Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000283032 |
Family | GH17 |
Protein Properties | Length: 571 Molecular Weight: 62828.1 Isoelectric Point: 5.1545 |
Chromosome | Chromosome/Scaffold: 006033315 Start: 5903 End: 10911 |
Description | Glycosyl hydrolase superfamily 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 |
GH17 | 88 | 365 | 0 |
QPFANSEVDFIIGLGNEYLQSMSTDPLKAQSWIQQHVQPHLPQTKITCINVGNEVLGGTDTQLWSYLLPAMQSVYRALVNLGLSKQVAVTTAHSLTILGN SYPPSSGSFRQDLAQYIQPILSFHSQVNSPFLINAYPYFAYKDNPGEVSIEYVLFQPNSGMVDSVTNLHYDNMLDAQIDAVYSAIKVMGHSDIEVRISET GWPSKGDANEAGATPENAGIYNGNLMRKIEEKKGTPAKTQVPIDIYVFALFNEDLKPGPASERNYGLYYPNGTQVYDI |
Full Sequence |
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Protein Sequence Length: 571 Download |
MAASTVLFTI ILLFLGLSVC SVFSPTKHXP IFGYVINLDS PLTNLQWDFL KFKFKCPSPE 60 PELRNQLWTN SQQPPISVAS GRPPPVPQPF ANSEVDFIIG LGNEYLQSMS TDPLKAQSWI 120 QQHVQPHLPQ TKITCINVGN EVLGGTDTQL WSYLLPAMQS VYRALVNLGL SKQVAVTTAH 180 SLTILGNSYP PSSGSFRQDL AQYIQPILSF HSQVNSPFLI NAYPYFAYKD NPGEVSIEYV 240 LFQPNSGMVD SVTNLHYDNM LDAQIDAVYS AIKVMGHSDI EVRISETGWP SKGDANEAGA 300 TPENAGIYNG NLMRKIEEKK GTPAKTQVPI DIYVFALFNE DLKPGPASER NYGLYYPNGT 360 QVYDIGSQGY LPQLTFSADS NINASHIHLQ FSEPSHCVHI IMCLLELIYS VNFLGGVNTD 420 AAWRKETSCA GVGWVARDFA GLLQAAGGSG GRLCHSAEAA EMLAIRNALD FCVRLGFKSV 480 AIESDAKNII QMIRNETTPD CSLECTLGDI ATLARGLESV TFDFVSRESN RAAHSVAKYV 540 FLEGKDFVWD HIGPDFLFNI LAQDVNISIR L |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd09279 | RNase_HI_archaeal_like | 2.0e-5 | 417 | 538 | 123 | + RNAse HI family that includes Archaeal RNase HI. Ribonuclease H (RNase H) is classified into two evolutionarily unrelated families, type 1 (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type 2 (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. RNase H is involved in DNA replication, repair and transcription. RNase H is widely present in various organisms, including bacteria, archaea and eukaryotes and most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, Type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site (DEDD) residues and have the same catalytic mechanism and functions in cells. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. Most archaeal genomes contain only type 2 RNase H (RNase HII); however, a few contain RNase HI as well. Although archaeal RNase HI sequences conserve the DEDD active-site motif, they lack other common features important for catalytic function, such as the basic protrusion region. Archaeal RNase HI homologs are more closely related to retroviral RNase HI than bacterial and eukaryotic type I RNase H in enzymatic properties. | ||
COG5309 | COG5309 | 3.0e-8 | 120 | 358 | 245 | + Exo-beta-1,3-glucanase [Carbohydrate transport and metabolism] | ||
cd06222 | RNase_H | 4.0e-17 | 418 | 539 | 122 | + RNase H is an endonuclease that cleaves the RNA strand of an RNA/DNA hybrid in a sequence non-specific manner. 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. Most prokaryotic and eukaryotic genomes contain multiple RNase H genes. Despite the lack of amino acid sequence homology, Type 1 and type 2 RNase H share a main-chain fold and steric configurations of the four acidic active-site residues and have the same catalytic mechanism and functions in cells. RNase H is involved in DNA replication, repair and transcription. One of the important functions of RNase H is to remove Okazaki fragments during DNA replication. RNase H inhibitors have been explored as an anti-HIV drug target because RNase H inactivation inhibits reverse transcription. | ||
pfam13456 | RVT_3 | 2.0e-17 | 456 | 541 | 86 | + Reverse transcriptase-like. This domain is found in plants and appears to be part of a retrotransposon. | ||
pfam00332 | Glyco_hydro_17 | 3.0e-87 | 84 | 365 | 282 | + 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 |
GenBank | ACU21124.1 | 0 | 84 | 381 | 73 | 369 | unknown [Glycine max] |
EMBL | CAN80621.1 | 0 | 84 | 405 | 135 | 454 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002312820.1 | 0 | 84 | 387 | 63 | 365 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002328249.1 | 0 | 84 | 387 | 65 | 368 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523810.1 | 0 | 84 | 383 | 49 | 347 | 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 | 3f55_D | 0 | 93 | 365 | 47 | 313 | A Chain A, Crystal Structure Of Rice Bglu1 E386a Mutant |
PDB | 3f55_C | 0 | 93 | 365 | 47 | 313 | A Chain A, Crystal Structure Of Rice Bglu1 E386a Mutant |
PDB | 3f55_B | 0 | 93 | 365 | 47 | 313 | A Chain A, Crystal Structure Of Rice Bglu1 E386a Mutant |
PDB | 3f55_A | 0 | 93 | 365 | 47 | 313 | A Chain A, Crystal Structure Of Rice Bglu1 E386a Mutant |
PDB | 3em5_D | 0 | 93 | 365 | 47 | 313 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |