type 2, based on amino acid sequence similarities and biochemical properties. RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner in the presence of divalent cations. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes. RNase HI has also been observed as adjunct domains to the reverse transcriptase gene in retroviruses, in long-term repeat (LTR)-bearing and non-LTR retrotransposons. RNase HI in LTR retrotransposons perform degradation of the original RNA template, generation of a polypurine tract (the primer for plus-strand DNA synthesis), and final removal of RNA primers from newly synthesized minus and plus strands. The catalytic residues for RNase H enzymatic activity, three aspartatic acids and one glutamatic acid residue (DEDD) are unvaried across all RNase H domains. Phylogenetic patterns of RNase HI of LTR retroelements is classified into five major families, Ty3/Gypsy, Ty1/Copia, Bel/Pao, DIRS1 and the vertebrate retroviruses. Ty1/Copia family is widely distributed among the genomes of plants, fungi and animals. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. | ||
pfam07983 | X8 | 1.0e-20 | 488 | 558 | 76 | + X8 domain. The X8 domain domain contains at least 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is found in an Olive pollen allergen as well as at the C-terminus of several families of glycosyl hydrolases. This domain may be involved in carbohydrate binding. This domain is characteristic of GPI-anchored domains. | ||
smart00768 | X8 | 3.0e-30 | 488 | 563 | 76 | + Possibly involved in carbohydrate binding. The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges. | ||
pfam00332 | Glyco_hydro_17 | 1.0e-93 | 138 | 452 | 321 | + Glycosyl hydrolases family 17. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI23036.1 | 0 | 123 | 561 | 8 | 447 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002271991.1 | 0 | 123 | 561 | 8 | 468 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002318439.1 | 0 | 108 | 561 | 1 | 452 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002321390.1 | 0 | 137 | 561 | 1 | 414 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526252.1 | 0 | 123 | 562 | 16 | 462 | Glucan endo-1,3-beta-glucosidase precursor, putative [Ricinus communis] |
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 | 2cyg_A | 0 | 138 | 452 | 1 | 310 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 1ghs_B | 0 | 138 | 452 | 1 | 304 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1ghs_A | 0 | 138 | 452 | 1 | 304 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 3ur8_B | 0 | 138 | 452 | 3 | 312 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 3ur8_A | 0 | 138 | 452 | 3 | 312 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY278014 | 386 | 121 | 503 | 0 |
DR992247 | 236 | 109 | 344 | 0 |
EG484762 | 298 | 133 | 430 | 0 |
FC903920 | 293 | 121 | 412 | 0 |
EG486112 | 299 | 164 | 462 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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