CAZyme Information: EAW17115.1

Basic Information

• Species: Aspergillus fischeri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
• CAZyme ID: EAW17115.1
• CAZy Family: PL3
• CAZyme Description: transglycosylase SLT domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
249	DS027697|CGC5	26020.67	4.1770

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

Full Sequence      

MAVLKSITLTSLALAIGATAQSANPGVGKNPKAQGATENVTPSTGPNGSEDWLNTGITTT
GWNPPFLSIDDVYTISLQDFYNGIGSACAQYDSYFQSSASKYGVNPVVLAVIAMQESSCN
ANAGGPTPGLMQVSCDNYPNGQCTDSIQDNVDAGTHYLKSQLDASGGNAIKALGSYNGWF
AAGSGLNGNRGLTKDYPCSAEGKAHGMPQNLDYLHQVLNGWMMGLDVYGEDNWIGTYHCD
QSCSDGSLC

Enzyme Prediction     

No EC number prediction in EAW17115.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396169	SLT	7.68e-11	95	178	1	94	Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.
223812	MltE	1.09e-08	90	219	138	278	Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM/invasin domains) [Cell wall/membrane/envelope biogenesis].
381604	Slt70-like	4.85e-08	91	185	6	109	70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.
381594	LT-like	1.37e-07	108	201	4	98	lytic transglycosylase(LT)-like domain. Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.
381617	LT_Slt70-like	1.62e-07	91	203	4	123	uncharacterized lytic transglycosylase subfamily with similarity to Slt70. Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX59202.1|GH23	QKX59202.1|GH23	1.49e-104	1	222	1	222
QYS93728.1|GH23	QYS93728.1|GH23	1.17e-96	30	249	25	252
UKZ72266.1|GH23	UKZ72266.1|GH23	3.87e-95	30	249	25	252
UPK92213.1|GH23	UPK92213.1|GH23	1.69e-93	30	249	24	250
UNI24763.1|GH23	UNI24763.1|GH23	1.55e-89	6	249	5	251

PDB Hits     

EAW17115.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O31976|YOMI_BACSU	sp|O31976|YOMI_BACSU	1.80e-10	85	177	1416	1512	SPbeta prophage-derived uncharacterized transglycosylase YomI OS=Bacillus subtilis (strain 168) OX=224308 GN=yomI PE=3 SV=2
sp|O64046|TMP_BPSPB	sp|O64046|TMP_BPSPB	1.80e-10	85	177	1416	1512	Probable tape measure protein OS=Bacillus phage SPbeta OX=66797 GN=yomI PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000321	0.999644	CS pos: 20-21. Pr: 0.9860

TMHMM  Annotations     

There is no transmembrane helices in EAW17115.1.