Species | RUG572 sp900547945 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; RUG572; RUG572 sp900547945 | |||||||||||
CAZyme ID | MGYG000003483_01892 | |||||||||||
CAZy Family | GH163 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 206; End: 2605 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH163 | 229 | 487 | 2.2e-91 | 0.9920318725099602 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam16126 | DUF4838 | 3.14e-115 | 223 | 487 | 2 | 262 | Domain of unknown function (DUF4838). This family consists of several uncharacterized proteins found in various Bacteroides and Chloroflexus species. The function of this family is unknown. |
pfam03648 | Glyco_hydro_67N | 7.38e-08 | 49 | 138 | 28 | 120 | Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQL44163.1 | 2.55e-237 | 29 | 776 | 9 | 750 |
ASV73444.1 | 1.34e-133 | 25 | 567 | 21 | 553 |
AXE18406.1 | 1.38e-106 | 41 | 560 | 310 | 810 |
AIE83908.1 | 1.26e-105 | 38 | 558 | 18 | 514 |
AIF26900.1 | 2.36e-103 | 107 | 561 | 79 | 542 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.005139 | 0.327299 | 0.666805 | 0.000323 | 0.000207 | 0.000216 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.