y
Basic Information | |
---|---|
Species | Medicago truncatula |
Cazyme ID | Medtr7g116350.1 |
Family | GH18 |
Protein Properties | Length: 856 Molecular Weight: 94441.9 Isoelectric Point: 8.1332 |
Chromosome | Chromosome/Scaffold: 7 Start: 37739285 End: 37744889 |
Description | MAC/Perforin domain-containing protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH18 | 30 | 273 | 5.9e-29 |
IYWGQNGNEGTLAKTCATGNYEYVNIAFLYTFGNGRVPRMDLAGHCDSCQSKGIKVILSIGGGAGSYSLASLEDARIVATYLWNNFLGGHSATRPLGDAV LDGIDFDIEGGTNLHWDDLAKYLSGYSKKGKKVYLTAAPQCPFPDAMLGEALKTGLFDYVWVQFYNNPPCQHSSADVGNLENAWKEWINDIPATKIFLGL PASPQAAGSGFVSVADLTSKVLPIIKGSTKYGGVMLWSKYYDDQ |
Full Sequence |
---|
Protein Sequence Length: 856 Download |
MTSYKLGTLI IFSLVILILA RGSNGGGISI YWGQNGNEGT LAKTCATGNY EYVNIAFLYT 60 FGNGRVPRMD LAGHCDSCQS KGIKVILSIG GGAGSYSLAS LEDARIVATY LWNNFLGGHS 120 ATRPLGDAVL DGIDFDIEGG TNLHWDDLAK YLSGYSKKGK KVYLTAAPQC PFPDAMLGEA 180 LKTGLFDYVW VQFYNNPPCQ HSSADVGNLE NAWKEWINDI PATKIFLGLP ASPQAAGSGF 240 VSVADLTSKV LPIIKGSTKY GGVMLWSKYY DDQTGYSSSI KTSLQHLFFF LVVLCGQTPE 300 EFNLHSCNIF CGLSNGFNVN NTNSYGNAWL DPQLAAEKAV SEIGQGYNLC NDIRFSACKP 360 RLIHIDNSSS NTRDLVFPSG VVVPNVPLSI KSDKGDCTRF RSDVLTFNQT IIFVALSGKI 420 PSGQFNSMFD MKKCWSRDAA STKSLAFDGW FITLYTVELD RTNTTLSETE KRRALFVEPR 480 CSCRYGTHVV VGVKMGGKDV VHIKQSKDSD IPPTELQKLL KQLADERFSA DSNQSSNVNP 540 VAISGKLKLR GLHKNKPPSL VGRPIVESHS KNDDIVSISV RRGGIDVCQP YNQWLSTISQ 600 SSNVSYQYLW YKPAIEELHQ FLEFQLPRQC YKRNASPSLQ FTLMGPKLYV NTVKVDSGNR 660 PVIIVIHSYL EGKKNNHLSI HLQHLSEVPG VLEISEDHSY DPIDEPDDRG YCEPVKRSMF 720 YHSTSIVTKA WFEVKLMGMK KVLFLRLGYS TVASAKIPLM SAKLSQELHS PEKQYKVDIN 780 SAIYHGGPPV PTRAPKMLNF VDTEEMVRGP EGRACPEDPP GYWVVTGAKL CVEGGRISIK 840 AKYSLLTILS EESIM* 900 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01823 | MACPF | 0.0005 | 425 | 599 | 198 | + MAC/Perforin domain. The membrane-attack complex (MAC) of the complement system forms transmembrane channels. These channels disrupt the phospholipid bilayer of target cells, leading to cell lysis and death. A number of proteins participate in the assembly of the MAC. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-7 complex. The C5b-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-8 complex. C5b-8 subsequently binds to C9 and acts as a catalyst in the polymerisation of C9. Active MAC has a subunit composition of C5b-C6-C7-C8-C9{n}. Perforin is a protein found in cytolytic T-cell and killer cells. In the presence of calcium, perforin polymerises into transmembrane tubules and is capable of lysing, non-specifically, a variety of target cells. There are a number of regions of similarity in the sequences of complement components C6, C7, C8-alpha, C8-beta, C9 and perforin. The X-ray crystal structure of a MACPF domain reveals that it shares a common fold with bacterial cholesterol dependent cytolysins (pfam01289) such as perfringolysin O. Three key pieces of evidence suggests that MACPF domains and CDCs are homologous: Functional similarity (pore formation), conservation of three glycine residues at a hinge in both families and conservation of a complex core fold. | ||
COG3469 | COG3469 | 7.0e-7 | 131 | 274 | 175 | + Chitinase [Carbohydrate transport and metabolism] | ||
cd02871 | GH18_chitinase_D-like | 3.0e-7 | 130 | 279 | 196 | + 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 | 4.0e-14 | 26 | 271 | 334 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 2.0e-110 | 26 | 281 | 279 | + 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. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAN74094.1 | 0 | 330 | 855 | 239 | 842 | hypothetical protein [Vitis vinifera] |
EMBL | CBI30600.1 | 0 | 330 | 855 | 8 | 611 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002273740.1 | 0 | 330 | 855 | 8 | 601 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305779.1 | 0 | 327 | 855 | 3 | 603 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509441.1 | 0 | 330 | 855 | 6 | 597 | conserved hypothetical protein [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2hvm_A | 0 | 26 | 284 | 1 | 273 | A Chain A, Pectin Methylesterase From Yersinia Enterocolitica |
PDB | 1llo_A | 0 | 26 | 284 | 1 | 273 | A Chain A, Pectin Methylesterase From Yersinia Enterocolitica |
PDB | 1hvq_A | 0 | 26 | 284 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
PDB | 1kr0_A | 0 | 26 | 284 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
PDB | 1kr1_A | 0 | 26 | 284 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |