CAZyme Information: jhhlp_000334-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_000334-t41_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
223		24027.31	4.5418

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000002:612385-613170(+)

Full Sequence      

MTKLFVIPILASLLAWAPAQIAAQGIRGTATFTGRDHTGGTCSLSNYTLPAGISGTGIGP
SNWAQAGKCGSCIQVNGPLGSTKVMIVDSCPSCLENRLNLFDDAFAQIADPVDGIVDVTF
DVVSCGLDSPLIVRNKIGTSRWFFSMQVLNCNFPITDLEVSTDNSQTWESTVRQDYNYFE
REDKTGFGKDEVMIRVSCANGRRVIIPSVSMDSEKEIVAPVNC

Enzyme Prediction     

No EC number prediction in jhhlp_000334-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	133	204	3.5e-19	0.8589743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226755	YoaJ	3.56e-24	4	205	7	207	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409004	DPBB_RlpA_EXP_N-like	6.03e-19	28	122	3	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.
409008	DPBB_EXP_N-like	2.28e-16	28	125	3	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	1.91e-11	28	122	5	101	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.
178595	PLN03024	1.16e-09	1	120	1	123	Putative EG45-like domain containing protein 1; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ58131.1|CBM63	7.52e-62	9	223	11	223
AZA15170.1|CBM63	5.21e-60	28	222	176	369
QMW44202.1|CBM63	7.21e-60	28	222	230	423
BAE62388.1|CBM63	7.21e-60	28	222	230	423
UDD57125.1|CBM63	7.21e-60	28	222	230	423

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3D30_A	7.19e-21	28	204	9	182	Structure of an expansin like protein from Bacillus Subtilis at 1.9A resolution [Bacillus subtilis],4FER_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellohexaose [Bacillus subtilis subsp. subtilis str. 168],4FER_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellohexaose [Bacillus subtilis subsp. subtilis str. 168],4FFT_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with mixed-linkage glucan [Bacillus subtilis subsp. subtilis str. 168],4FFT_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with mixed-linkage glucan [Bacillus subtilis subsp. subtilis str. 168],4FG2_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellotetraose [Bacillus subtilis subsp. subtilis str. 168],4FG2_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with cellotetraose [Bacillus subtilis subsp. subtilis str. 168],4FG4_A Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin [Bacillus subtilis subsp. subtilis str. 168],4FG4_B Crystal structure of Bacillus Subtilis expansin (EXLX1) in complex with hemithiocellodextrin [Bacillus subtilis subsp. subtilis str. 168]
4JS7_A	3.38e-20	40	211	21	186	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]
2BH0_A	7.49e-20	28	204	9	182	Crystal structure of a SeMet derivative of EXPA from Bacillus subtilis at 2.5 angstrom [Bacillus subtilis]
4JCW_A	1.80e-19	40	211	21	186	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O34918|YOAJ_BACSU	2.20e-20	5	204	8	206	Expansin-YoaJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yoaJ PE=1 SV=1
sp|Q54J35|EXPL7_DICDI	1.28e-09	28	174	30	183	Expansin-like protein 7 OS=Dictyostelium discoideum OX=44689 GN=expl7 PE=2 SV=1
sp|Q54PA4|EXPL2_DICDI	1.97e-06	69	179	75	190	Expansin-like protein 2 OS=Dictyostelium discoideum OX=44689 GN=expl2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000246	0.999706	CS pos: 23-24. Pr: 0.9724

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_000334-t41_1-p1.