Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 409562 |
Family | GH18 |
Protein Properties | Length: 650 Molecular Weight: 68842.4 Isoelectric Point: 7.1721 |
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 |
GH18 | 377 | 598 | 5.2e-26 |
IVSYWGQFGQEGPLDKVCASGNYEIINIAFLNEFGNFRQPVLNLAGHCDATTSDGCAAVGGQIKSCQSMGVKVLLSIGGASGSALLVSEADAANLAHQLF DSFLGGESSYKPLGDAVLDGIDLDIESGKTPKLYASMVRHLRTIAGRSKIIVAAAPQCPFPDENLGSALKVPGLFDLIFVQFYNNPPCAFDGSDSKKLLD SWKQWTSSIPMAKFYLGLPASR | |||
GH18 | 48 | 270 | 7.8e-28 |
KIAAYWGQHDGEDDLDQVCSSGKYKIVMLAFLASFGNFLDPVLNLANHCDPSNGGCKAYSSKIKACQAKGVQIILSIGGGASGGYLVSDADARDFAEKLW NSYLGGHSSDRPLGSAVLNGIDLDIEGGGIPDRYGVMVKSLRSLAHGSGKKKLVVTAAPQCPFPDLNLGTAIQIPGLFDYLFVQFYNNPCGYGGGGAENL LDSWKQWTTAIPTAKIFLGLPAS |
Full Sequence |
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Protein Sequence Length: 650 Download |
MAAPFPLLAA VLFVFGAAAA AAACETPSPA PAPSPDADLP DYPSGRGKIA AYWGQHDGED 60 DLDQVCSSGK YKIVMLAFLA SFGNFLDPVL NLANHCDPSN GGCKAYSSKI KACQAKGVQI 120 ILSIGGGASG GYLVSDADAR DFAEKLWNSY LGGHSSDRPL GSAVLNGIDL DIEGGGIPDR 180 YGVMVKSLRS LAHGSGKKKL VVTAAPQCPF PDLNLGTAIQ IPGLFDYLFV QFYNNPCGYG 240 GGGAENLLDS WKQWTTAIPT AKIFLGLPAS PSAAGSGFLP PNVCKSSVLP EIKRSKNYGG 300 VMFWSVYYDQ QEQYSEAIRS TIQVHCCLEH ALYLIKQEHD KRKWSPRNGL KFLAAAATIA 360 AASSPRRLRS KSRDGGIVSY WGQFGQEGPL DKVCASGNYE IINIAFLNEF GNFRQPVLNL 420 AGHCDATTSD GCAAVGGQIK SCQSMGVKVL LSIGGASGSA LLVSEADAAN LAHQLFDSFL 480 GGESSYKPLG DAVLDGIDLD IESGKTPKLY ASMVRHLRTI AGRSKIIVAA APQCPFPDEN 540 LGSALKVPGL FDLIFVQFYN NPPCAFDGSD SKKLLDSWKQ WTSSIPMAKF YLGLPASRAA 600 AGSGFLPANV ARSSVLPVIK STRNYGGIML WAVFFDQQES YSDSILSSV* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd02871 | GH18_chitinase_D-like | 5.0e-18 | 376 | 642 | 317 | + GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus. | ||
pfam00704 | Glyco_hydro_18 | 9.0e-19 | 47 | 309 | 342 | + Glycosyl hydrolases family 18. | ||
pfam00704 | Glyco_hydro_18 | 2.0e-22 | 375 | 597 | 247 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 1.0e-102 | 47 | 320 | 282 | + This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. | ||
cd02877 | GH18_hevamine_XipI_class_III | 1.0e-106 | 375 | 645 | 280 | + This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAC55717.1 | 0 | 44 | 322 | 23 | 297 | putative class III acidic chitinase [Oryza sativa Japonica Group] |
DDBJ | BAC55717.1 | 0 | 372 | 649 | 23 | 297 | putative class III acidic chitinase [Oryza sativa Japonica Group] |
RefSeq | XP_002461857.1 | 0 | 44 | 322 | 23 | 300 | hypothetical protein SORBIDRAFT_02g009390 [Sorghum bicolor] |
RefSeq | XP_002461857.1 | 0 | 372 | 649 | 23 | 300 | hypothetical protein SORBIDRAFT_02g009390 [Sorghum bicolor] |
RefSeq | XP_002513612.1 | 0 | 373 | 649 | 23 | 297 | hevamine-A 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 | 2hvm_A | 0 | 375 | 649 | 1 | 273 | A Chain A, Crystal Structure Of Aquifex Aeolicus Lpxc Complexed With Imidazole. |
PDB | 2hvm_A | 0 | 47 | 322 | 1 | 273 | A Chain A, Crystal Structure Of Aquifex Aeolicus Lpxc Complexed With Imidazole. |
PDB | 1llo_A | 0 | 375 | 649 | 1 | 273 | A Chain A, Crystal Structure Of Aquifex Aeolicus Lpxc Complexed With Imidazole. |
PDB | 1llo_A | 0 | 47 | 322 | 1 | 273 | A Chain A, Crystal Structure Of Aquifex Aeolicus Lpxc Complexed With Imidazole. |
PDB | 1hvq_A | 0 | 375 | 649 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
chitin degradation II | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12623 | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12624 | EC-3.2.1.14 | chitinase |
chitin degradation III (carnivorous plants) | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |