CAZyme Information: OTA33807.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA33807.1
• CAZy Family: GH47
• CAZyme Description: Expansin-like EG45 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1Z5TCM8]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
236	MUNK01000069|CGC3	25224.27	6.0839

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

• Gene Location: location=MUNK01000069:142194-142966(+)

Full Sequence      

MYAKAAAFMAFASSAFAAVTPGMTLDERSLAKRSLSGEATFYGGNVQGGTCSFSTYSLPE
GLYGTALSDSNWNNAYNCGGCVRVNHGGKSVTAMIVDQCPGCGDNHLDLFPDAFKALEDP
SVGVMDITWDYVSCPTDIIPVSEPLSIHMKSGVSQYWFSAQVVGARRRTAKLEVSTDQGN
TWQEAKRTTYNFFEISSGVGASSAWIRATSHVGTTVLVKDVQMTGDSVTKGPKNYV

Enzyme Prediction     

No EC number prediction in OTA33807.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	147	217	1.3e-18	0.8717948717948718

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409004	DPBB_RlpA_EXP_N-like	1.52e-34	36	131	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.
409008	DPBB_EXP_N-like	5.06e-24	35	134	1	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.
409010	DPBB_SPI-like	2.55e-18	36	131	2	101	double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins. Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.
226755	YoaJ	4.35e-11	34	216	30	206	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409009	DPBB_EXLX1-like	9.40e-10	36	129	4	99	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA07190.1|CBM63	1.97e-76	13	224	11	213
CCD54783.1|CBM63	6.46e-75	30	221	23	209
ATZ45466.1|CBM63	6.46e-75	30	221	23	209
UJO13329.1|CBM63	2.11e-70	51	235	2	182
CBY01027.1|CBM63	8.71e-68	35	235	182	378

PDB Hits     

OTA33807.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4PNY1|EXP11_ORYSJ	1.11e-06	36	134	29	151	Expansin-A11 OS=Oryza sativa subsp. japonica OX=39947 GN=EXPA11 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002880	0.997113	CS pos: 17-18. Pr: 0.8974

TMHMM  Annotations     

There is no transmembrane helices in OTA33807.1.