CAZyme Information: CDH57732.1

Basic Information

• Species: Lichtheimia corymbifera
• Lineage: Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
• CAZyme ID: CDH57732.1
• CAZy Family: PL14
• CAZyme Description: 3d domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
528	CBTN010000049|CGC1	58539.76	6.5601

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=CBTN010000049:52055-53830(+)

Full Sequence      

MYYPKSFIATALVALQFTTGSSAFFFRNNLEIVHGGANIQPEHAASYYSVFAREDDPEPE
FELVPMSVKDKIVSLKRRAIAGCEEEYTGTPFILTISNAISMILITIMPLIVKRGDTCHE
ITHKFGIHLEDFYYWNPQVNSRCKNLKPGRKYCVKNSDAGADPDSCNVRHKVVAGDTCTS
VAKQYGISHSKFIALNDNITSGCKNLKIGHSYCISTNRESSSNNGDSAAKKKAAEKAAVY
EKNDAKEDAKKQEEAEKAAEAKKKAVEAEAAEKKKQEEAEKAAADKKDDSDKIKENVSHL
ASKTKGDKKDDDNDDDDWEKTEVPTKDSDKDDDDNKNSGSSSSSTEKRKAIHHNIPMTYY
WIAMPEDYKQSGKQVSIKTCDGKTLGRTSVEYADALVMEGTGILGDKVVNLGACSCTNYN
CFMEVDKKEDPYGLTSYSTALRPFITAAANDIPRGSKVYVPQLDGVMLPTKKKHNGCLLV
DDKGWSFSSRHLDFYVYAMKNYETLNSQLGISKVDVYEGGSCKLLDYM

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
270619	3D_domain	3.56e-08	425	496	18	85	3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts. This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation.
197609	LysM	6.41e-08	170	214	2	44	Lysin motif.
212030	LysM	9.07e-08	111	154	4	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
212030	LysM	1.34e-07	168	214	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
396179	LysM	7.77e-06	170	209	1	37	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS10896.1|CBM50	5.81e-276	3	528	2	499
CDS12256.1|CBM50	9.17e-109	8	528	7	415
CDS04122.1|CBM50	4.13e-101	8	528	7	438
UCK58478.1|CBM50	3.01e-13	112	214	189	296
QYT04780.1|CBM50	1.09e-12	111	214	207	333

PDB Hits     

CDH57732.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4ALG0|LYSM1_ARTBC	1.50e-10	111	215	248	372	LysM domain-containing protein ARB_05157 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05157 PE=1 SV=1
sp|D4AVW3|LYSM5_ARTBC	9.50e-06	112	154	268	310	LysM domain-containing protein ARB_00327 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00327 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000270	0.999733	CS pos: 23-24. Pr: 0.9571

TMHMM  Annotations     

There is no transmembrane helices in CDH57732.1.