CAZyme Information: EEU42231.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU42231.1
• CAZy Family: GH43|CBM91
• CAZyme Description: Expansin-like EG45 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C7Z0N0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
282	GG698905|CGC1	29439.22	5.7061

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698905:330535-331547(+)

Full Sequence      

MKFLLPILLAAPAVMGRACKSAPNLLPSRSPITTTAPSFPPSSSLLPTSKTALSSQTLPP
RPPLSPLWLPPPPAPAPSRRLDLGGSAKTGSSTFYGGNLAGGNCMFSTYTLPSGIYGTAF
SGAVWNNAASCGACIEVTGPSGTIKAMIVDQCPECEEGHLDLFPDAFTAVGGTDGIVQTS
YKFVSCGITSPLYLHNKEGTSQHWFSIQVVNANEPVTKLEVSTDGGSTWQETERKDYNFF
ENSAGFGVDSVDVKITSKTGKTVTVSGVGVEAGAKYDADSNF

Enzyme Prediction     

No EC number prediction in EEU42231.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	195	264	7.3e-24	0.8589743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409004	DPBB_RlpA_EXP_N-like	1.04e-26	89	183	2	94	double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains. The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), and the N-terminal domain of plant and bacterial expansins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs.
226755	YoaJ	1.77e-22	85	263	28	206	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409008	DPBB_EXP_N-like	1.61e-21	89	186	2	117	N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains. The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold.
409009	DPBB_EXLX1-like	2.00e-12	89	171	4	88	N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus subtilis EXLX1. This subfamily is composed of bacterial expansins including Bacillus subtilis EXLX1, also called expansin-YoaJ. Similar to plant expansins, EXLX1 contains an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. It strongly binds to crystalline cellulose via D2, and weakly binds soluble cellooligosaccharides. Bacterial expansins, which are present in some plant pathogens, have the ability to loosen plant cell walls, but with weaker activity compared to plant expansins. They may have a role in plant-bacterial interactions. This model represents the N-terminal domain of EXLX1 and similar bacterial expansins, which adopts a double-psi beta-barrel (DPBB) fold.
409006	DPBB_EG45-like	3.11e-08	109	181	20	104	double-psi beta-barrel fold of EG45-like domain-containing proteins. This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL00742.1|CBM63	3.98e-136	93	282	131	320
QGI84616.1|CBM63	1.07e-114	85	282	134	331
QGI98272.1|CBM63	1.07e-114	85	282	134	331
QGI67389.1|CBM63	1.07e-114	85	282	134	331
CCT71632.1|CBM63	1.35e-114	85	282	141	338

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JCW_A	2.32e-28	90	282	5	198	Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JCW_B Crystal structure of Clavibacter michiganensis expansin in complex with cellopentaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4JJO_A crystal structure of apo-clavibacter Michiganensis expansin [Clavibacter michiganensis]
4JS7_A	1.25e-27	90	282	5	198	Crystal structure of D78N mutant apo form of clavibacter michiganensis expansin [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_A Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382],4L48_C Crystal structure of d78n mutant clavibacter michiganensis expansin in complex with cellohexaose [Clavibacter michiganensis subsp. michiganensis NCPPB 382]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q54PA4|EXPL2_DICDI	2.55e-21	102	260	43	222	Expansin-like protein 2 OS=Dictyostelium discoideum OX=44689 GN=expl2 PE=3 SV=1
sp|Q4PNY1|EXP11_ORYSJ	9.02e-10	89	268	29	232	Expansin-A11 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA11 PE=2 SV=2
sp|Q2QP13|EXP26_ORYSJ	8.45e-08	90	255	85	260	Expansin-A26 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA26 PE=2 SV=1
sp|A2Y5R6|EXPA4_ORYSI	5.63e-06	85	268	22	230	Expansin-A4 OS=Oryza sativa subsp. indica OX=39946 GN=EXPA4 PE=2 SV=1
sp|Q0DHB7|EXPA4_ORYSJ	5.63e-06	85	268	22	230	Expansin-A4 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA4 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.055416	0.944562	CS pos: 16-17. Pr: 0.8857

TMHMM  Annotations     

There is no transmembrane helices in EEU42231.1.