Species | Pythium aphanidermatum | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum | |||||||||||
CAZyme ID | EPrPAT00000018350-p1 | |||||||||||
CAZy Family | PL3 | |||||||||||
CAZyme Description | Cellulose synthase 2. | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 2.4.1.12:3 |
---|
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
133043 | CESA_CelA_like | 4.47e-41 | 341 | 722 | 1 | 234 | CESA_CelA_like are involved in the elongation of the glucan chain of cellulose. Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end. |
236918 | bcsA | 2.48e-18 | 299 | 807 | 223 | 569 | cellulose synthase catalytic subunit; Provisional |
133057 | CESA_NdvC_like | 1.52e-11 | 585 | 724 | 102 | 234 | NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response. |
275388 | PH | 8.41e-11 | 73 | 176 | 2 | 92 | Pleckstrin homology (PH) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. |
214574 | PH | 2.10e-10 | 73 | 180 | 4 | 101 | Pleckstrin homology domain. Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 971 | 1 | 1025 | |
0.0 | 6 | 971 | 13 | 1026 | |
0.0 | 6 | 971 | 4 | 1019 | |
0.0 | 6 | 971 | 13 | 1026 | |
0.0 | 6 | 971 | 13 | 1028 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.68e-16 | 288 | 801 | 79 | 441 | Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1] |
|
1.84e-16 | 288 | 801 | 91 | 453 | Chain A, Cellulose Synthase Subunit A [Cereibacter sphaeroides] |
|
1.84e-16 | 288 | 801 | 92 | 454 | Chain A, Cellulose Synthase A subunit [Cereibacter sphaeroides 2.4.1],4P02_A Chain A, Cellulose Synthase subunit A [Cereibacter sphaeroides 2.4.1],5EIY_A Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1],5EJZ_A Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1] |
|
2.32e-15 | 299 | 929 | 236 | 692 | Chain A, Cellulose synthase catalytic subunit [UDP-forming] [Escherichia coli K-12] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.33e-18 | 588 | 835 | 642 | 878 | Cellulose synthase catalytic subunit A [UDP-forming] OS=Dictyostelium discoideum OX=44689 GN=dcsA PE=1 SV=1 |
|
1.18e-14 | 299 | 929 | 236 | 692 | Cellulose synthase catalytic subunit [UDP-forming] OS=Escherichia coli (strain K12) OX=83333 GN=bcsA PE=1 SV=3 |
|
1.55e-14 | 299 | 929 | 236 | 692 | Cellulose synthase catalytic subunit [UDP-forming] OS=Escherichia coli O157:H7 OX=83334 GN=bcsA PE=3 SV=2 |
|
6.10e-14 | 299 | 929 | 236 | 692 | Cellulose synthase catalytic subunit [UDP-forming] OS=Salmonella typhi OX=90370 GN=bcsA PE=3 SV=1 |
|
6.10e-14 | 299 | 929 | 236 | 692 | Cellulose synthase catalytic subunit [UDP-forming] OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=bcsA PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000050 | 0.000000 |
Start | End |
---|---|
209 | 231 |
293 | 315 |
755 | 777 |
792 | 814 |
869 | 891 |
901 | 923 |
944 | 963 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.