CAZyme Information: PTTG_00895-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_00895-t43_1-p1
• CAZy Family: AA9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
255		27290.92	8.4041

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02000052.1:195796-197177(+)

Full Sequence      

MVMIYKAPTASLVLFCFLLFLIPETTAISSGEVHHHPGAATSKLRRRSAPLSETYSGKGT
YHPDDWTSGNCAFIKWPRPQGLGPVAIASNMWNSSQSCGACLEIEGPSGGRFTGIVSNQC
PSCEQNGLDLDVGIWNQVSGNQSPGIISLKWKIVPCGFSKPIIFMNKSGVSQYWTSIQVQ
GANTPLKSLEVSTNGGSSWTALERQSNSNYFQPKDGKGLGTTGDIRVTCLSGKQFVTKNV
DLANPESPKPGSANC

Enzyme Prediction     

No EC number prediction in PTTG_00895-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM63	164	238	2.2e-16	0.8974358974358975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
409004	DPBB_RlpA_EXP_N-like	7.87e-16	55	153	1	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	1.08e-13	48	254	24	225	Peptidoglycan-binding domain, expansin [Cell wall/membrane/envelope biogenesis].
409008	DPBB_EXP_N-like	1.51e-12	55	156	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	4.60e-04	55	153	1	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.
409009	DPBB_EXLX1-like	0.003	54	153	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALL40755.1|CBM63	4.11e-55	52	255	21	228
CAK47858.1|CBM63	7.10e-46	51	247	323	516
BCS00460.1|CBM63	1.86e-44	55	247	323	512
BCS12235.1|CBM63	1.86e-44	55	247	323	512
UPL03539.1|CBM63	4.82e-43	52	252	21	217

PDB Hits     

PTTG_00895-t43_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q54PA4|EXPL2_DICDI	2.24e-06	47	205	22	185	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
0.000251	0.999739	CS pos: 27-28. Pr: 0.9757

TMHMM  Annotations     

There is no transmembrane helices in PTTG_00895-t43_1-p1.