CAZyme Information: CDH58828.1

Basic Information

• Species: Lichtheimia corymbifera
• Lineage: Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
• CAZyme ID: CDH58828.1
• CAZy Family: GT39
• CAZyme Description: lysophospholipase a

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
548		61487.78	5.9762

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LcorymbiferaJMRCFSU9682	12379	1263082	97	12282

• Gene Location: location=CBTN010000061:105285-108320(+)

Full Sequence      

MKTAFASTLALGVLASLATAAPTQHNKKGHSFCWHRTDTVIIINSFVFGDSYSNLMGGGG
TVDHTWSNFSSNAQIYDNPIIENKTSSGGLDWNQYLTGCHEGLPQKCDPQLWNFAYSGAV
IDNDAIDNHEPDSVSFVEQIDRWINKLNPTLKWNPASSLGIFFIGLNDVYYTAPMKNVTA
SLYDEIQDTYFEKMHEMYLHNLRSFMFFNVPSWTRTPYGLENPDIPNDKWASIYNHKLVE
RMEKFQKAHKDAHVLYFDTRTHMDYYIDHYDRYGFENITTFCPNNTAADIHTNYADYGCL
PMEKEREKQNRLSLTHTLDLFPFTHTSYSMNEADPHFEHNPRHSSGTRLSMPVAAQVPTT
TSTIPATQAYNQLDNELPSTIWTRIIDRFRYGKLMLVGSGFVGVLAVMFIVLGSLDVFHN
NRYRSALGLGPSSGDHSKFEGDSWGSVSADHFDLHGKGDGTYYDPGVGILSCGTRFTAQD
NVVALNHVDYGSYVNPNESPVCGACIKITGPLGSVKATIQDMCPQCGQGKLITRGMGYFE
DAFANMMD

Enzyme Prediction     

No EC number prediction in CDH58828.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE16	47	287	8.7e-45	0.8838951310861424

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
238882	fatty_acyltransferase_like	2.12e-31	46	284	3	230	Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Might catalyze fatty acid transfer between phosphatidylcholine and sterols.
409004	DPBB_RlpA_EXP_N-like	1.36e-20	458	531	3	70	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.
238875	SGNH_plant_lipase_like	1.58e-11	113	282	79	265	SGNH_plant_lipase_like, a plant specific subfamily of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
409010	DPBB_SPI-like	1.76e-09	456	527	1	72	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.
395531	Lipase_GDSL	1.99e-06	46	272	2	202	GDSL-like Lipase/Acylhydrolase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS10839.1|CE16	2.87e-211	1	304	1	300
ATZ57303.1|CE0	2.89e-44	10	302	6	309
APA16273.1|CE0	5.52e-43	13	302	10	308
CDS06767.1|CE16	1.71e-40	30	313	45	334
CDS12816.1|CE16	3.88e-40	15	169	19	165

PDB Hits     

CDH58828.1 has no PDB hit.

Swiss-Prot Hits     

CDH58828.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000201	0.999768	CS pos: 20-21. Pr: 0.9850

TMHMM  Annotations     

Start	End
396	418