y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma06g47750.1 |
Family | GH5 |
Protein Properties | Length: 500 Molecular Weight: 56237.9 Isoelectric Point: 5.4904 |
Chromosome | Chromosome/Scaffold: 06 Start: 50154436 End: 50158689 |
Description | |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH5 | 218 | 480 | 0 |
MRDHWSTYITEDDFRFMSENGLNAVRIPVGWWIAKGPNPPKPFVGGSLAALDNAFIWAQNHGMKVIIDLHAAEGSQNGNDHSGTRDGYTEWGDSYIPNTV QVIDFLAERYGNRPNLGGIELMNEPQGVNLESLKKYYKEAYDAVRKHNPSAYVIMSNPLDADSKVLLSFVKGFDRVVIDVHYYNLYSSKFNNMTAQQNID YIRNERASDLSGVSSSNALSFVGEWTGAWSIKGASKEDLKRYAQAQLDVYSRATFGWAYWSYK |
Full Sequence |
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Protein Sequence Length: 500 Download |
MGYLYFLSFL FALCLSSPHN VLFAQNLPYK VVNLGNWLVV EGWMQEPSLF DGIVSKDLLD 60 GTQVQLKSTK FNKYLTSENG GGADVVANRD SASGWETFKL WRISDSSFNL RVFNKKFVGL 120 ENHGGGNKIE AVSDSPNNPE TFEIIRDDND PFKIRIKASN GHFLQVGSET SVTADYEGTN 180 WDESDPSVFR MNIVPGTTLQ GEYQLTNGYG PNRAPQIMRD HWSTYITEDD FRFMSENGLN 240 AVRIPVGWWI AKGPNPPKPF VGGSLAALDN AFIWAQNHGM KVIIDLHAAE GSQNGNDHSG 300 TRDGYTEWGD SYIPNTVQVI DFLAERYGNR PNLGGIELMN EPQGVNLESL KKYYKEAYDA 360 VRKHNPSAYV IMSNPLDADS KVLLSFVKGF DRVVIDVHYY NLYSSKFNNM TAQQNIDYIR 420 NERASDLSGV SSSNALSFVG EWTGAWSIKG ASKEDLKRYA QAQLDVYSRA TFGWAYWSYK 480 CRYMEWSLKS MIENGYIKL* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00257 | Fascin | 9.0e-5 | 108 | 177 | 70 | + Fascin-like domain; members include actin-bundling/crosslinking proteins facsin, histoactophilin and singed; identified in sea urchin, Drosophila, Xenopus, rodents, and humans; The fascin-like domain adopts a beta-trefoil topology and contains an internal threefold repeat; the fascin subgroup contains four copies of the domain; Structurally similar to fibroblast growth factor (FGF) | ||
pfam06268 | Fascin | 4.0e-5 | 72 | 183 | 113 | + Fascin domain. This family consists of several eukaryotic fascin or singed proteins. The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture. Dictyostelium hisactophilin, another actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerisation and binding to microfilaments only at pH values below seven. Members of this family are histidine rich, typically contain the repeated motif of HHXH. | ||
cd00257 | Fascin | 3.0e-7 | 62 | 164 | 104 | + Fascin-like domain; members include actin-bundling/crosslinking proteins facsin, histoactophilin and singed; identified in sea urchin, Drosophila, Xenopus, rodents, and humans; The fascin-like domain adopts a beta-trefoil topology and contains an internal threefold repeat; the fascin subgroup contains four copies of the domain; Structurally similar to fibroblast growth factor (FGF) | ||
pfam00150 | Cellulase | 7.0e-25 | 221 | 479 | 270 | + Cellulase (glycosyl hydrolase family 5). | ||
COG2730 | BglC | 3.0e-29 | 194 | 480 | 328 | + Endoglucanase [Carbohydrate transport and metabolism] |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0030674 | protein binding, bridging |
GO:0051015 | actin filament binding |
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 | ADD09589.1 | 0 | 4 | 499 | 5 | 504 | unknown [Trifolium repens] |
EMBL | CAN74231.1 | 0 | 27 | 499 | 141 | 607 | hypothetical protein [Vitis vinifera] |
EMBL | CBI18831.1 | 0 | 27 | 499 | 33 | 505 | unnamed protein product [Vitis vinifera] |
EMBL | CBI33033.1 | 0 | 11 | 499 | 13 | 505 | unnamed protein product [Vitis vinifera] |
EMBL | CBI33035.1 | 0 | 9 | 480 | 14 | 486 | unnamed protein product [Vitis vinifera] |
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 | 3o6a_A | 1e-36 | 202 | 495 | 50 | 381 | A Chain A, F144yF258Y DOUBLE MUTANT OF EXO-Beta-1,3-Glucanase From Candida Albicans At 2 A |
PDB | 1eqp_A | 2e-36 | 202 | 495 | 45 | 376 | A Chain A, Exo-B-(1,3)-Glucanase From Candida Albicans |
PDB | 3n9k_A | 2e-36 | 202 | 495 | 50 | 381 | A Chain A, F229aE292S DOUBLE MUTANT OF EXO-Beta-1,3-Glucanase From Candida Albicans In Complex With Laminaritriose At 1.7 A |
PDB | 2pc8_A | 2e-36 | 202 | 495 | 51 | 382 | A Chain A, E292q Mutant Of Exo-B-(1,3)-Glucanase From Candida Albicans In Complex With Two Separately Bound Glucopyranoside Units At 1.8 A |
PDB | 2pbo_A | 2e-36 | 202 | 495 | 51 | 382 | A Chain A, E27q Mutant Of Exo-B-(1,3)-Glucanase From Candida Albicans At 1.85 A |